swissparser 0.5.1

This diff represents the content of publicly available package versions that have been released to one of the supported registries. The information contained in this diff is provided for informational purposes only and reflects changes between package versions as they appear in their respective public registries.
Files changed (12) hide show
  1. data/History.txt +8 -0
  2. data/LICENSE +675 -0
  3. data/README.txt +32 -0
  4. data/Rakefile +23 -0
  5. data/examples/data/EColPositives_noTAT.bas +520 -0
  6. data/examples/data/kegg_enzyme_short.txt +881 -0
  7. data/examples/data/uniprot.txt +2855 -0
  8. data/examples/kegg_demo.rb +103 -0
  9. data/examples/signal_demo.rb +100 -0
  10. data/examples/uniprot_demo.rb +83 -0
  11. data/lib/swiss_parser.rb +214 -0
  12. metadata +76 -0
data/examples/data/uniprot.txt ADDED
@@ -0,0 +1,2855 @@
1
+ ID PPBT_HUMAN Reviewed; 524 AA.
2
+ AC P05186; A1A4E7; B2RMP8; O75090; Q2TAI7; Q59EJ7; Q5BKZ5; Q5VTG5;
3
+ AC Q6NZI8; Q8WU32; Q9UBK0;
4
+ DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
5
+ DT 21-JUN-2005, sequence version 4.
6
+ DT 28-JUL-2009, entry version 125.
7
+ DE RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme;
8
+ DE EC=3.1.3.1;
9
+ DE AltName: Full=AP-TNAP;
10
+ DE AltName: Full=TNSALP;
11
+ DE AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme;
12
+ DE Flags: Precursor;
13
+ GN Name=ALPL;
14
+ OS Homo sapiens (Human).
15
+ OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
16
+ OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
17
+ OC Catarrhini; Hominidae; Homo.
18
+ OX NCBI_TaxID=9606;
19
+ RN [1]
20
+ RP NUCLEOTIDE SEQUENCE [MRNA].
21
+ RC TISSUE=Osteosarcoma;
22
+ RX MEDLINE=87016911; PubMed=3532105; DOI=10.1073/pnas.83.19.7182;
23
+ RA Weiss M.J., Henthorn P.S., Lafferty M.A., Slaughter C., Raducha M.,
24
+ RA Harris H.;
25
+ RT "Isolation and characterization of a cDNA encoding a human
26
+ RT liver/bone/kidney-type alkaline phosphatase.";
27
+ RL Proc. Natl. Acad. Sci. U.S.A. 83:7182-7186(1986).
28
+ RN [2]
29
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
30
+ RC TISSUE=Osteosarcoma;
31
+ RX MEDLINE=88298884; PubMed=3165380;
32
+ RA Weiss M.J., Ray K., Henthorn P.S., Lamb B., Kadesch T., Harris H.;
33
+ RT "Structure of the human liver/bone/kidney alkaline phosphatase gene.";
34
+ RL J. Biol. Chem. 263:12002-12010(1988).
35
+ RN [3]
36
+ RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-263.
37
+ RC TISSUE=Liver;
38
+ RX MEDLINE=89183624; PubMed=2928120; DOI=10.1093/nar/17.5.2129;
39
+ RA Kishi F., Matsuura S., Kajii T.;
40
+ RT "Nucleotide sequence of the human liver-type alkaline phosphatase
41
+ RT cDNA.";
42
+ RL Nucleic Acids Res. 17:2129-2129(1989).
43
+ RN [4]
44
+ RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HYPOPHOSPHATASIA PHE-289.
45
+ RX MEDLINE=98419164; PubMed=9747027; DOI=10.1007/s100380050061;
46
+ RA Sugimoto N., Iwamoto S., Hoshino Y., Kajii E.;
47
+ RT "A novel missense mutation of the tissue-nonspecific alkaline
48
+ RT phosphatase gene detected in a patient with hypophosphatasia.";
49
+ RL J. Hum. Genet. 43:160-164(1998).
50
+ RN [5]
51
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-152.
52
+ RC TISSUE=Brain;
53
+ RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
54
+ RA Ohara O., Nagase T., Kikuno R.F.;
55
+ RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
56
+ RN [6]
57
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
58
+ RX PubMed=16710414; DOI=10.1038/nature04727;
59
+ RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
60
+ RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
61
+ RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
62
+ RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
63
+ RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
64
+ RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
65
+ RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
66
+ RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
67
+ RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
68
+ RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
69
+ RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
70
+ RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
71
+ RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
72
+ RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
73
+ RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
74
+ RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
75
+ RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
76
+ RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
77
+ RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
78
+ RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
79
+ RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
80
+ RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
81
+ RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
82
+ RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
83
+ RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
84
+ RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
85
+ RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
86
+ RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
87
+ RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
88
+ RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
89
+ RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
90
+ RA Beck S., Rogers J., Bentley D.R.;
91
+ RT "The DNA sequence and biological annotation of human chromosome 1.";
92
+ RL Nature 441:315-321(2006).
93
+ RN [7]
94
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-263.
95
+ RC TISSUE=Brain, Cerebellum, Lymphoma, and Peripheral nerve;
96
+ RX PubMed=15489334; DOI=10.1101/gr.2596504;
97
+ RG The MGC Project Team;
98
+ RT "The status, quality, and expansion of the NIH full-length cDNA
99
+ RT project: the Mammalian Gene Collection (MGC).";
100
+ RL Genome Res. 14:2121-2127(2004).
101
+ RN [8]
102
+ RP PROTEIN SEQUENCE OF 18-49.
103
+ RC TISSUE=Liver;
104
+ RX MEDLINE=86157574; PubMed=3954357; DOI=10.1016/0003-9861(86)90223-7;
105
+ RA Garattini E., Hua J.-C., Pan Y.C.E., Udenfriend S.;
106
+ RT "Human liver alkaline phosphatase, purification and partial
107
+ RT sequencing: homology with the placental isozyme.";
108
+ RL Arch. Biochem. Biophys. 245:331-337(1986).
109
+ RN [9]
110
+ RP PROTEIN SEQUENCE OF 18-32, AND GLYCOSYLATION.
111
+ RX PubMed=1458595;
112
+ RA Nishihara Y., Hayashi Y., Adachi T., Koyama I., Stigbrand T.,
113
+ RA Hirano K.;
114
+ RT "Chemical nature of intestinal-type alkaline phosphatase in human
115
+ RT kidney.";
116
+ RL Clin. Chem. 38:2539-2542(1992).
117
+ RN [10]
118
+ RP GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
119
+ RX PubMed=14517339; DOI=10.1074/mcp.M300079-MCP200;
120
+ RA Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,
121
+ RA Jensen O.N.;
122
+ RT "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane
123
+ RT proteins.";
124
+ RL Mol. Cell. Proteomics 2:1261-1270(2003).
125
+ RN [11]
126
+ RP GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
127
+ RX PubMed=16602701; DOI=10.1021/pr050419u;
128
+ RA Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
129
+ RA Brodbeck U., Peck S.C., Jensen O.N.;
130
+ RT "Modification-specific proteomics of plasma membrane proteins:
131
+ RT identification and characterization of glycosylphosphatidylinositol-
132
+ RT anchored proteins released upon phospholipase D treatment.";
133
+ RL J. Proteome Res. 5:935-943(2006).
134
+ RN [12]
135
+ RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-430, AND MASS
136
+ RP SPECTROMETRY.
137
+ RC TISSUE=Liver;
138
+ RX PubMed=19159218; DOI=10.1021/pr8008012;
139
+ RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
140
+ RT "Glycoproteomics analysis of human liver tissue by combination of
141
+ RT multiple enzyme digestion and hydrazide chemistry.";
142
+ RL J. Proteome Res. 8:651-661(2009).
143
+ RN [13]
144
+ RP VARIANT HYPOPHOSPHATASIA THR-179.
145
+ RX MEDLINE=89017258; PubMed=3174660; DOI=10.1073/pnas.85.20.7666;
146
+ RA Weiss M.J., Cole D.E.C., Ray K., Whyte M.P., Lafferty M.A.,
147
+ RA Mulivor R.A., Harris H.;
148
+ RT "A missense mutation in the human liver/bone/kidney alkaline
149
+ RT phosphatase gene causing a lethal form of hypophosphatasia.";
150
+ RL Proc. Natl. Acad. Sci. U.S.A. 85:7666-7669(1988).
151
+ RN [14]
152
+ RP VARIANTS HYPOPHOSPHATASIA VAL-33; CYS-71; PRO-71; LYS-191; PRO-207;
153
+ RP ALA-294; VAL-378 AND HIS-436, AND VARIANT HIS-263.
154
+ RX MEDLINE=93028575; PubMed=1409720; DOI=10.1073/pnas.89.20.9924;
155
+ RA Henthorn P.S., Raducha M., Fedde K.N., Lafferty M.A., Whyte M.P.;
156
+ RT "Different missense mutations at the tissue-nonspecific alkaline
157
+ RT phosphatase gene locus in autosomal recessively inherited forms of
158
+ RT mild and severe hypophosphatasia.";
159
+ RL Proc. Natl. Acad. Sci. U.S.A. 89:9924-9928(1992).
160
+ RN [15]
161
+ RP VARIANT HYPOPHOSPHATASIA ASP-334.
162
+ RX MEDLINE=94010889; PubMed=8406453; DOI=10.1006/geno.1993.1305;
163
+ RA Greenberg C.R., Taylor C.L., Haworth J.C., Seargeant L.E.,
164
+ RA Philipps S., Triggs-Raine B., Chodirker B.N.;
165
+ RT "A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal
166
+ RT (lethal) form of hypophosphatasia in Canadian mennonites.";
167
+ RL Genomics 17:215-217(1993).
168
+ RN [16]
169
+ RP VARIANT HYPOPHOSPHATASIA LYS-298.
170
+ RX PubMed=7833929; DOI=10.1093/hmg/3.9.1683;
171
+ RA Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T.,
172
+ RA Shimada T.;
173
+ RT "Novel missense and frameshift mutations in the tissue-nonspecific
174
+ RT alkaline phosphatase gene in a Japanese patient with
175
+ RT hypophosphatasia.";
176
+ RL Hum. Mol. Genet. 3:1683-1684(1994).
177
+ RN [17]
178
+ RP VARIANTS HYPOPHOSPHATASIA LEU-327 AND ARG-456.
179
+ RX MEDLINE=97112379; PubMed=8954059; DOI=10.1210/jc.81.12.4458;
180
+ RA Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G.,
181
+ RA Satomura K., Yasui N., Okada S., Nakayama M.;
182
+ RT "Identification of novel missense mutations (Phe310Leu and Gly439Arg)
183
+ RT in a neonatal case of hypophosphatasia.";
184
+ RL J. Clin. Endocrinol. Metab. 81:4458-4461(1996).
185
+ RN [18]
186
+ RP VARIANTS HYPOPHOSPHATASIA PHE-17; VAL-40; SER-75; ARG-120; ARG-129;
187
+ RP ASP-170; TRP-184; LYS-191; TRP-223; LYS-291; ASP-334; PRO-445;
188
+ RP CYS-450; SER-473 AND ARG-491, AND VARIANT HIS-263.
189
+ RX PubMed=9781036; DOI=10.1038/sj.ejhg.5200190;
190
+ RA Mornet E., Taillandier A., Peyramaure S., Kaper F., Muller F.,
191
+ RA Brenner R., Bussiere P., Freisinger P., Godard J., Le Merrer M.,
192
+ RA Oury J.F., Plauchu H., Puddu R., Rival J.M., Superti-Furga A.,
193
+ RA Touraine R.L., Serre J.L., Simon-Bouy B.;
194
+ RT "Identification of fifteen novel mutations in the tissue-nonspecific
195
+ RT alkaline phosphatase (TNSALP) gene in European patients with severe
196
+ RT hypophosphatasia.";
197
+ RL Eur. J. Hum. Genet. 6:308-314(1998).
198
+ RN [19]
199
+ RP VARIANTS HYPOPHOSPHATASIA THR-111; THR-177; GLY-191; LEU-327 AND
200
+ RP ILE-382.
201
+ RX MEDLINE=98112484; PubMed=9452105;
202
+ RA Goseki-Sone M., Orimo H., Iimura T., Takagi Y., Watanabe H.,
203
+ RA Taketa K., Sato S., Mayanagi H., Shimada T., Oida S.;
204
+ RT "Hypophosphatasia: identification of five novel missense mutations
205
+ RT (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific
206
+ RT alkaline phosphatase gene among Japanese patients.";
207
+ RL Hum. Mutat. Suppl. 1:S263-S267(1998).
208
+ RN [20]
209
+ RP VARIANTS HYPOPHOSPHATASIA VAL-40; LEU-62; SER-75; THR-111; ARG-120;
210
+ RP ARG-129; HIS-136; VAL-162; ASP-170; TYR-171; TRP-184; LYS-191;
211
+ RP TRP-223; VAL-249; LYS-291; VAL-306; ASP-334; CYS-391; PRO-445;
212
+ RP CYS-450; SER-473; LYS-476 AND ARG-491, 3D-STRUCTURE MODELING, AND
213
+ RP CHARACTERIZATION OF VARIANTS.
214
+ RX MEDLINE=99265919; PubMed=10332035; DOI=10.1093/hmg/8.6.1039;
215
+ RA Zurutuza L., Muller F., Gibrat J.F., Taillandier A., Simon-Bouy B.,
216
+ RA Serre J.L., Mornet E.;
217
+ RT "Correlations of genotype and phenotype in hypophosphatasia.";
218
+ RL Hum. Mol. Genet. 8:1039-1046(1999).
219
+ RN [21]
220
+ RP VARIANTS HYPOPHOSPHATASIA LEU-62; HIS-136; VAL-162; TYR-171; LYS-191;
221
+ RP TYR-201; VAL-249; VAL-306 AND LYS-476.
222
+ RX MEDLINE=99140268; PubMed=10094560;
223
+ RX DOI=10.1002/(SICI)1098-1004(1999)13:2<171::AID-HUMU16>3.0.CO;2-T;
224
+ RA Taillandier A., Zurutuza L., Muller F., Simon-Bouy B., Serre J.L.,
225
+ RA Bird L., Brenner R., Boute O., Cousin J., Gaillard D., Heidemann P.H.,
226
+ RA Steinmann B., Wallot M., Mornet E.;
227
+ RT "Characterization of eleven novel mutations (M45L, R119H, 544delG,
228
+ RT G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the
229
+ RT tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with
230
+ RT severe hypophosphatasia.";
231
+ RL Hum. Mutat. 13:171-172(1999).
232
+ RN [22]
233
+ RP VARIANTS HYPOPHOSPHATASIA GLU-224 AND CYS-426.
234
+ RX MEDLINE=20292359; PubMed=10834525; DOI=10.1007/s004310051290;
235
+ RA Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N.,
236
+ RA Yamaguchi S., Ozono K.;
237
+ RT "Severe hypercalcaemia and respiratory insufficiency associated with
238
+ RT infantile hypophosphatasia caused by two novel mutations of the
239
+ RT tissue-nonspecific alkaline phosphatase gene.";
240
+ RL Eur. J. Pediatr. 159:375-379(2000).
241
+ RN [23]
242
+ RP VARIANTS HYPOPHOSPHATASIA VAL-40; THR-111; ASN-134; THR-176; LYS-191;
243
+ RP TYR-201; SER-246; THR-348; ARG-381; GLY-406; HIS-450; ILE-478 AND
244
+ RP SER-489.
245
+ RX MEDLINE=20146218; PubMed=10679946;
246
+ RX DOI=10.1002/(SICI)1098-1004(200003)15:3<293::AID-HUMU11>3.0.CO;2-Q;
247
+ RA Taillandier A., Cozien E., Muller F., Merrien Y., Bonnin E.,
248
+ RA Fribourg C., Simon-Bouy B., Serre J.L., Bieth E., Brenner R.,
249
+ RA Cordier M.P., De Bie S., Fellmann F., Freisinger P., Hesse V.,
250
+ RA Hennekam R.C.M., Josifova D., Kerzin-Storrar L., Leporrier N.,
251
+ RA Zabot M.-T., Mornet E.;
252
+ RT "Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S,
253
+ RT 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S)
254
+ RT in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in
255
+ RT patients with hypophosphatasia.";
256
+ RL Hum. Mutat. 15:293-293(2000).
257
+ RN [24]
258
+ RP VARIANT HYPOPHOSPHATASIA VAL-378, AND VARIANT ALA-522.
259
+ RX MEDLINE=20152744; PubMed=10690885; DOI=10.1210/jc.85.2.743;
260
+ RA Mueller H.L., Yamazaki M., Michigami T., Kageyama T., Schoenau E.,
261
+ RA Schneider P., Ozono K.;
262
+ RT "Asp361Val mutant of alkaline phosphatase found in patients with
263
+ RT dominantly inherited hypophosphatasia inhibits the activity of the
264
+ RT wild-type enzyme.";
265
+ RL J. Clin. Endocrinol. Metab. 85:743-747(2000).
266
+ RN [25]
267
+ RP VARIANT HYPOPHOSPHATASIA SER-417.
268
+ RX PubMed=11745997; DOI=10.1002/ajmg.1541.abs;
269
+ RA Sergi C., Mornet E., Troeger J., Voigtlaender T.;
270
+ RT "Perinatal hypophosphatasia: radiology, pathology and molecular
271
+ RT biology studies in a family harboring a splicing mutation (648+1A) and
272
+ RT a novel missense mutation (N400S) in the tissue-nonspecific alkaline
273
+ RT phosphatase (TNSALP) gene.";
274
+ RL Am. J. Med. Genet. 103:235-240(2001).
275
+ RN [26]
276
+ RP CHARACTERIZATION OF VARIANTS HYPOPHOSPHATASIA VAL-40; VAL-63; THR-116;
277
+ RP LEU-181; TRP-184; TRP-223; VAL-249; VAL-378; ILE-478 AND PHE-490.
278
+ RX MEDLINE=21372078; PubMed=11479741; DOI=10.1007/s004390100546;
279
+ RA Lia-Baldini A.S., Muller F., Taillandier A., Gibrat J.F., Mouchard M.,
280
+ RA Robin B., Simon-Bouy B., Serre J.L., Aylsworth A.S., Bieth E.,
281
+ RA Delanote S., Freisinger P., Hu J.C.-C., Krohn H.-P., Nunes M.E.,
282
+ RA Mornet E.;
283
+ RT "A molecular approach to dominance in hypophosphatasia.";
284
+ RL Hum. Genet. 109:99-108(2001).
285
+ RN [27]
286
+ RP VARIANTS HYPOPHOSPHATASIA CYS-28; VAL-40; VAL-51; HIS-71; THR-116;
287
+ RP HIS-136; HIS-152; THR-176; THR-179; LYS-191; ASP-211; VAL-220;
288
+ RP GLY-235; TYR-294; GLY-327; SER-399; ALA-423 AND MET-459.
289
+ RX MEDLINE=21331694; PubMed=11438998; DOI=10.1002/humu.1154;
290
+ RA Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F.,
291
+ RA Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M.,
292
+ RA Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L.,
293
+ RA Malou E., Sillence D., Temple I.K., Viot G., Mornet E.;
294
+ RT "Twelve novel mutations in the tissue-nonspecific alkaline phosphatase
295
+ RT gene (ALPL) in patients with various forms of hypophosphatasia.";
296
+ RL Hum. Mutat. 18:83-84(2001).
297
+ RN [28]
298
+ RP VARIANTS HYPOPHOSPHATASIA MET-68; SER-71; THR-177; TRP-223; PRO-275
299
+ RP AND HIS-391, CHARACTERIZATION OF VARIANTS HYPOPHOSPHATASIA MET-68;
300
+ RP SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, VARIANT ALA-522, AND
301
+ RP CHARACTERIZATION OF VARIANT ALA-522.
302
+ RX PubMed=11760847; DOI=10.1359/jbmr.2001.16.12.2313;
303
+ RA Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.;
304
+ RT "Mutational analysis and functional correlation with phenotype in
305
+ RT German patients with childhood-type hypophosphatasia.";
306
+ RL J. Bone Miner. Res. 16:2313-2319(2001).
307
+ RN [29]
308
+ RP VARIANT HYPOPHOSPHATASIA VAL-132.
309
+ RX MEDLINE=21821416; PubMed=11834095;
310
+ RX DOI=10.1034/j.1601-0825.2001.00740.x;
311
+ RA Watanabe H., Hashimoto-Uoshima M., Goseki-Sone M., Orimo H.,
312
+ RA Ishikawa I.;
313
+ RT "A novel point mutation (C571T) in the tissue-non-specific alkaline
314
+ RT phosphatase gene in a case of adult-type hypophosphatasia.";
315
+ RL Oral Dis. 7:331-335(2001).
316
+ RN [30]
317
+ RP VARIANTS HYPOPHOSPHATASIA LYS-291 AND ARG-326.
318
+ RX MEDLINE=21994639; PubMed=11999978; DOI=10.1023/A:1015121414782;
319
+ RA Litmanovitz I., Reish O., Dolfin T., Arnon S., Regev R., Grinshpan G.,
320
+ RA Yamazaki M., Ozono K.;
321
+ RT "Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline
322
+ RT phosphatase gene in neonatal hypophosphatasia associated with
323
+ RT convulsions.";
324
+ RL J. Inherit. Metab. Dis. 25:35-40(2002).
325
+ RN [31]
326
+ RP VARIANTS HYPOPHOSPHATASIA SER-51; HIS-71; THR-111; MET-128; HIS-134;
327
+ RP HIS-136; THR-176; LYS-191; GLN-223; TRP-223; SER-246; ALA-294;
328
+ RP PRO-299; PHE-327 DEL; ARG-339; THR-348; VAL-378; MET-414; ASP-426 AND
329
+ RP LYS-476, AND VARIANTS HIS-263 AND ALA-522.
330
+ RX PubMed=11855933; DOI=10.1006/mgme.2001.3283;
331
+ RA Mumm S., Jones J., Finnegan P., Henthorn P.S., Podgornik M.N.,
332
+ RA Whyte M.P.;
333
+ RT "Denaturing gradient gel electrophoresis analysis of the tissue
334
+ RT nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia.";
335
+ RL Mol. Genet. Metab. 75:143-153(2002).
336
+ RN [32]
337
+ RP VARIANTS HYPOPHOSPHATASIA VAL-62; ARG-63; THR-111; ILE-148; SER-162;
338
+ RP GLU-189; ALA-220; LEU-272; GLY-293-294-ASP DEL; LYS-311; LYS-452 AND
339
+ RP THR-468.
340
+ RX PubMed=12815606; DOI=10.1002/humu.9159;
341
+ RA Spentchian M., Merrien Y., Herasse M., Dobbie Z., Glaeser D.,
342
+ RA Holder S.E., Ivarsson S.-A., Kostiner D., Mansour S., Norman A.,
343
+ RA Roth J., Stipoljev F., Taillemite J.-L., van der Smagt J.J.,
344
+ RA Serre J.-L., Simon-Bouy B., Taillandier A., Mornet E.;
345
+ RT "Severe hypophosphatasia: characterization of fifteen novel mutations
346
+ RT in the ALPL gene.";
347
+ RL Hum. Mutat. 22:105-106(2003).
348
+ RN [33]
349
+ RP VARIANTS HYPOPHOSPHATASIA LEU-108; THR-116 AND MET-414, AND
350
+ RP CHARACTERIZATION OF VARIANT HYPOPHOSPHATASIA LEU-108.
351
+ RX PubMed=12920074; DOI=10.1136/jmg.40.8.605;
352
+ RA Herasse M., Spentchian M., Taillandier A., Keppler-Noreuil K.,
353
+ RA Fliorito A.N.M., Bergoffen J., Wallerstein R., Muti C., Simon-Bouy B.,
354
+ RA Mornet E.;
355
+ RT "Molecular study of three cases of odontohypophosphatasia resulting
356
+ RT from heterozygosity for mutations in the tissue non-specific alkaline
357
+ RT phosphatase gene.";
358
+ RL J. Med. Genet. 40:605-609(2003).
359
+ RN [34]
360
+ RP VARIANT HYPOPHOSPHATASIA GLY-114.
361
+ RX PubMed=15135428; DOI=10.1016/j.arcped.2004.02.018;
362
+ RA Draguet C., Gillerot Y., Mornet E.;
363
+ RT "Childhood hypophosphatasia: a case report due to a novel mutation.";
364
+ RL Arch. Pediatr. 11:440-443(2004).
365
+ RN [35]
366
+ RP VARIANTS HYPOPHOSPHATASIA VAL-33; HIS-136; GLN-223; TRP-223; HIS-272;
367
+ RP THR-292; ALA-294; THR-295; ASP-297; ASP-334 AND ALA-411, AND
368
+ RP CHARACTERIZATION OF VARIANTS HYPOPHOSPHATASIA VAL-33; HIS-272;
369
+ RP THR-292; THR-295; ASP-297 AND ALA-411.
370
+ RX PubMed=15694177; DOI=10.1016/j.ymgme.2004.11.003;
371
+ RA Brun-Heath I., Taillandier A., Serre J.-L., Mornet E.;
372
+ RT "Characterization of 11 novel mutations in the tissue non-specific
373
+ RT alkaline phosphatase gene responsible for hypophosphatasia and
374
+ RT genotype-phenotype correlations.";
375
+ RL Mol. Genet. Metab. 84:273-277(2005).
376
+ CC -!- FUNCTION: This isozyme may play a role in skeletal mineralization.
377
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
378
+ CC phosphate.
379
+ CC -!- COFACTOR: Binds 1 magnesium ion (By similarity).
380
+ CC -!- COFACTOR: Binds 2 zinc ions (By similarity).
381
+ CC -!- SUBUNIT: Homodimer.
382
+ CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
383
+ CC -!- PTM: Glycosylated.
384
+ CC -!- DISEASE: Defects in ALPL are a cause of hypophosphatasia infantile
385
+ CC (hypophosphatasia) [MIM:241500]; an inherited metabolic bone
386
+ CC disease characterized by defective skeletal mineralization. Four
387
+ CC hypophosphatasia forms are distinguished, depending on the age of
388
+ CC onset: perinatal, infantile, childhood and adult type. The
389
+ CC perinatal form is the most severe and is almost always fatal.
390
+ CC Patients with only premature loss of deciduous teeth, but with no
391
+ CC bone disease are regarded as having odontohypophosphatasia
392
+ CC (odonto).
393
+ CC -!- DISEASE: Defects in ALPL are a cause of hypophosphatasia childhood
394
+ CC (hypophosphatasia) [MIM:241510].
395
+ CC -!- DISEASE: Defects in ALPL are a cause of hypophosphatasia adult
396
+ CC type (hypophosphatasia) [MIM:146300].
397
+ CC -!- MISCELLANEOUS: In most mammals there are four different isozymes:
398
+ CC placental, placental-like, intestinal and tissue non-specific
399
+ CC (liver/bone/kidney).
400
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
401
+ CC -!- WEB RESOURCE: Name=ALPL; Note=Tissue nonspecific alkaline
402
+ CC phosphatase gene mutations database;
403
+ CC URL="http://www.sesep.uvsq.fr/Database.html";
404
+ CC -!- WEB RESOURCE: Name=GeneReviews;
405
+ CC URL="http://www.genetests.org/query?gene=ALPL";
406
+ CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
407
+ CC URL="http://en.wikipedia.org/wiki/Alkaline_phosphatase";
408
+ CC -----------------------------------------------------------------------
409
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
410
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
411
+ CC -----------------------------------------------------------------------
412
+ DR EMBL; M24439; AAB59378.1; -; Genomic_DNA.
413
+ DR EMBL; M24429; AAB59378.1; JOINED; Genomic_DNA.
414
+ DR EMBL; M24430; AAB59378.1; JOINED; Genomic_DNA.
415
+ DR EMBL; M24431; AAB59378.1; JOINED; Genomic_DNA.
416
+ DR EMBL; M24432; AAB59378.1; JOINED; Genomic_DNA.
417
+ DR EMBL; M24433; AAB59378.1; JOINED; Genomic_DNA.
418
+ DR EMBL; M24434; AAB59378.1; JOINED; Genomic_DNA.
419
+ DR EMBL; M24435; AAB59378.1; JOINED; Genomic_DNA.
420
+ DR EMBL; M24436; AAB59378.1; JOINED; Genomic_DNA.
421
+ DR EMBL; M24437; AAB59378.1; JOINED; Genomic_DNA.
422
+ DR EMBL; M24438; AAB59378.1; JOINED; Genomic_DNA.
423
+ DR EMBL; X14174; CAA32376.1; -; mRNA.
424
+ DR EMBL; AB011406; BAA32129.1; -; mRNA.
425
+ DR EMBL; AB209814; BAD93051.1; ALT_INIT; mRNA.
426
+ DR EMBL; AL592309; CAH72079.1; -; Genomic_DNA.
427
+ DR EMBL; AL359815; CAH72079.1; JOINED; Genomic_DNA.
428
+ DR EMBL; AL359815; CAI16259.1; -; Genomic_DNA.
429
+ DR EMBL; AL592309; CAI16259.1; JOINED; Genomic_DNA.
430
+ DR EMBL; BC021289; AAH21289.3; -; mRNA.
431
+ DR EMBL; BC066116; AAH66116.2; -; mRNA.
432
+ DR EMBL; BC090861; AAH90861.2; -; mRNA.
433
+ DR EMBL; BC110909; AAI10910.2; -; mRNA.
434
+ DR EMBL; BC126165; AAI26166.1; -; mRNA.
435
+ DR EMBL; BC136325; AAI36326.1; -; mRNA.
436
+ DR IPI; IPI00419916; -.
437
+ DR PIR; S03613; PAHUH.
438
+ DR RefSeq; NP_000469.3; -.
439
+ DR RefSeq; NP_001120973.1; -.
440
+ DR UniGene; Hs.75431; -.
441
+ DR HSSP; P05187; 1EW2.
442
+ DR IntAct; P05186; 1.
443
+ DR PhosphoSite; P05186; -.
444
+ DR PeptideAtlas; P05186; -.
445
+ DR PRIDE; P05186; -.
446
+ DR Ensembl; ENST00000374832; ENSP00000363965; ENSG00000162551; Homo sapiens.
447
+ DR Ensembl; ENST00000374840; ENSP00000363973; ENSG00000162551; Homo sapiens.
448
+ DR GeneID; 249; -.
449
+ DR KEGG; hsa:249; -.
450
+ DR NMPDR; fig|9606.3.peg.484; -.
451
+ DR UCSC; uc001bet.1; human.
452
+ DR GeneCards; GC01P021708; -.
453
+ DR H-InvDB; HIX0000225; -.
454
+ DR HGNC; HGNC:438; ALPL.
455
+ DR HPA; HPA007105; -.
456
+ DR HPA; HPA008765; -.
457
+ DR MIM; 146300; phenotype.
458
+ DR MIM; 171760; gene.
459
+ DR MIM; 241500; phenotype.
460
+ DR MIM; 241510; phenotype.
461
+ DR Orphanet; 436; Hypophosphatasia.
462
+ DR PharmGKB; PA24729; -.
463
+ DR HOVERGEN; P05186; -.
464
+ DR OMA; P05186; MISPFLV.
465
+ DR BRENDA; 3.1.3.1; 247.
466
+ DR DrugBank; DB01143; Amifostine.
467
+ DR NextBio; 997; -.
468
+ DR ArrayExpress; P05186; -.
469
+ DR Bgee; P05186; -.
470
+ DR GermOnline; ENSG00000162551; Homo sapiens.
471
+ DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
472
+ DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
473
+ DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
474
+ DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
475
+ DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:EC.
476
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
477
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
478
+ DR GO; GO:0008152; P:metabolic process; IEA:InterPro.
479
+ DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
480
+ DR GO; GO:0033280; P:response to vitamin D; IEP:UniProtKB.
481
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
482
+ DR InterPro; IPR001952; Alkaline_phosphatase.
483
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
484
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
485
+ DR Pfam; PF00245; Alk_phosphatase; 1.
486
+ DR PRINTS; PR00113; ALKPHPHTASE.
487
+ DR SMART; SM00098; alkPPc; 1.
488
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
489
+ PE 1: Evidence at protein level;
490
+ KW Biomineralization; Cell membrane; Complete proteome;
491
+ KW Direct protein sequencing; Disease mutation; Glycoprotein; GPI-anchor;
492
+ KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
493
+ KW Phosphoprotein; Polymorphism; Signal; Transmembrane; Zinc.
494
+ FT SIGNAL 1 17
495
+ FT CHAIN 18 502 Alkaline phosphatase, tissue-nonspecific
496
+ FT isozyme.
497
+ FT /FTId=PRO_0000024023.
498
+ FT PROPEP 503 524 Removed in mature form (Probable).
499
+ FT /FTId=PRO_0000024024.
500
+ FT ACT_SITE 110 110 Phosphoserine intermediate.
501
+ FT METAL 60 60 Magnesium (Potential).
502
+ FT METAL 60 60 Zinc 2 (Potential).
503
+ FT METAL 173 173 Magnesium (Potential).
504
+ FT METAL 332 332 Magnesium (Potential).
505
+ FT METAL 337 337 Zinc 1 (Potential).
506
+ FT METAL 341 341 Zinc 1 (Potential).
507
+ FT METAL 378 378 Zinc 2 (Potential).
508
+ FT METAL 379 379 Zinc 2 (Potential).
509
+ FT METAL 454 454 Zinc 1 (Potential).
510
+ FT LIPID 502 502 GPI-anchor amidated serine (Probable).
511
+ FT CARBOHYD 140 140 N-linked (GlcNAc...) (Potential).
512
+ FT CARBOHYD 230 230 N-linked (GlcNAc...) (Potential).
513
+ FT CARBOHYD 271 271 N-linked (GlcNAc...) (Potential).
514
+ FT CARBOHYD 303 303 N-linked (GlcNAc...) (Potential).
515
+ FT CARBOHYD 430 430 N-linked (GlcNAc...).
516
+ FT VARIANT 17 17 S -> F (in hypophosphatasia).
517
+ FT /FTId=VAR_025903.
518
+ FT VARIANT 28 28 Y -> C (in hypophosphatasia; infantile;
519
+ FT 7% of activity).
520
+ FT /FTId=VAR_013972.
521
+ FT VARIANT 33 33 A -> V (in hypophosphatasia; 7.2% of
522
+ FT wild-type activity).
523
+ FT /FTId=VAR_006147.
524
+ FT VARIANT 40 40 A -> V (in hypophosphatasia; 2% of
525
+ FT activity).
526
+ FT /FTId=VAR_011081.
527
+ FT VARIANT 51 51 A -> S (in hypophosphatasia).
528
+ FT /FTId=VAR_025904.
529
+ FT VARIANT 51 51 A -> V (in hypophosphatasia).
530
+ FT /FTId=VAR_013973.
531
+ FT VARIANT 62 62 M -> L (in hypophosphatasia; moderate;
532
+ FT 27% of activity).
533
+ FT /FTId=VAR_006148.
534
+ FT VARIANT 62 62 M -> V (in hypophosphatasia).
535
+ FT /FTId=VAR_025905.
536
+ FT VARIANT 63 63 G -> R (in hypophosphatasia).
537
+ FT /FTId=VAR_025906.
538
+ FT VARIANT 63 63 G -> V (in hypophosphatasia; loss of
539
+ FT activity).
540
+ FT /FTId=VAR_013974.
541
+ FT VARIANT 68 68 T -> M (in hypophosphatasia; childhood-
542
+ FT type; severe allele).
543
+ FT /FTId=VAR_025907.
544
+ FT VARIANT 71 71 R -> C (in hypophosphatasia).
545
+ FT /FTId=VAR_006149.
546
+ FT VARIANT 71 71 R -> H (in hypophosphatasia).
547
+ FT /FTId=VAR_013975.
548
+ FT VARIANT 71 71 R -> P (in hypophosphatasia).
549
+ FT /FTId=VAR_006150.
550
+ FT VARIANT 71 71 R -> S (in hypophosphatasia; childhood-
551
+ FT type; severe allele).
552
+ FT /FTId=VAR_025908.
553
+ FT VARIANT 75 75 G -> S (in hypophosphatasia; severe; 3.5%
554
+ FT of activity).
555
+ FT /FTId=VAR_013976.
556
+ FT VARIANT 76 76 Q -> R (in hypophosphatasia).
557
+ FT /FTId=VAR_025909.
558
+ FT VARIANT 108 108 P -> L (in hypophosphatasia; 0.4% of
559
+ FT wild-type activity; severe allele).
560
+ FT /FTId=VAR_025910.
561
+ FT VARIANT 111 111 A -> T (in hypophosphatasia; odonto).
562
+ FT /FTId=VAR_006151.
563
+ FT VARIANT 114 114 A -> G (in hypophosphatasia).
564
+ FT /FTId=VAR_025911.
565
+ FT VARIANT 116 116 A -> T (in hypophosphatasia; loss of
566
+ FT activity).
567
+ FT /FTId=VAR_013977.
568
+ FT VARIANT 120 120 G -> R (in hypophosphatasia).
569
+ FT /FTId=VAR_013978.
570
+ FT VARIANT 128 128 V -> M (in hypophosphatasia).
571
+ FT /FTId=VAR_025912.
572
+ FT VARIANT 129 129 G -> R (in hypophosphatasia).
573
+ FT /FTId=VAR_013979.
574
+ FT VARIANT 132 132 A -> V (in hypophosphatasia).
575
+ FT /FTId=VAR_013146.
576
+ FT VARIANT 134 134 T -> H (in hypophosphatasia; requires 2
577
+ FT nucleotide substitutions).
578
+ FT /FTId=VAR_025913.
579
+ FT VARIANT 134 134 T -> N (in hypophosphatasia; 9% of
580
+ FT activity).
581
+ FT /FTId=VAR_011082.
582
+ FT VARIANT 136 136 R -> H (in hypophosphatasia; moderate;
583
+ FT 33% of activity).
584
+ FT /FTId=VAR_006152.
585
+ FT VARIANT 148 148 T -> I (in hypophosphatasia).
586
+ FT /FTId=VAR_025914.
587
+ FT VARIANT 152 152 R -> H (in hypophosphatasia).
588
+ FT /FTId=VAR_013980.
589
+ FT VARIANT 162 162 G -> S (in hypophosphatasia).
590
+ FT /FTId=VAR_025915.
591
+ FT VARIANT 162 162 G -> V (in hypophosphatasia; severe; 1%
592
+ FT of activity).
593
+ FT /FTId=VAR_006153.
594
+ FT VARIANT 170 170 N -> D (in hypophosphatasia).
595
+ FT /FTId=VAR_013981.
596
+ FT VARIANT 171 171 H -> R (in hypophosphatasia).
597
+ FT /FTId=VAR_025916.
598
+ FT VARIANT 171 171 H -> Y (in hypophosphatasia; severe; 2%
599
+ FT of activity).
600
+ FT /FTId=VAR_006154.
601
+ FT VARIANT 176 176 A -> T (in hypophosphatasia).
602
+ FT /FTId=VAR_011083.
603
+ FT VARIANT 177 177 A -> T (in hypophosphatasia; adult type;
604
+ FT moderate allele).
605
+ FT /FTId=VAR_006155.
606
+ FT VARIANT 179 179 A -> T (in hypophosphatasia).
607
+ FT /FTId=VAR_006156.
608
+ FT VARIANT 181 181 S -> L (in hypophosphatasia; 1% OF
609
+ FT activity).
610
+ FT /FTId=VAR_013982.
611
+ FT VARIANT 184 184 R -> W (in hypophosphatasia; loss of
612
+ FT activity).
613
+ FT /FTId=VAR_013983.
614
+ FT VARIANT 189 189 D -> E (in hypophosphatasia).
615
+ FT /FTId=VAR_025917.
616
+ FT VARIANT 191 191 E -> G (in hypophosphatasia; odonto).
617
+ FT /FTId=VAR_006157.
618
+ FT VARIANT 191 191 E -> K (in hypophosphatasia; moderate;
619
+ FT frequent mutation in European countries).
620
+ FT /FTId=VAR_006158.
621
+ FT VARIANT 201 201 C -> Y (in hypophosphatasia).
622
+ FT /FTId=VAR_006159.
623
+ FT VARIANT 207 207 Q -> P (in hypophosphatasia).
624
+ FT /FTId=VAR_006160.
625
+ FT VARIANT 211 211 N -> D (in hypophosphatasia).
626
+ FT /FTId=VAR_013984.
627
+ FT VARIANT 212 212 I -> F (in hypophosphatasia).
628
+ FT /FTId=VAR_025918.
629
+ FT VARIANT 220 220 G -> A (in hypophosphatasia).
630
+ FT /FTId=VAR_025919.
631
+ FT VARIANT 220 220 G -> V (in hypophosphatasia; odonto).
632
+ FT /FTId=VAR_013985.
633
+ FT VARIANT 223 223 R -> Q (in hypophosphatasia).
634
+ FT /FTId=VAR_025920.
635
+ FT VARIANT 223 223 R -> W (in hypophosphatasia; 3% of
636
+ FT activity; severe allele).
637
+ FT /FTId=VAR_013986.
638
+ FT VARIANT 224 224 K -> E (in hypophosphatasia; infantile;
639
+ FT partial loss of activity).
640
+ FT /FTId=VAR_011084.
641
+ FT VARIANT 235 235 E -> G (in hypophosphatasia).
642
+ FT /FTId=VAR_013987.
643
+ FT VARIANT 246 246 R -> S (in hypophosphatasia; 4% of
644
+ FT activity).
645
+ FT /FTId=VAR_011085.
646
+ FT VARIANT 249 249 G -> V (in hypophosphatasia; partial loss
647
+ FT of activity).
648
+ FT /FTId=VAR_013988.
649
+ FT VARIANT 263 263 Y -> H (common polymorphism;
650
+ FT dbSNP:rs3200254).
651
+ FT /FTId=VAR_006161.
652
+ FT VARIANT 272 272 R -> H (in hypophosphatasia; 6.8% of
653
+ FT wild-type activity).
654
+ FT /FTId=VAR_025921.
655
+ FT VARIANT 272 272 R -> L (in hypophosphatasia).
656
+ FT /FTId=VAR_025922.
657
+ FT VARIANT 275 275 L -> P (in hypophosphatasia; childhood-
658
+ FT type; severe allele).
659
+ FT /FTId=VAR_025923.
660
+ FT VARIANT 289 289 L -> F (in hypophosphatasia).
661
+ FT /FTId=VAR_006162.
662
+ FT VARIANT 291 291 E -> K (in hypophosphatasia; moderate; 8%
663
+ FT of activity).
664
+ FT /FTId=VAR_013989.
665
+ FT VARIANT 292 292 P -> T (in hypophosphatasia; 4% of wild-
666
+ FT type activity).
667
+ FT /FTId=VAR_025924.
668
+ FT VARIANT 293 294 Missing (in hypophosphatasia).
669
+ FT /FTId=VAR_025925.
670
+ FT VARIANT 294 294 D -> A (in hypophosphatasia).
671
+ FT /FTId=VAR_006163.
672
+ FT VARIANT 294 294 D -> Y (in hypophosphatasia).
673
+ FT /FTId=VAR_013990.
674
+ FT VARIANT 295 295 M -> T (in hypophosphatasia; 8.5% of
675
+ FT wild-type activity).
676
+ FT /FTId=VAR_025926.
677
+ FT VARIANT 297 297 Y -> D (in hypophosphatasia; 1.3% of
678
+ FT wild-type activity).
679
+ FT /FTId=VAR_025927.
680
+ FT VARIANT 298 298 E -> K (in hypophosphatasia).
681
+ FT /FTId=VAR_025928.
682
+ FT VARIANT 299 299 L -> P (in hypophosphatasia).
683
+ FT /FTId=VAR_025929.
684
+ FT VARIANT 306 306 D -> V (in hypophosphatasia).
685
+ FT /FTId=VAR_006164.
686
+ FT VARIANT 311 311 E -> K (in hypophosphatasia).
687
+ FT /FTId=VAR_025930.
688
+ FT VARIANT 326 326 G -> R (in hypophosphatasia; in a patient
689
+ FT carrying also lys-291).
690
+ FT /FTId=VAR_013991.
691
+ FT VARIANT 327 327 F -> G (in hypophosphatasia; requires 2
692
+ FT nucleotide substitutions).
693
+ FT /FTId=VAR_013992.
694
+ FT VARIANT 327 327 F -> L (in hypophosphatasia; childhood).
695
+ FT /FTId=VAR_006165.
696
+ FT VARIANT 327 327 Missing (in hypophosphatasia).
697
+ FT /FTId=VAR_025931.
698
+ FT VARIANT 334 334 G -> D (in hypophosphatasia).
699
+ FT /FTId=VAR_006166.
700
+ FT VARIANT 339 339 G -> R (in hypophosphatasia).
701
+ FT /FTId=VAR_025932.
702
+ FT VARIANT 348 348 A -> T (in hypophosphatasia).
703
+ FT /FTId=VAR_011086.
704
+ FT VARIANT 354 354 E -> D (in hypophosphatasia).
705
+ FT /FTId=VAR_025933.
706
+ FT VARIANT 378 378 D -> V (in hypophosphatasia; loss of
707
+ FT activity).
708
+ FT /FTId=VAR_006167.
709
+ FT VARIANT 381 381 H -> R (in hypophosphatasia).
710
+ FT /FTId=VAR_011087.
711
+ FT VARIANT 382 382 V -> I (in hypophosphatasia).
712
+ FT /FTId=VAR_006168.
713
+ FT VARIANT 391 391 R -> C (in hypophosphatasia; moderate;
714
+ FT 10% of activity).
715
+ FT /FTId=VAR_013993.
716
+ FT VARIANT 391 391 R -> H (in hypophosphatasia; childhood-
717
+ FT type; severe allele).
718
+ FT /FTId=VAR_025934.
719
+ FT VARIANT 399 399 A -> S (in hypophosphatasia).
720
+ FT /FTId=VAR_013994.
721
+ FT VARIANT 406 406 D -> G (in hypophosphatasia; 15% of
722
+ FT activity).
723
+ FT /FTId=VAR_011088.
724
+ FT VARIANT 411 411 T -> A (in hypophosphatasia; absence of
725
+ FT residual enzymatic activity).
726
+ FT /FTId=VAR_025935.
727
+ FT VARIANT 414 414 L -> M (in hypophosphatasia).
728
+ FT /FTId=VAR_025936.
729
+ FT VARIANT 417 417 N -> S (in hypophosphatasia).
730
+ FT /FTId=VAR_025937.
731
+ FT VARIANT 423 423 V -> A (in hypophosphatasia; 16% of
732
+ FT activity).
733
+ FT /FTId=VAR_013995.
734
+ FT VARIANT 426 426 G -> C (in hypophosphatasia; infantile;
735
+ FT partial loss of activity).
736
+ FT /FTId=VAR_011089.
737
+ FT VARIANT 426 426 G -> D (in hypophosphatasia).
738
+ FT /FTId=VAR_025938.
739
+ FT VARIANT 436 436 Y -> H (in hypophosphatasia).
740
+ FT /FTId=VAR_006169.
741
+ FT VARIANT 445 445 S -> P (in hypophosphatasia; severe; 2%
742
+ FT of activity).
743
+ FT /FTId=VAR_013996.
744
+ FT VARIANT 450 450 R -> C (in hypophosphatasia; severe; 4%
745
+ FT of activity).
746
+ FT /FTId=VAR_013997.
747
+ FT VARIANT 450 450 R -> H (in hypophosphatasia).
748
+ FT /FTId=VAR_011090.
749
+ FT VARIANT 452 452 E -> K (in hypophosphatasia).
750
+ FT /FTId=VAR_025939.
751
+ FT VARIANT 456 456 G -> R (in hypophosphatasia; loss of
752
+ FT activity).
753
+ FT /FTId=VAR_011091.
754
+ FT VARIANT 459 459 V -> M (in hypophosphatasia; infantile).
755
+ FT /FTId=VAR_013998.
756
+ FT VARIANT 468 468 A -> T (in hypophosphatasia).
757
+ FT /FTId=VAR_025940.
758
+ FT VARIANT 473 473 G -> S (in hypophosphatasia).
759
+ FT /FTId=VAR_013999.
760
+ FT VARIANT 476 476 E -> K (in hypophosphatasia).
761
+ FT /FTId=VAR_006170.
762
+ FT VARIANT 478 478 N -> I (in hypophosphatasia; 9% of
763
+ FT activity).
764
+ FT /FTId=VAR_011092.
765
+ FT VARIANT 489 489 C -> S (in hypophosphatasia; 9% of
766
+ FT activity).
767
+ FT /FTId=VAR_011093.
768
+ FT VARIANT 490 490 I -> F (in hypophosphatasia; odonto;
769
+ FT partial loss of activity).
770
+ FT /FTId=VAR_014000.
771
+ FT VARIANT 491 491 G -> R (in hypophosphatasia).
772
+ FT /FTId=VAR_014001.
773
+ FT VARIANT 522 522 V -> A (in dbSNP:rs34605986).
774
+ FT /FTId=VAR_011094.
775
+ FT CONFLICT 29 29 W -> A (in Ref. 8; AA sequence).
776
+ FT CONFLICT 104 104 N -> K (in Ref. 3; CAA32376).
777
+ FT CONFLICT 361 361 Q -> H (in Ref. 1; BAA32129).
778
+ FT CONFLICT 446 446 A -> P (in Ref. 1; BAA32129).
779
+ SQ SEQUENCE 524 AA; 57305 MW; 71B45F17F6211900 CRC64;
780
+ MISPFLVLAI GTCLTNSLVP EKEKDPKYWR DQAQETLKYA LELQKLNTNV AKNVIMFLGD
781
+ GMGVSTVTAA RILKGQLHHN PGEETRLEMD KFPFVALSKT YNTNAQVPDS AGTATAYLCG
782
+ VKANEGTVGV SAATERSRCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSAAYAH
783
+ SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIRDIDVIMG GGRKYMYPKN KTDVEYESDE
784
+ KARGTRLDGL DLVDTWKSFK PRYKHSHFIW NRTELLTLDP HNVDYLLGLF EPGDMQYELN
785
+ RNNVTDPSLS EMVVVAIQIL RKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDRAIG
786
+ QAGSLTSSED TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MLSDTDKKPF TAILYGNGPG
787
+ YKVVGGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFSKGPMAHL LHGVHEQNYV
788
+ PHVMAYAACI GANLGHCAPA SSAGSLAAGP LLLALALYPL SVLF
789
+ //
790
+ ID PPB_ECOLI Reviewed; 471 AA.
791
+ AC P00634; P77801; P78051; Q2MC42; Q47041;
792
+ DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
793
+ DT 13-AUG-1987, sequence version 1.
794
+ DT 28-JUL-2009, entry version 117.
795
+ DE RecName: Full=Alkaline phosphatase;
796
+ DE Short=APase;
797
+ DE EC=3.1.3.1;
798
+ DE Flags: Precursor;
799
+ GN Name=phoA; OrderedLocusNames=b0383, JW0374;
800
+ OS Escherichia coli (strain K12).
801
+ OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
802
+ OC Enterobacteriaceae; Escherichia.
803
+ OX NCBI_TaxID=83333;
804
+ RN [1]
805
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
806
+ RC STRAIN=ATCC 35607 / JM83;
807
+ RX MEDLINE=87066741; PubMed=3537962; DOI=10.1093/nar/14.21.8689;
808
+ RA Shuttleworth H., Taylor J., Minton N.;
809
+ RT "Sequence of the gene for alkaline phosphatase from Escherichia coli
810
+ RT JM83.";
811
+ RL Nucleic Acids Res. 14:8689-8689(1986).
812
+ RN [2]
813
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
814
+ RX MEDLINE=87031576; PubMed=3533724; DOI=10.1016/0378-1119(86)90050-8;
815
+ RA Chang C.N., Kuang W.-J., Chen E.Y.;
816
+ RT "Nucleotide sequence of the alkaline phosphatase gene of Escherichia
817
+ RT coli.";
818
+ RL Gene 44:121-125(1986).
819
+ RN [3]
820
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
821
+ RX MEDLINE=88320572; PubMed=3045828; DOI=10.1073/pnas.85.18.7036;
822
+ RA Dubose R.F., Dykhuizen D.E., Hartl D.L.;
823
+ RT "Genetic exchange among natural isolates of bacteria: recombination
824
+ RT within the phoA gene of Escherichia coli.";
825
+ RL Proc. Natl. Acad. Sci. U.S.A. 85:7036-7040(1988).
826
+ RN [4]
827
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
828
+ RC STRAIN=K12 / MG1655 / ATCC 47076;
829
+ RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
830
+ RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
831
+ RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
832
+ RT "Sequence of minutes 4-25 of Escherichia coli.";
833
+ RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
834
+ RN [5]
835
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
836
+ RC STRAIN=K12 / MG1655 / ATCC 47076;
837
+ RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
838
+ RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
839
+ RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
840
+ RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
841
+ RA Mau B., Shao Y.;
842
+ RT "The complete genome sequence of Escherichia coli K-12.";
843
+ RL Science 277:1453-1474(1997).
844
+ RN [6]
845
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
846
+ RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
847
+ RX PubMed=16738553; DOI=10.1038/msb4100049;
848
+ RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
849
+ RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
850
+ RT "Highly accurate genome sequences of Escherichia coli K-12 strains
851
+ RT MG1655 and W3110.";
852
+ RL Mol. Syst. Biol. 2:E1-E5(2006).
853
+ RN [7]
854
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
855
+ RX MEDLINE=90264311; PubMed=2345142;
856
+ RA Agrawal D.K., Wanner B.L.;
857
+ RT "A phoA structural gene mutation that conditionally affects formation
858
+ RT of the enzyme bacterial alkaline phosphatase.";
859
+ RL J. Bacteriol. 172:3180-3190(1990).
860
+ RN [8]
861
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
862
+ RX MEDLINE=82081850; PubMed=6273802; DOI=10.1093/nar/9.21.5671;
863
+ RA Kikuchi Y., Yoda K., Yamasaki M., Tamura G.;
864
+ RT "The nucleotide sequence of the promoter and the amino-terminal region
865
+ RT of alkaline phosphatase structural gene (phoA) of Escherichia coli.";
866
+ RL Nucleic Acids Res. 9:5671-5678(1981).
867
+ RN [9]
868
+ RP PROTEIN SEQUENCE OF 23-471 (ISOZYME 3).
869
+ RX MEDLINE=81273081; PubMed=7022451; DOI=10.1073/pnas.78.6.3473;
870
+ RA Bradshaw R.A., Cancedda F., Ericsson L.H., Neumann P.A., Piccoli S.P.,
871
+ RA Schlesinger M.J., Shriefer K., Walsh K.A.;
872
+ RT "Amino acid sequence of Escherichia coli alkaline phosphatase.";
873
+ RL Proc. Natl. Acad. Sci. U.S.A. 78:3473-3477(1981).
874
+ RN [10]
875
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-193 AND 385-399.
876
+ RX MEDLINE=82119946; PubMed=7035431;
877
+ RA Inouye H., Barnes W., Beckwith J.;
878
+ RT "Signal sequence of alkaline phosphatase of Escherichia coli.";
879
+ RL J. Bacteriol. 149:434-439(1982).
880
+ RN [11]
881
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
882
+ RX MEDLINE=89340570; PubMed=2668291;
883
+ RA Laforet G.A., Kaiser E.T., Kendall D.A.;
884
+ RT "Signal peptide subsegments are not always functionally
885
+ RT interchangeable. M13 procoat hydrophobic core fails to transport
886
+ RT alkaline phosphatase in Escherichia coli.";
887
+ RL J. Biol. Chem. 264:14478-14485(1989).
888
+ RN [12]
889
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
890
+ RX MEDLINE=86137393; PubMed=3912261; DOI=10.1016/0378-1119(85)90319-1;
891
+ RA Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N.;
892
+ RT "Periplasmic production of correctly processed human growth hormone in
893
+ RT Escherichia coli: natural and bacterial signal sequences are
894
+ RT interchangeable.";
895
+ RL Gene 39:247-254(1985).
896
+ RN [13]
897
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
898
+ RX MEDLINE=86250586; PubMed=3522543;
899
+ RA Michaelis S., Hunt J.F., Beckwith J.;
900
+ RT "Effects of signal sequence mutations on the kinetics of alkaline
901
+ RT phosphatase export to the periplasm in Escherichia coli.";
902
+ RL J. Bacteriol. 167:160-167(1986).
903
+ RN [14]
904
+ RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
905
+ RX MEDLINE=86115281; PubMed=3910843; DOI=10.1016/0022-2836(85)90115-9;
906
+ RA Sowadski J.M., Handschumacher M.D., Krishna Murthy H.M., Foster B.A.,
907
+ RA Wyckoff H.W.;
908
+ RT "Refined structure of alkaline phosphatase from Escherichia coli at
909
+ RT 2.8-A resolution.";
910
+ RL J. Mol. Biol. 186:417-433(1985).
911
+ RN [15]
912
+ RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
913
+ RX MEDLINE=91186406; PubMed=2010919; DOI=10.1016/0022-2836(91)90724-K;
914
+ RA Kim E.E., Wyckoff H.W.;
915
+ RT "Reaction mechanism of alkaline phosphatase based on crystal
916
+ RT structures. Two-metal ion catalysis.";
917
+ RL J. Mol. Biol. 218:449-464(1991).
918
+ RN [16]
919
+ RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
920
+ RX PubMed=7577993; DOI=10.1021/bi00043a001;
921
+ RA Dealwis C.G., Brennan C., Christianson K., Mandecki W.,
922
+ RA Abad-Zapatero C.;
923
+ RT "Crystallographic analysis of reversible metal binding observed in a
924
+ RT mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase.";
925
+ RL Biochemistry 34:13967-13973(1995).
926
+ RN [17]
927
+ RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
928
+ RX MEDLINE=96194161; PubMed=8652582; DOI=10.1021/bi9523421;
929
+ RA Ma L., Kantrowitz E.R.;
930
+ RT "Kinetic and X-ray structural studies of a mutant Escherichia coli
931
+ RT alkaline phosphatase (His-412-->Gln) at one of the zinc binding
932
+ RT sites.";
933
+ RL Biochemistry 35:2394-2402(1996).
934
+ RN [18]
935
+ RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
936
+ RX MEDLINE=97397347; PubMed=9253408; DOI=10.1038/nsb0897-618;
937
+ RA Murphy J.E., Stec B., Ma L., Kantrowitz E.R.;
938
+ RT "Trapping and visualization of a covalent enzyme-phosphate
939
+ RT intermediate.";
940
+ RL Nat. Struct. Biol. 4:618-622(1997).
941
+ RN [19]
942
+ RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
943
+ RX MEDLINE=98202577; PubMed=9533886; DOI=10.1006/jmbi.1998.1635;
944
+ RA Stec B., Hehir M.J., Brennan C., Nolte M., Kantrowitz E.R.;
945
+ RT "Kinetic and X-ray structural studies of three mutant E. coli alkaline
946
+ RT phosphatases: insights into the catalytic mechanism without the
947
+ RT nucleophile Ser102.";
948
+ RL J. Mol. Biol. 277:647-662(1998).
949
+ RN [20]
950
+ RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
951
+ RX MEDLINE=99185045; PubMed=10085061; DOI=10.1074/jbc.274.13.8351;
952
+ RA Holtz K.M., Stec B., Kantrowitz E.R.;
953
+ RT "A model of the transition state in the alkaline phosphatase
954
+ RT reaction.";
955
+ RL J. Biol. Chem. 274:8351-8354(1999).
956
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
957
+ CC phosphate.
958
+ CC -!- COFACTOR: Binds 1 magnesium ion.
959
+ CC -!- COFACTOR: Binds 2 zinc ions.
960
+ CC -!- SUBUNIT: Isozymes 1 and 3 are a dimer of identical chains, isozyme
961
+ CC 2 is a dimer of heterogeneous chains, one of each of the subunits
962
+ CC from isozymes 1 and 3.
963
+ CC -!- INTERACTION:
964
+ CC P0A6Y8:dnaK; NbExp=1; IntAct=EBI-552958, EBI-542092;
965
+ CC P10408:secA; NbExp=1; IntAct=EBI-552958, EBI-543213;
966
+ CC -!- SUBCELLULAR LOCATION: Periplasm.
967
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
968
+ CC -----------------------------------------------------------------------
969
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
970
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
971
+ CC -----------------------------------------------------------------------
972
+ DR EMBL; X04586; CAA28257.1; -; Genomic_DNA.
973
+ DR EMBL; M13345; AAA83893.1; -; Genomic_DNA.
974
+ DR EMBL; M29664; AAA24364.1; -; Genomic_DNA.
975
+ DR EMBL; M29665; AAA24365.1; -; Genomic_DNA.
976
+ DR EMBL; U73857; AAB18107.1; -; Genomic_DNA.
977
+ DR EMBL; U00096; AAC73486.2; ALT_INIT; Genomic_DNA.
978
+ DR EMBL; AP009048; BAE76164.1; -; Genomic_DNA.
979
+ DR EMBL; M33536; AAA24372.1; -; Genomic_DNA.
980
+ DR EMBL; J01659; AAA24359.2; -; Genomic_DNA.
981
+ DR EMBL; J01660; AAA24360.1; -; Genomic_DNA.
982
+ DR EMBL; J01661; AAA24361.1; -; Genomic_DNA.
983
+ DR EMBL; J05005; AAA24362.1; -; Genomic_DNA.
984
+ DR EMBL; M14399; AAA23431.1; -; mRNA.
985
+ DR EMBL; M13763; AAA24358.1; -; Genomic_DNA.
986
+ DR PIR; A00776; PAECA.
987
+ DR RefSeq; AP_001034.1; -.
988
+ DR RefSeq; NP_414917.2; -.
989
+ DR PDB; 1AJA; X-ray; 2.50 A; A/B=23-471.
990
+ DR PDB; 1AJB; X-ray; 2.50 A; A/B=23-471.
991
+ DR PDB; 1AJC; X-ray; 2.50 A; A/B=23-471.
992
+ DR PDB; 1AJD; X-ray; 2.50 A; A/B=23-471.
993
+ DR PDB; 1ALH; X-ray; 2.50 A; A/B=26-471.
994
+ DR PDB; 1ALI; X-ray; 2.20 A; A/B=23-471.
995
+ DR PDB; 1ALJ; X-ray; 2.60 A; A/B=23-471.
996
+ DR PDB; 1ALK; X-ray; 2.00 A; A/B=23-471.
997
+ DR PDB; 1ANI; X-ray; 2.50 A; A/B=26-471.
998
+ DR PDB; 1ANJ; X-ray; 2.30 A; A/B=26-471.
999
+ DR PDB; 1B8J; X-ray; 1.90 A; A/B=23-471.
1000
+ DR PDB; 1ED8; X-ray; 1.75 A; A/B=23-471.
1001
+ DR PDB; 1ED9; X-ray; 1.75 A; A/B=23-471.
1002
+ DR PDB; 1ELX; X-ray; 2.60 A; A/B=23-471.
1003
+ DR PDB; 1ELY; X-ray; 2.80 A; A/B=23-471.
1004
+ DR PDB; 1ELZ; X-ray; 2.80 A; A/B=23-471.
1005
+ DR PDB; 1EW8; X-ray; 2.20 A; A/B=23-471.
1006
+ DR PDB; 1EW9; X-ray; 2.00 A; A/B=23-471.
1007
+ DR PDB; 1HJK; X-ray; 2.30 A; A/B=23-471.
1008
+ DR PDB; 1HQA; X-ray; 2.25 A; A/B=23-471.
1009
+ DR PDB; 1KH4; X-ray; 2.40 A; A/B=23-471.
1010
+ DR PDB; 1KH5; X-ray; 2.00 A; A/B=23-471.
1011
+ DR PDB; 1KH7; X-ray; 2.40 A; A/B=23-471.
1012
+ DR PDB; 1KH9; X-ray; 2.50 A; A/B=23-471.
1013
+ DR PDB; 1KHJ; X-ray; 2.30 A; A/B=23-471.
1014
+ DR PDB; 1KHK; X-ray; 2.50 A; A/B=23-471.
1015
+ DR PDB; 1KHL; X-ray; 2.50 A; A/B=23-471.
1016
+ DR PDB; 1KHN; X-ray; 2.60 A; A/B=23-471.
1017
+ DR PDB; 1URA; X-ray; 2.04 A; A/B=26-471.
1018
+ DR PDB; 1URB; X-ray; 2.14 A; A/B=26-471.
1019
+ DR PDB; 1Y6V; X-ray; 1.60 A; A/B=23-471.
1020
+ DR PDB; 1Y7A; X-ray; 1.77 A; A/B=23-471.
1021
+ DR PDB; 2ANH; X-ray; 2.40 A; A/B=26-471.
1022
+ DR PDB; 2G9Y; X-ray; 2.00 A; A/B=23-471.
1023
+ DR PDB; 2GA3; X-ray; 2.20 A; A/B=23-471.
1024
+ DR PDB; 3BDF; X-ray; 1.40 A; A/B=22-471.
1025
+ DR PDB; 3BDG; X-ray; 1.40 A; A=22-471, B=22-471.
1026
+ DR PDB; 3BDH; X-ray; 1.85 A; A/B=22-471.
1027
+ DR PDB; 3CMR; X-ray; 2.05 A; A/B=23-471.
1028
+ DR PDB; 3DPC; X-ray; 2.30 A; A/B=23-471.
1029
+ DR PDB; 3DYC; X-ray; 2.30 A; A/B=23-471.
1030
+ DR PDBsum; 1AJA; -.
1031
+ DR PDBsum; 1AJB; -.
1032
+ DR PDBsum; 1AJC; -.
1033
+ DR PDBsum; 1AJD; -.
1034
+ DR PDBsum; 1ALH; -.
1035
+ DR PDBsum; 1ALI; -.
1036
+ DR PDBsum; 1ALJ; -.
1037
+ DR PDBsum; 1ALK; -.
1038
+ DR PDBsum; 1ANI; -.
1039
+ DR PDBsum; 1ANJ; -.
1040
+ DR PDBsum; 1B8J; -.
1041
+ DR PDBsum; 1ED8; -.
1042
+ DR PDBsum; 1ED9; -.
1043
+ DR PDBsum; 1ELX; -.
1044
+ DR PDBsum; 1ELY; -.
1045
+ DR PDBsum; 1ELZ; -.
1046
+ DR PDBsum; 1EW8; -.
1047
+ DR PDBsum; 1EW9; -.
1048
+ DR PDBsum; 1HJK; -.
1049
+ DR PDBsum; 1HQA; -.
1050
+ DR PDBsum; 1KH4; -.
1051
+ DR PDBsum; 1KH5; -.
1052
+ DR PDBsum; 1KH7; -.
1053
+ DR PDBsum; 1KH9; -.
1054
+ DR PDBsum; 1KHJ; -.
1055
+ DR PDBsum; 1KHK; -.
1056
+ DR PDBsum; 1KHL; -.
1057
+ DR PDBsum; 1KHN; -.
1058
+ DR PDBsum; 1URA; -.
1059
+ DR PDBsum; 1URB; -.
1060
+ DR PDBsum; 1Y6V; -.
1061
+ DR PDBsum; 1Y7A; -.
1062
+ DR PDBsum; 2ANH; -.
1063
+ DR PDBsum; 2G9Y; -.
1064
+ DR PDBsum; 2GA3; -.
1065
+ DR PDBsum; 3BDF; -.
1066
+ DR PDBsum; 3BDG; -.
1067
+ DR PDBsum; 3BDH; -.
1068
+ DR PDBsum; 3CMR; -.
1069
+ DR PDBsum; 3DPC; -.
1070
+ DR PDBsum; 3DYC; -.
1071
+ DR DIP; DIP:10496N; -.
1072
+ DR IntAct; P00634; 3.
1073
+ DR ECO2DBASE; F046.6; 6TH EDITION.
1074
+ DR GeneID; 945041; -.
1075
+ DR GenomeReviews; AP009048_GR; JW0374.
1076
+ DR GenomeReviews; U00096_GR; b0383.
1077
+ DR KEGG; ecj:JW0374; -.
1078
+ DR KEGG; eco:b0383; -.
1079
+ DR EchoBASE; EB0720; -.
1080
+ DR EcoGene; EG10727; phoA.
1081
+ DR HOGENOM; P00634; -.
1082
+ DR OMA; P00634; VKQSTIA.
1083
+ DR BioCyc; EcoCyc:ALKAPHOSPHA-MON; -.
1084
+ DR BioCyc; MetaCyc:ALKAPHOSPHA-MON; -.
1085
+ DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
1086
+ DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:EC.
1087
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
1088
+ DR GO; GO:0005515; F:protein binding; IPI:IntAct.
1089
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
1090
+ DR GO; GO:0008152; P:metabolic process; IEA:InterPro.
1091
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
1092
+ DR InterPro; IPR001952; Alkaline_phosphatase.
1093
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
1094
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
1095
+ DR Pfam; PF00245; Alk_phosphatase; 1.
1096
+ DR PRINTS; PR00113; ALKPHPHTASE.
1097
+ DR SMART; SM00098; alkPPc; 1.
1098
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1099
+ PE 1: Evidence at protein level;
1100
+ KW 3D-structure; Complete proteome; Direct protein sequencing;
1101
+ KW Disulfide bond; Hydrolase; Magnesium; Metal-binding; Periplasm;
1102
+ KW Phosphoprotein; Signal; Zinc.
1103
+ FT SIGNAL 1 21
1104
+ FT CHAIN 22 471 Alkaline phosphatase.
1105
+ FT /FTId=PRO_0000024012.
1106
+ FT ACT_SITE 124 124 Phosphoserine intermediate.
1107
+ FT METAL 73 73 Magnesium.
1108
+ FT METAL 73 73 Zinc 2.
1109
+ FT METAL 175 175 Magnesium.
1110
+ FT METAL 177 177 Magnesium.
1111
+ FT METAL 344 344 Magnesium.
1112
+ FT METAL 349 349 Zinc 1.
1113
+ FT METAL 353 353 Zinc 1.
1114
+ FT METAL 391 391 Zinc 2.
1115
+ FT METAL 392 392 Zinc 2.
1116
+ FT METAL 434 434 Zinc 1.
1117
+ FT DISULFID 190 200
1118
+ FT DISULFID 308 358
1119
+ FT VARIANT 22 22 Missing (in isozyme 3).
1120
+ FT CONFLICT 10 10 L -> V (in Ref. 12; AAA23431).
1121
+ FT CONFLICT 78 80 SEI -> WGS (in Ref. 8; AAA24359).
1122
+ FT CONFLICT 198 198 E -> Q (in Ref. 9; AA sequence).
1123
+ FT TURN 41 44
1124
+ FT HELIX 52 56
1125
+ FT STRAND 65 72
1126
+ FT HELIX 77 88
1127
+ FT TURN 95 98
1128
+ FT STRAND 101 107
1129
+ FT TURN 113 115
1130
+ FT STRAND 118 121
1131
+ FT HELIX 124 133
1132
+ FT STRAND 142 144
1133
+ FT HELIX 154 160
1134
+ FT STRAND 164 172
1135
+ FT HELIX 176 179
1136
+ FT TURN 180 182
1137
+ FT HELIX 193 199
1138
+ FT HELIX 201 203
1139
+ FT HELIX 205 207
1140
+ FT HELIX 213 220
1141
+ FT STRAND 223 228
1142
+ FT HELIX 231 234
1143
+ FT STRAND 235 240
1144
+ FT HELIX 247 253
1145
+ FT STRAND 257 259
1146
+ FT HELIX 262 267
1147
+ FT STRAND 272 275
1148
+ FT STRAND 277 280
1149
+ FT STRAND 282 285
1150
+ FT STRAND 289 291
1151
+ FT HELIX 299 302
1152
+ FT HELIX 312 314
1153
+ FT STRAND 316 318
1154
+ FT HELIX 321 333
1155
+ FT STRAND 339 345
1156
+ FT HELIX 347 353
1157
+ FT HELIX 357 381
1158
+ FT STRAND 382 393
1159
+ FT STRAND 397 399
1160
+ FT STRAND 406 413
1161
+ FT STRAND 417 424
1162
+ FT STRAND 428 431
1163
+ FT STRAND 439 445
1164
+ FT HELIX 448 451
1165
+ FT STRAND 452 456
1166
+ FT HELIX 457 467
1167
+ SQ SEQUENCE 471 AA; 49439 MW; 8A8DE1F29D9D9253 CRC64;
1168
+ MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD QTAALRDSLS
1169
+ DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY
1170
+ VTDSAASATA WSTGVKTYNG ALGVDIHEKD HPTILEMAKA AGLATGNVST AELQDATPAA
1171
+ LVAHVTSRKC YGPSATSEKC PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG
1172
+ EWQGKTLREQ AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN
1173
+ IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK QDHAANPCGQ
1174
+ IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA PDTKAPGLTQ ALNTKDGAVM
1175
+ VMSYGNSEED SQEHTGSQLR IAAYGPHAAN VVGLTDQTDL FYTMKAALGL K
1176
+ //
1177
+ ID PPB1_HUMAN Reviewed; 535 AA.
1178
+ AC P05187; P05188; P06861; Q53S78; Q96DB7;
1179
+ DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
1180
+ DT 01-JUL-1989, sequence version 2.
1181
+ DT 28-JUL-2009, entry version 122.
1182
+ DE RecName: Full=Alkaline phosphatase, placental type;
1183
+ DE EC=3.1.3.1;
1184
+ DE AltName: Full=PLAP-1;
1185
+ DE AltName: Full=Alkaline phosphatase Regan isozyme;
1186
+ DE Flags: Precursor;
1187
+ GN Name=ALPP; Synonyms=PLAP;
1188
+ OS Homo sapiens (Human).
1189
+ OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
1190
+ OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
1191
+ OC Catarrhini; Hominidae; Homo.
1192
+ OX NCBI_TaxID=9606;
1193
+ RN [1]
1194
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
1195
+ RX MEDLINE=88298886; PubMed=3042787;
1196
+ RA Knoll B.J., Rothblum K.N., Longley M.A.;
1197
+ RT "Nucleotide sequence of the human placental alkaline phosphatase gene.
1198
+ RT Evolution of the 5' flanking region by deletion/substitution.";
1199
+ RL J. Biol. Chem. 263:12020-12027(1988).
1200
+ RN [2]
1201
+ RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-231.
1202
+ RX MEDLINE=86140079; PubMed=3512548;
1203
+ RA Millan J.L.;
1204
+ RT "Molecular cloning and sequence analysis of human placental alkaline
1205
+ RT phosphatase.";
1206
+ RL J. Biol. Chem. 261:3112-3115(1986).
1207
+ RN [3]
1208
+ RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANTS
1209
+ RP LEU-25 AND HIS-263.
1210
+ RX MEDLINE=86287303; PubMed=3461452; DOI=10.1073/pnas.83.15.5597;
1211
+ RA Henthorn P.S., Knoll B.J., Raducha M., Rothblum K.N., Slaughter C.,
1212
+ RA Weiss M., Lafferty M.A., Fischer T., Harris H.;
1213
+ RT "Products of two common alleles at the locus for human placental
1214
+ RT alkaline phosphatase differ by seven amino acids.";
1215
+ RL Proc. Natl. Acad. Sci. U.S.A. 83:5597-5601(1986).
1216
+ RN [4]
1217
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
1218
+ RX PubMed=15815621; DOI=10.1038/nature03466;
1219
+ RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
1220
+ RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
1221
+ RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
1222
+ RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
1223
+ RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
1224
+ RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
1225
+ RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
1226
+ RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
1227
+ RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
1228
+ RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
1229
+ RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
1230
+ RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
1231
+ RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
1232
+ RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
1233
+ RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
1234
+ RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
1235
+ RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
1236
+ RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
1237
+ RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
1238
+ RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
1239
+ RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
1240
+ RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
1241
+ RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
1242
+ RA Waterston R.H., Wilson R.K.;
1243
+ RT "Generation and annotation of the DNA sequences of human chromosomes 2
1244
+ RT and 4.";
1245
+ RL Nature 434:724-731(2005).
1246
+ RN [5]
1247
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-89.
1248
+ RC TISSUE=Cervix, and Placenta;
1249
+ RX PubMed=15489334; DOI=10.1101/gr.2596504;
1250
+ RG The MGC Project Team;
1251
+ RT "The status, quality, and expansion of the NIH full-length cDNA
1252
+ RT project: the Mammalian Gene Collection (MGC).";
1253
+ RL Genome Res. 14:2121-2127(2004).
1254
+ RN [6]
1255
+ RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-535, AND VARIANT LEU-25.
1256
+ RX MEDLINE=86094295; PubMed=3001717; DOI=10.1073/pnas.82.24.8715;
1257
+ RA Kam W., Clauser E., Kim Y.S., Kan Y.W., Rutter W.J.;
1258
+ RT "Cloning, sequencing, and chromosomal localization of human term
1259
+ RT placental alkaline phosphatase cDNA.";
1260
+ RL Proc. Natl. Acad. Sci. U.S.A. 82:8715-8719(1985).
1261
+ RN [7]
1262
+ RP PROTEIN SEQUENCE OF 23-64.
1263
+ RX MEDLINE=84079906; PubMed=6651840; DOI=10.1016/S0006-291X(83)80252-6;
1264
+ RA Ezra E., Blacher R., Udenfriend S.;
1265
+ RT "Purification and partial sequencing of human placental alkaline
1266
+ RT phosphatase.";
1267
+ RL Biochem. Biophys. Res. Commun. 116:1076-1083(1983).
1268
+ RN [8]
1269
+ RP NUCLEOTIDE SEQUENCE OF 382-535.
1270
+ RX MEDLINE=86233318; PubMed=3459156; DOI=10.1073/pnas.83.11.3781;
1271
+ RA Ovitt C.E., Strauss A.W., Alpers D.H., Chou J.Y., Boime I.;
1272
+ RT "Expression of different-sized placental alkaline phosphatase mRNAs in
1273
+ RT placenta and choriocarcinoma cells.";
1274
+ RL Proc. Natl. Acad. Sci. U.S.A. 83:3781-3785(1986).
1275
+ RN [9]
1276
+ RP PROTEIN SEQUENCE OF 485-535.
1277
+ RX MEDLINE=88144444; PubMed=3422741; DOI=10.1073/pnas.85.5.1398;
1278
+ RA Micanovic R., Bailey C.A., Brink L., Gerber L., Pan Y.C.E.,
1279
+ RA Hulmes J.D., Udenfriend S.;
1280
+ RT "Aspartic acid-484 of nascent placental alkaline phosphatase condenses
1281
+ RT with a phosphatidylinositol glycan to become the carboxyl terminus of
1282
+ RT the mature enzyme.";
1283
+ RL Proc. Natl. Acad. Sci. U.S.A. 85:1398-1402(1988).
1284
+ RN [10]
1285
+ RP GPI-ANCHOR AT ASP-506.
1286
+ RX MEDLINE=90115829; PubMed=2153284; DOI=10.1073/pnas.87.1.157;
1287
+ RA Micanovic R., Gerber L.D., Berger J., Kodukula K., Udenfriend S.;
1288
+ RT "Selectivity of the cleavage/attachment site of phosphatidylinositol-
1289
+ RT glycan-anchored membrane proteins determined by site-specific
1290
+ RT mutagenesis at Asp-484 of placental alkaline phosphatase.";
1291
+ RL Proc. Natl. Acad. Sci. U.S.A. 87:157-161(1990).
1292
+ RN [11]
1293
+ RP EFFECT OF MUTAGENESIS OF C-TERMINAL PEPTIDE ON GPI-ANCHORING.
1294
+ RX MEDLINE=92113014; PubMed=1730777; DOI=10.1083/jcb.116.3.799;
1295
+ RA Lowe M.E.;
1296
+ RT "Site-specific mutations in the COOH-terminus of placental alkaline
1297
+ RT phosphatase: a single amino acid change converts a
1298
+ RT phosphatidylinositol-glycan-anchored protein to a secreted protein.";
1299
+ RL J. Cell Biol. 116:799-807(1992).
1300
+ RN [12]
1301
+ RP DISULFIDE BONDS.
1302
+ RX MEDLINE=22063279; PubMed=11937510; DOI=10.1074/jbc.M202298200;
1303
+ RA Kozlenkov A., Manes T., Hoylaerts M.F., Millan J.L.;
1304
+ RT "Function assignment to conserved residues in mammalian alkaline
1305
+ RT phosphatases.";
1306
+ RL J. Biol. Chem. 277:22992-22999(2002).
1307
+ RN [13]
1308
+ RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
1309
+ RP SPECTROMETRY.
1310
+ RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
1311
+ RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
1312
+ RA Elledge S.J., Gygi S.P.;
1313
+ RT "A quantitative atlas of mitotic phosphorylation.";
1314
+ RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
1315
+ RN [14]
1316
+ RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 56-535.
1317
+ RX PubMed=11124260; DOI=10.1074/jbc.M009250200;
1318
+ RA Le Du M.H., Stigbrand T., Taussig M.J., Menez A., Stura E.A.;
1319
+ RT "Crystal structure of alkaline phosphatase from human placenta at 1.8
1320
+ RT A resolution. Implication for a substrate specificity.";
1321
+ RL J. Biol. Chem. 276:9158-9165(2001).
1322
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
1323
+ CC phosphate.
1324
+ CC -!- COFACTOR: Binds 1 magnesium ion (By similarity).
1325
+ CC -!- COFACTOR: Binds 2 zinc ions (By similarity).
1326
+ CC -!- SUBUNIT: Homodimer.
1327
+ CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
1328
+ CC -!- POLYMORPHISM: Placental ALP is highly polymorphic, there are at
1329
+ CC least three common alleles.
1330
+ CC -!- MISCELLANEOUS: In most mammals there are four different isozymes:
1331
+ CC placental, placental-like, intestinal and tissue non-specific
1332
+ CC (liver/bone/kidney).
1333
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
1334
+ CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
1335
+ CC URL="http://en.wikipedia.org/wiki/Alkaline_phosphatase";
1336
+ CC -----------------------------------------------------------------------
1337
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
1338
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
1339
+ CC -----------------------------------------------------------------------
1340
+ DR EMBL; M19159; AAA51710.1; -; Genomic_DNA.
1341
+ DR EMBL; M13077; AAC97139.1; -; mRNA.
1342
+ DR EMBL; M14169; AAA51708.1; ALT_INIT; mRNA.
1343
+ DR EMBL; M14170; AAA51709.1; -; mRNA.
1344
+ DR EMBL; AC068134; AAY24087.1; -; Genomic_DNA.
1345
+ DR EMBL; BC009647; AAH09647.1; -; mRNA.
1346
+ DR EMBL; BC068501; AAH68501.1; -; mRNA.
1347
+ DR EMBL; BC094743; AAH94743.1; -; mRNA.
1348
+ DR EMBL; M12551; AAA51706.1; -; mRNA.
1349
+ DR IPI; IPI00007289; -.
1350
+ DR PIR; A31074; PAHUA.
1351
+ DR RefSeq; NP_001623.3; -.
1352
+ DR UniGene; Hs.284255; -.
1353
+ DR PDB; 1EW2; X-ray; 1.82 A; A=23-535.
1354
+ DR PDB; 1ZEB; X-ray; 1.90 A; A=23-506.
1355
+ DR PDB; 1ZED; X-ray; 1.57 A; A=23-506.
1356
+ DR PDB; 1ZEF; X-ray; 1.90 A; A=23-506.
1357
+ DR PDB; 2GLQ; X-ray; 1.60 A; A=23-506.
1358
+ DR PDBsum; 1EW2; -.
1359
+ DR PDBsum; 1ZEB; -.
1360
+ DR PDBsum; 1ZED; -.
1361
+ DR PDBsum; 1ZEF; -.
1362
+ DR PDBsum; 2GLQ; -.
1363
+ DR PhosphoSite; P05187; -.
1364
+ DR PRIDE; P05187; -.
1365
+ DR Ensembl; ENST00000392027; ENSP00000375881; ENSG00000163283; Homo sapiens.
1366
+ DR GeneID; 250; -.
1367
+ DR KEGG; hsa:250; -.
1368
+ DR NMPDR; fig|9606.3.peg.19512; -.
1369
+ DR UCSC; uc002vsq.1; human.
1370
+ DR GeneCards; GC02P232951; -.
1371
+ DR H-InvDB; HIX0002924; -.
1372
+ DR HGNC; HGNC:439; ALPP.
1373
+ DR HPA; CAB000067; -.
1374
+ DR MIM; 171800; gene.
1375
+ DR PharmGKB; PA24730; -.
1376
+ DR HOGENOM; P05187; -.
1377
+ DR HOVERGEN; P05187; -.
1378
+ DR OMA; P05187; EIPLAMD.
1379
+ DR BRENDA; 3.1.3.1; 247.
1380
+ DR NextBio; 1001; -.
1381
+ DR ArrayExpress; P05187; -.
1382
+ DR Bgee; P05187; -.
1383
+ DR CleanEx; HS_ALPP; -.
1384
+ DR GermOnline; ENSG00000163283; Homo sapiens.
1385
+ DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
1386
+ DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
1387
+ DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
1388
+ DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
1389
+ DR GO; GO:0004035; F:alkaline phosphatase activity; NAS:UniProtKB.
1390
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
1391
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
1392
+ DR GO; GO:0008152; P:metabolic process; IEA:InterPro.
1393
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
1394
+ DR InterPro; IPR001952; Alkaline_phosphatase.
1395
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
1396
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
1397
+ DR Pfam; PF00245; Alk_phosphatase; 1.
1398
+ DR PRINTS; PR00113; ALKPHPHTASE.
1399
+ DR SMART; SM00098; alkPPc; 1.
1400
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1401
+ PE 1: Evidence at protein level;
1402
+ KW 3D-structure; Cell membrane; Complete proteome;
1403
+ KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
1404
+ KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
1405
+ KW Phosphoprotein; Polymorphism; Signal; Transmembrane; Zinc.
1406
+ FT SIGNAL 1 22
1407
+ FT CHAIN 23 506 Alkaline phosphatase, placental type.
1408
+ FT /FTId=PRO_0000024031.
1409
+ FT PROPEP 507 535 Removed in mature form.
1410
+ FT /FTId=PRO_0000024032.
1411
+ FT TRANSMEM 513 529
1412
+ FT ACT_SITE 114 114 Phosphoserine intermediate.
1413
+ FT METAL 64 64 Magnesium (Potential).
1414
+ FT METAL 64 64 Zinc 2 (Potential).
1415
+ FT METAL 333 333 Magnesium (Potential).
1416
+ FT METAL 338 338 Zinc 1 (Potential).
1417
+ FT METAL 342 342 Zinc 1 (Potential).
1418
+ FT METAL 379 379 Zinc 2 (Potential).
1419
+ FT METAL 380 380 Zinc 2 (Potential).
1420
+ FT METAL 454 454 Zinc 1 (Potential).
1421
+ FT MOD_RES 114 114 Phosphoserine.
1422
+ FT LIPID 506 506 GPI-anchor amidated aspartate.
1423
+ FT CARBOHYD 144 144 N-linked (GlcNAc...) (Potential).
1424
+ FT CARBOHYD 271 271 N-linked (GlcNAc...) (Potential).
1425
+ FT DISULFID 143 205
1426
+ FT DISULFID 489 496
1427
+ FT VARIANT 25 25 P -> L (in dbSNP:rs1130335).
1428
+ FT /FTId=VAR_017419.
1429
+ FT VARIANT 89 89 I -> L (in dbSNP:rs13026692).
1430
+ FT /FTId=VAR_050520.
1431
+ FT VARIANT 231 231 R -> P (in dbSNP:rs1048988).
1432
+ FT /FTId=VAR_050521.
1433
+ FT VARIANT 263 263 R -> H (in dbSNP:rs2853378).
1434
+ FT /FTId=VAR_050522.
1435
+ FT VARIANT 451 451 E -> G (in dbSNP:rs1048994).
1436
+ FT /FTId=VAR_050523.
1437
+ FT CONFLICT 66 66 M -> V (in Ref. 3; AAA51709).
1438
+ FT CONFLICT 261 262 AK -> GE (in Ref. 6; AAA51706).
1439
+ FT CONFLICT 277 277 Q -> R (in Ref. 3; AAA51709).
1440
+ FT CONFLICT 285 285 T -> A (in Ref. 3; AAA51709).
1441
+ FT CONFLICT 324 324 N -> H (in Ref. 6; AAA51706).
1442
+ FT CONFLICT 389 389 Y -> C (in Ref. 3; AAA51709).
1443
+ FT CONFLICT 394 394 S -> G (in Ref. 3; AAA51709).
1444
+ FT CONFLICT 396 397 IF -> FI (in Ref. 6; AAA51706).
1445
+ FT CONFLICT 401 401 P -> A (in Ref. 6; AAA51706).
1446
+ FT CONFLICT 436 436 S -> T (in Ref. 8).
1447
+ FT HELIX 26 29
1448
+ FT HELIX 31 47
1449
+ FT STRAND 56 63
1450
+ FT HELIX 68 81
1451
+ FT HELIX 92 95
1452
+ FT STRAND 97 103
1453
+ FT STRAND 107 111
1454
+ FT HELIX 114 123
1455
+ FT STRAND 132 134
1456
+ FT HELIX 143 145
1457
+ FT HELIX 154 160
1458
+ FT STRAND 164 172
1459
+ FT HELIX 176 179
1460
+ FT TURN 180 182
1461
+ FT HELIX 193 195
1462
+ FT HELIX 198 202
1463
+ FT HELIX 208 214
1464
+ FT STRAND 219 224
1465
+ FT HELIX 227 229
1466
+ FT HELIX 243 245
1467
+ FT STRAND 249 251
1468
+ FT HELIX 255 261
1469
+ FT STRAND 266 269
1470
+ FT HELIX 272 280
1471
+ FT STRAND 286 290
1472
+ FT STRAND 292 295
1473
+ FT HELIX 299 301
1474
+ FT TURN 304 306
1475
+ FT HELIX 310 321
1476
+ FT STRAND 328 334
1477
+ FT HELIX 337 342
1478
+ FT HELIX 346 366
1479
+ FT TURN 369 371
1480
+ FT STRAND 372 379
1481
+ FT STRAND 381 386
1482
+ FT STRAND 411 418
1483
+ FT HELIX 433 436
1484
+ FT STRAND 445 447
1485
+ FT STRAND 459 465
1486
+ FT HELIX 468 470
1487
+ FT STRAND 473 476
1488
+ FT HELIX 479 487
1489
+ SQ SEQUENCE 535 AA; 57954 MW; 13C136679A70C76B CRC64;
1490
+ MLGPCMLLLL LLLGLRLQLS LGIIPVEEEN PDFWNREAAE ALGAAKKLQP AQTAAKNLII
1491
+ FLGDGMGVST VTAARILKGQ KKDKLGPEIP LAMDRFPYVA LSKTYNVDKH VPDSGATATA
1492
+ YLCGVKGNFQ TIGLSAAARF NQCNTTRGNE VISVMNRAKK AGKSVGVVTT TRVQHASPAG
1493
+ TYAHTVNRNW YSDADVPASA RQEGCQDIAT QLISNMDIDV ILGGGRKYMF RMGTPDPEYP
1494
+ DDYSQGGTRL DGKNLVQEWL AKRQGARYVW NRTELMQASL DPSVTHLMGL FEPGDMKYEI
1495
+ HRDSTLDPSL MEMTEAALRL LSRNPRGFFL FVEGGRIDHG HHESRAYRAL TETIMFDDAI
1496
+ ERAGQLTSEE DTLSLVTADH SHVFSFGGYP LRGSSIFGLA PGKARDRKAY TVLLYGNGPG
1497
+ YVLKDGARPD VTESESGSPE YRQQSAVPLD EETHAGEDVA VFARGPQAHL VHGVQEQTFI
1498
+ AHVMAFAACL EPYTACDLAP PAGTTDAAHP GRSVVPALLP LLAGTLLLLE TATAP
1499
+ //
1500
+ ID PPBI_HUMAN Reviewed; 528 AA.
1501
+ AC P09923; Q53S80; Q9UBV5; Q9UCL2;
1502
+ DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
1503
+ DT 01-APR-1990, sequence version 2.
1504
+ DT 28-JUL-2009, entry version 102.
1505
+ DE RecName: Full=Intestinal alkaline phosphatase;
1506
+ DE Short=IAP;
1507
+ DE EC=3.1.3.1;
1508
+ DE Flags: Precursor;
1509
+ GN Name=ALPI;
1510
+ OS Homo sapiens (Human).
1511
+ OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
1512
+ OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
1513
+ OC Catarrhini; Hominidae; Homo.
1514
+ OX NCBI_TaxID=9606;
1515
+ RN [1]
1516
+ RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
1517
+ RX MEDLINE=87118235; PubMed=3468508; DOI=10.1073/pnas.84.3.695;
1518
+ RA Berger J., Garattini E., Hua J.-C., Udenfriend S.;
1519
+ RT "Cloning and sequencing of human intestinal alkaline phosphatase
1520
+ RT cDNA.";
1521
+ RL Proc. Natl. Acad. Sci. U.S.A. 84:695-698(1987).
1522
+ RN [2]
1523
+ RP NUCLEOTIDE SEQUENCE [MRNA].
1524
+ RX MEDLINE=87147248; PubMed=3469665; DOI=10.1073/pnas.84.5.1234;
1525
+ RA Henthorn P.S., Raducha M., Edwards Y.H., Weiss M.J., Slaughter C.,
1526
+ RA Lafferty M.A., Harris H.;
1527
+ RT "Nucleotide and amino acid sequences of human intestinal alkaline
1528
+ RT phosphatase: close homology to placental alkaline phosphatase.";
1529
+ RL Proc. Natl. Acad. Sci. U.S.A. 84:1234-1238(1987).
1530
+ RN [3]
1531
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
1532
+ RX MEDLINE=88298885; PubMed=2841341;
1533
+ RA Henthorn P.S., Raducha M., Kadesch T., Weiss M.J., Harris H.;
1534
+ RT "Sequence and characterization of the human intestinal alkaline
1535
+ RT phosphatase gene.";
1536
+ RL J. Biol. Chem. 263:12011-12019(1988).
1537
+ RN [4]
1538
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
1539
+ RX PubMed=15815621; DOI=10.1038/nature03466;
1540
+ RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
1541
+ RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
1542
+ RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
1543
+ RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
1544
+ RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
1545
+ RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
1546
+ RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
1547
+ RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
1548
+ RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
1549
+ RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
1550
+ RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
1551
+ RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
1552
+ RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
1553
+ RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
1554
+ RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
1555
+ RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
1556
+ RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
1557
+ RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
1558
+ RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
1559
+ RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
1560
+ RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
1561
+ RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
1562
+ RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
1563
+ RA Waterston R.H., Wilson R.K.;
1564
+ RT "Generation and annotation of the DNA sequences of human chromosomes 2
1565
+ RT and 4.";
1566
+ RL Nature 434:724-731(2005).
1567
+ RN [5]
1568
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
1569
+ RX PubMed=15489334; DOI=10.1101/gr.2596504;
1570
+ RG The MGC Project Team;
1571
+ RT "The status, quality, and expansion of the NIH full-length cDNA
1572
+ RT project: the Mammalian Gene Collection (MGC).";
1573
+ RL Genome Res. 14:2121-2127(2004).
1574
+ RN [6]
1575
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
1576
+ RX MEDLINE=88096602; PubMed=3697102; DOI=10.1093/nar/15.24.10599;
1577
+ RA Millan J.L.;
1578
+ RT "Promoter structure of the human intestinal alkaline phosphatase
1579
+ RT gene.";
1580
+ RL Nucleic Acids Res. 15:10599-10599(1987).
1581
+ RN [7]
1582
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
1583
+ RX MEDLINE=88167830; PubMed=3443302; DOI=10.1016/0378-1119(87)90235-6;
1584
+ RA Knoll B.J., Rothblum K.N., Longley M.;
1585
+ RT "Two gene duplication events in the evolution of the human heat-stable
1586
+ RT alkaline phosphatases.";
1587
+ RL Gene 60:267-276(1987).
1588
+ RN [8]
1589
+ RP PROTEIN SEQUENCE OF 20-58.
1590
+ RX MEDLINE=86205956; PubMed=3458202; DOI=10.1073/pnas.83.8.2368;
1591
+ RA Hua J.-C., Berger J., Pan Y.C.E., Hulmes J.D., Udenfriend S.;
1592
+ RT "Partial sequencing of human adult, human fetal, and bovine intestinal
1593
+ RT alkaline phosphatases: comparison with the human placental and liver
1594
+ RT isozymes.";
1595
+ RL Proc. Natl. Acad. Sci. U.S.A. 83:2368-2372(1986).
1596
+ RN [9]
1597
+ RP PROTEIN SEQUENCE OF 20-49.
1598
+ RX PubMed=1458595;
1599
+ RA Nishihara Y., Hayashi Y., Adachi T., Koyama I., Stigbrand T.,
1600
+ RA Hirano K.;
1601
+ RT "Chemical nature of intestinal-type alkaline phosphatase in human
1602
+ RT kidney.";
1603
+ RL Clin. Chem. 38:2539-2542(1992).
1604
+ RN [10]
1605
+ RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASS
1606
+ RP SPECTROMETRY.
1607
+ RC TISSUE=Epithelium;
1608
+ RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
1609
+ RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
1610
+ RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
1611
+ RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
1612
+ RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
1613
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
1614
+ CC phosphate.
1615
+ CC -!- COFACTOR: Binds 1 magnesium ion (By similarity).
1616
+ CC -!- COFACTOR: Binds 2 zinc ions (By similarity).
1617
+ CC -!- SUBUNIT: Homodimer.
1618
+ CC -!- INTERACTION:
1619
+ CC Q14240:EIF4A2; NbExp=1; IntAct=EBI-1052631, EBI-73473;
1620
+ CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
1621
+ CC -!- MISCELLANEOUS: In most mammals there are four different isozymes:
1622
+ CC placental, placental-like, intestinal and tissue non-specific
1623
+ CC (liver/bone/kidney).
1624
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
1625
+ CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
1626
+ CC URL="http://en.wikipedia.org/wiki/Alkaline_phosphatase";
1627
+ CC -----------------------------------------------------------------------
1628
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
1629
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
1630
+ CC -----------------------------------------------------------------------
1631
+ DR EMBL; M15694; AAA51703.1; -; mRNA.
1632
+ DR EMBL; M31008; AAA51704.1; -; mRNA.
1633
+ DR EMBL; J03930; AAA98617.1; -; Genomic_DNA.
1634
+ DR EMBL; AC068134; AAY24089.1; -; Genomic_DNA.
1635
+ DR EMBL; BC132678; AAI32679.1; -; mRNA.
1636
+ DR EMBL; Y00512; CAA68564.1; -; Genomic_DNA.
1637
+ DR EMBL; M19161; AAA51705.1; -; Genomic_DNA.
1638
+ DR IPI; IPI00298622; -.
1639
+ DR PIR; A31073; PAHUI.
1640
+ DR RefSeq; NP_001622.2; -.
1641
+ DR UniGene; Hs.284255; -.
1642
+ DR UniGene; Hs.37009; -.
1643
+ DR HSSP; P05187; 1EW2.
1644
+ DR SMR; P09923; 20-498.
1645
+ DR IntAct; P09923; 1.
1646
+ DR GlycoSuiteDB; P09923; -.
1647
+ DR PhosphoSite; P09923; -.
1648
+ DR PRIDE; P09923; -.
1649
+ DR Ensembl; ENST00000295463; ENSP00000295463; ENSG00000163295; Homo sapiens.
1650
+ DR GeneID; 248; -.
1651
+ DR KEGG; hsa:248; -.
1652
+ DR NMPDR; fig|9606.3.peg.19514; -.
1653
+ DR UCSC; uc002vst.2; human.
1654
+ DR GeneCards; GC02P233029; -.
1655
+ DR HGNC; HGNC:437; ALPI.
1656
+ DR MIM; 171740; gene.
1657
+ DR PharmGKB; PA24728; -.
1658
+ DR HOGENOM; P09923; -.
1659
+ DR HOVERGEN; P09923; -.
1660
+ DR OMA; P09923; KAYTSIL.
1661
+ DR BRENDA; 3.1.3.1; 247.
1662
+ DR NextBio; 993; -.
1663
+ DR ArrayExpress; P09923; -.
1664
+ DR Bgee; P09923; -.
1665
+ DR CleanEx; HS_ALPI; -.
1666
+ DR GermOnline; ENSG00000163295; Homo sapiens.
1667
+ DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
1668
+ DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
1669
+ DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
1670
+ DR GO; GO:0004035; F:alkaline phosphatase activity; NAS:UniProtKB.
1671
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
1672
+ DR GO; GO:0005515; F:protein binding; IPI:IntAct.
1673
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
1674
+ DR GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
1675
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
1676
+ DR InterPro; IPR001952; Alkaline_phosphatase.
1677
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
1678
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
1679
+ DR Pfam; PF00245; Alk_phosphatase; 1.
1680
+ DR PRINTS; PR00113; ALKPHPHTASE.
1681
+ DR SMART; SM00098; alkPPc; 1.
1682
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1683
+ PE 1: Evidence at protein level;
1684
+ KW Cell membrane; Complete proteome; Direct protein sequencing;
1685
+ KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
1686
+ KW Magnesium; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
1687
+ KW Signal; Transmembrane; Zinc.
1688
+ FT SIGNAL 1 19
1689
+ FT CHAIN 20 503 Intestinal alkaline phosphatase.
1690
+ FT /FTId=PRO_0000024037.
1691
+ FT PROPEP 504 528 Removed in mature form (By similarity).
1692
+ FT /FTId=PRO_0000024038.
1693
+ FT ACT_SITE 111 111 Phosphoserine intermediate.
1694
+ FT METAL 61 61 Magnesium (Potential).
1695
+ FT METAL 61 61 Zinc 2 (Potential).
1696
+ FT METAL 330 330 Magnesium (Potential).
1697
+ FT METAL 335 335 Zinc 1 (Potential).
1698
+ FT METAL 339 339 Zinc 1 (Potential).
1699
+ FT METAL 376 376 Zinc 2 (Potential).
1700
+ FT METAL 377 377 Zinc 2 (Potential).
1701
+ FT METAL 451 451 Zinc 1 (Potential).
1702
+ FT MOD_RES 111 111 Phosphoserine.
1703
+ FT LIPID 503 503 GPI-anchor amidated aspartate (By
1704
+ FT similarity).
1705
+ FT CARBOHYD 141 141 N-linked (GlcNAc...) (Potential).
1706
+ FT CARBOHYD 268 268 N-linked (GlcNAc...) (Potential).
1707
+ FT CARBOHYD 429 429 N-linked (GlcNAc...) (Potential).
1708
+ FT DISULFID 140 202 By similarity.
1709
+ FT DISULFID 486 493 By similarity.
1710
+ FT VARIANT 144 144 R -> H (in dbSNP:rs7559279).
1711
+ FT /FTId=VAR_050524.
1712
+ FT VARIANT 298 298 H -> L (in dbSNP:rs1047223).
1713
+ FT /FTId=VAR_011816.
1714
+ FT CONFLICT 347 347 L -> V (in Ref. 2; AAA51703).
1715
+ FT CONFLICT 410 410 I -> T (in Ref. 1; AAA51704).
1716
+ FT CONFLICT 497 497 P -> L (in Ref. 2; AAA51703).
1717
+ SQ SEQUENCE 528 AA; 56812 MW; 465306BEDF9F0B79 CRC64;
1718
+ MQGPWVLLLL GLRLQLSLGV IPAEEENPAF WNRQAAEALD AAKKLQPIQK VAKNLILFLG
1719
+ DGLGVPTVTA TRILKGQKNG KLGPETPLAM DRFPYLALSK TYNVDRQVPD SAATATAYLC
1720
+ GVKANFQTIG LSAAARFNQC NTTRGNEVIS VMNRAKQAGK SVGVVTTTRV QHASPAGTYA
1721
+ HTVNRNWYSD ADMPASARQE GCQDIATQLI SNMDIDVILG GGRKYMFPMG TPDPEYPADA
1722
+ SQNGIRLDGK NLVQEWLAKH QGAWYVWNRT ELMQASLDQS VTHLMGLFEP GDTKYEIHRD
1723
+ PTLDPSLMEM TEAALRLLSR NPRGFYLFVE GGRIDHGHHE GVAYQALTEA VMFDDAIERA
1724
+ GQLTSEEDTL TLVTADHSHV FSFGGYTLRG SSIFGLAPSK AQDSKAYTSI LYGNGPGYVF
1725
+ NSGVRPDVNE SESGSPDYQQ QAAVPLSSET HGGEDVAVFA RGPQAHLVHG VQEQSFVAHV
1726
+ MAFAACLEPY TACDLAPPAC TTDAAHPVAA SLPLLAGTLL LLGASAAP
1727
+ //
1728
+ ID PPBN_HUMAN Reviewed; 532 AA.
1729
+ AC P10696; Q16727; Q53S81; Q96CM1;
1730
+ DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
1731
+ DT 06-MAR-2007, sequence version 4.
1732
+ DT 28-JUL-2009, entry version 107.
1733
+ DE RecName: Full=Alkaline phosphatase, placental-like;
1734
+ DE EC=3.1.3.1;
1735
+ DE AltName: Full=Alkaline phosphatase Nagao isozyme;
1736
+ DE AltName: Full=Germ cell alkaline phosphatase;
1737
+ DE Short=GCAP;
1738
+ DE AltName: Full=PLAP-like;
1739
+ DE AltName: Full=ALP-1;
1740
+ DE Flags: Precursor;
1741
+ GN Name=ALPPL2; Synonyms=ALPPL;
1742
+ OS Homo sapiens (Human).
1743
+ OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
1744
+ OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
1745
+ OC Catarrhini; Hominidae; Homo.
1746
+ OX NCBI_TaxID=9606;
1747
+ RN [1]
1748
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
1749
+ RX MEDLINE=88203632; PubMed=2834730; DOI=10.1073/pnas.85.9.3024;
1750
+ RA Millan J.L., Manes T.;
1751
+ RT "Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline
1752
+ RT phosphatase gene.";
1753
+ RL Proc. Natl. Acad. Sci. U.S.A. 85:3024-3028(1988).
1754
+ RN [2]
1755
+ RP NUCLEOTIDE SEQUENCE [MRNA].
1756
+ RC TISSUE=Choriocarcinoma;
1757
+ RX MEDLINE=89308696; PubMed=2745460;
1758
+ RA Watanabe S., Watanabe T., Li W.L., Soong B.-W., Chou J.Y.;
1759
+ RT "Expression of the germ cell alkaline phosphatase gene in human
1760
+ RT choriocarcinoma cells.";
1761
+ RL J. Biol. Chem. 264:12611-12619(1989).
1762
+ RN [3]
1763
+ RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MET-273 AND ARG-316.
1764
+ RC TISSUE=Colon;
1765
+ RX MEDLINE=90124311; PubMed=2297757;
1766
+ RA Gum J.R. Jr., Hicks J.W., Sack T.L., Kim Y.S.;
1767
+ RT "Molecular cloning of complementary DNAs encoding alkaline phosphatase
1768
+ RT in human colon cancer cells.";
1769
+ RL Cancer Res. 50:1085-1091(1990).
1770
+ RN [4]
1771
+ RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-316.
1772
+ RX MEDLINE=90283879; PubMed=2162249;
1773
+ RA Lowe M.E., Strauss A.W.;
1774
+ RT "Expression of a Nagao-type, phosphatidylinositol-glycan anchored
1775
+ RT alkaline phosphatase in human choriocarcinomas.";
1776
+ RL Cancer Res. 50:3956-3962(1990).
1777
+ RN [5]
1778
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
1779
+ RX PubMed=15815621; DOI=10.1038/nature03466;
1780
+ RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
1781
+ RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
1782
+ RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
1783
+ RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
1784
+ RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
1785
+ RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
1786
+ RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
1787
+ RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
1788
+ RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
1789
+ RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
1790
+ RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
1791
+ RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
1792
+ RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
1793
+ RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
1794
+ RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
1795
+ RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
1796
+ RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
1797
+ RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
1798
+ RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
1799
+ RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
1800
+ RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
1801
+ RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
1802
+ RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
1803
+ RA Waterston R.H., Wilson R.K.;
1804
+ RT "Generation and annotation of the DNA sequences of human chromosomes 2
1805
+ RT and 4.";
1806
+ RL Nature 434:724-731(2005).
1807
+ RN [6]
1808
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-273 AND
1809
+ RP ARG-316.
1810
+ RC TISSUE=Placenta;
1811
+ RX PubMed=15489334; DOI=10.1101/gr.2596504;
1812
+ RG The MGC Project Team;
1813
+ RT "The status, quality, and expansion of the NIH full-length cDNA
1814
+ RT project: the Mammalian Gene Collection (MGC).";
1815
+ RL Genome Res. 14:2121-2127(2004).
1816
+ RN [7]
1817
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
1818
+ RX MEDLINE=88167830; PubMed=3443302; DOI=10.1016/0378-1119(87)90235-6;
1819
+ RA Knoll B.J., Rothblum K.N., Longley M.;
1820
+ RT "Two gene duplication events in the evolution of the human heat-stable
1821
+ RT alkaline phosphatases.";
1822
+ RL Gene 60:267-276(1987).
1823
+ RN [8]
1824
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
1825
+ RX MEDLINE=88262578; PubMed=3387245; DOI=10.1093/nar/16.12.5694;
1826
+ RA Shen L.P., Liu H., Kan Y.W., Kam W.;
1827
+ RT "5' nucleotide sequence of a putative human placental alkaline
1828
+ RT phosphatase-like gene.";
1829
+ RL Nucleic Acids Res. 16:5694-5694(1988).
1830
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
1831
+ CC phosphate.
1832
+ CC -!- COFACTOR: Binds 1 magnesium ion (By similarity).
1833
+ CC -!- COFACTOR: Binds 2 zinc ions (By similarity).
1834
+ CC -!- SUBUNIT: Homodimer.
1835
+ CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
1836
+ CC -!- TISSUE SPECIFICITY: Trace amounts in the testis and thymus, and in
1837
+ CC elevated amounts in germ cell tumors.
1838
+ CC -!- MISCELLANEOUS: In most mammals there are four different isozymes:
1839
+ CC placental, placental-like, intestinal and tissue non-specific
1840
+ CC (liver/bone/kidney).
1841
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
1842
+ CC -!- SEQUENCE CAUTION:
1843
+ CC Sequence=CAA30232.1; Type=Erroneous gene model prediction;
1844
+ CC -----------------------------------------------------------------------
1845
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
1846
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
1847
+ CC -----------------------------------------------------------------------
1848
+ DR EMBL; J03252; AAA98616.1; -; Genomic_DNA.
1849
+ DR EMBL; J04948; AAA51700.1; -; mRNA.
1850
+ DR EMBL; X53279; CAA37374.1; -; mRNA.
1851
+ DR EMBL; X55958; CAA39425.1; -; mRNA.
1852
+ DR EMBL; AC068134; AAY24088.1; -; Genomic_DNA.
1853
+ DR EMBL; BC014139; AAH14139.1; -; mRNA.
1854
+ DR EMBL; M19160; AAA51707.1; -; Genomic_DNA.
1855
+ DR EMBL; X07247; CAA30232.1; ALT_SEQ; Genomic_DNA.
1856
+ DR IPI; IPI00290380; -.
1857
+ DR PIR; S12076; S12076.
1858
+ DR RefSeq; NP_112603.2; -.
1859
+ DR UniGene; Hs.333509; -.
1860
+ DR HSSP; P05187; 1EW2.
1861
+ DR SMR; P10696; 20-497.
1862
+ DR Siena-2DPAGE; P10696; -.
1863
+ DR PRIDE; P10696; -.
1864
+ DR Ensembl; ENST00000295453; ENSP00000295453; ENSG00000163286; Homo sapiens.
1865
+ DR GeneID; 251; -.
1866
+ DR KEGG; hsa:251; -.
1867
+ DR NMPDR; fig|9606.3.peg.19513; -.
1868
+ DR UCSC; uc002vss.2; human.
1869
+ DR GeneCards; GC02P232979; -.
1870
+ DR HGNC; HGNC:441; ALPPL2.
1871
+ DR MIM; 171810; gene.
1872
+ DR PharmGKB; PA24731; -.
1873
+ DR HOGENOM; P10696; -.
1874
+ DR HOVERGEN; P10696; -.
1875
+ DR OMA; P10696; VKQSTIA.
1876
+ DR BRENDA; 3.1.3.1; 247.
1877
+ DR DrugBank; DB01143; Amifostine.
1878
+ DR DrugBank; DB00848; Levamisole.
1879
+ DR NextBio; 1005; -.
1880
+ DR ArrayExpress; P10696; -.
1881
+ DR Bgee; P10696; -.
1882
+ DR CleanEx; HS_ALPPL2; -.
1883
+ DR GermOnline; ENSG00000163286; Homo sapiens.
1884
+ DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
1885
+ DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
1886
+ DR GO; GO:0004035; F:alkaline phosphatase activity; NAS:UniProtKB.
1887
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
1888
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
1889
+ DR GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
1890
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
1891
+ DR InterPro; IPR001952; Alkaline_phosphatase.
1892
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
1893
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
1894
+ DR Pfam; PF00245; Alk_phosphatase; 1.
1895
+ DR PRINTS; PR00113; ALKPHPHTASE.
1896
+ DR SMART; SM00098; alkPPc; 1.
1897
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1898
+ PE 1: Evidence at protein level;
1899
+ KW Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
1900
+ KW GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane;
1901
+ KW Metal-binding; Phosphoprotein; Polymorphism; Signal; Zinc.
1902
+ FT SIGNAL 1 19 Potential.
1903
+ FT CHAIN 20 503 Alkaline phosphatase, placental-like.
1904
+ FT /FTId=PRO_0000024033.
1905
+ FT PROPEP 504 532 Removed in mature form (By similarity).
1906
+ FT /FTId=PRO_0000024034.
1907
+ FT ACT_SITE 111 111 Phosphoserine intermediate.
1908
+ FT METAL 61 61 Magnesium (Potential).
1909
+ FT METAL 61 61 Zinc 2 (Potential).
1910
+ FT METAL 330 330 Magnesium (Potential).
1911
+ FT METAL 335 335 Zinc 1 (Potential).
1912
+ FT METAL 339 339 Zinc 1 (Potential).
1913
+ FT METAL 376 376 Zinc 2 (Potential).
1914
+ FT METAL 377 377 Zinc 2 (Potential).
1915
+ FT METAL 451 451 Zinc 1 (Potential).
1916
+ FT LIPID 503 503 GPI-anchor amidated aspartate (By
1917
+ FT similarity).
1918
+ FT CARBOHYD 141 141 N-linked (GlcNAc...) (Potential).
1919
+ FT CARBOHYD 268 268 N-linked (GlcNAc...) (Potential).
1920
+ FT DISULFID 140 202 By similarity.
1921
+ FT DISULFID 486 493 By similarity.
1922
+ FT VARIANT 34 34 Q -> E (in dbSNP:rs1048983).
1923
+ FT /FTId=VAR_027552.
1924
+ FT VARIANT 273 273 L -> M (in dbSNP:rs17416141).
1925
+ FT /FTId=VAR_027553.
1926
+ FT VARIANT 316 316 L -> R (in dbSNP:rs1048992).
1927
+ FT /FTId=VAR_027554.
1928
+ FT VARIANT 527 527 G -> E (in dbSNP:rs1048999).
1929
+ FT /FTId=VAR_027555.
1930
+ FT CONFLICT 57 57 I -> M (in Ref. 1; AAA98616).
1931
+ FT CONFLICT 152 152 M -> V (in Ref. 1; AAA98616 and 4;
1932
+ FT CAA39425).
1933
+ FT CONFLICT 178 178 A -> T (in Ref. 1; AAA98616, 2; AAA51700
1934
+ FT and 4; CAA39425).
1935
+ FT CONFLICT 260 260 H -> R (in Ref. 6; AAH14139).
1936
+ FT CONFLICT 380 380 V -> L (in Ref. 2; AAA51700).
1937
+ FT CONFLICT 498 498 R -> P (in Ref. 1; AAA98616 and 4;
1938
+ FT CAA39425).
1939
+ FT CONFLICT 498 498 R -> S (in Ref. 3; CAA37374).
1940
+ FT CONFLICT 531 531 A -> T (in Ref. 3; CAA37374).
1941
+ SQ SEQUENCE 532 AA; 57377 MW; 25EB56C901B61505 CRC64;
1942
+ MQGPWVLLLL GLRLQLSLGI IPVEEENPDF WNRQAAEALG AAKKLQPAQT AAKNLIIFLG
1943
+ DGMGVSTVTA ARILKGQKKD KLGPETFLAM DRFPYVALSK TYSVDKHVPD SGATATAYLC
1944
+ GVKGNFQTIG LSAAARFNQC NTTRGNEVIS VMNRAKKAGK SVGVVTTTRV QHASPAGAYA
1945
+ HTVNRNWYSD ADVPASARQE GCQDIATQLI SNMDIDVILG GGRKYMFPMG TPDPEYPDDY
1946
+ SQGGTRLDGK NLVQEWLAKH QGARYVWNRT ELLQASLDPS VTHLMGLFEP GDMKYEIHRD
1947
+ STLDPSLMEM TEAALLLLSR NPRGFFLFVE GGRIDHGHHE SRAYRALTET IMFDDAIERA
1948
+ GQLTSEEDTL SLVTADHSHV FSFGGYPLRG SSIFGLAPGK ARDRKAYTVL LYGNGPGYVL
1949
+ KDGARPDVTE SESGSPEYRQ QSAVPLDGET HAGEDVAVFA RGPQAHLVHG VQEQTFIAHV
1950
+ MAFAACLEPY TACDLAPRAG TTDAAHPGPS VVPALLPLLA GTLLLLGTAT AP
1951
+ //
1952
+ ID PPB4_BACSU Reviewed; 461 AA.
1953
+ AC P19406;
1954
+ DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
1955
+ DT 16-JUN-2009, sequence version 4.
1956
+ DT 07-JUL-2009, entry version 83.
1957
+ DE RecName: Full=Alkaline phosphatase 4;
1958
+ DE EC=3.1.3.1;
1959
+ DE AltName: Full=Alkaline phosphatase IV;
1960
+ DE Short=APase IV;
1961
+ DE Flags: Precursor;
1962
+ GN Name=phoA; Synonyms=phoAIV; OrderedLocusNames=BSU09410;
1963
+ OS Bacillus subtilis.
1964
+ OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
1965
+ OX NCBI_TaxID=1423;
1966
+ RN [1]
1967
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
1968
+ RC STRAIN=168 / JH642;
1969
+ RX MEDLINE=94156839; PubMed=8113174;
1970
+ RA Hulett F.M., Lee J., Shi L., Sun G., Chesnut R., Sharkova E.,
1971
+ RA Duggan M.F., Kapp N.;
1972
+ RT "Sequential action of two-component genetic switches regulates the PHO
1973
+ RT regulon in Bacillus subtilis.";
1974
+ RL J. Bacteriol. 176:1348-1358(1994).
1975
+ RN [2]
1976
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
1977
+ RC STRAIN=168;
1978
+ RX MEDLINE=98240224; PubMed=9579061;
1979
+ RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R.,
1980
+ RA Wedler H., Venema G., Bron S.;
1981
+ RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the
1982
+ RT Bacillus subtilis chromosome contains several dysfunctional genes, the
1983
+ RT glyB marker, many genes encoding transporter proteins, and the
1984
+ RT ubiquitous hit gene.";
1985
+ RL Microbiology 144:859-875(1998).
1986
+ RN [3]
1987
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
1988
+ RC STRAIN=168;
1989
+ RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
1990
+ RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
1991
+ RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
1992
+ RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
1993
+ RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
1994
+ RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
1995
+ RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
1996
+ RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
1997
+ RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
1998
+ RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
1999
+ RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
2000
+ RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
2001
+ RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
2002
+ RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
2003
+ RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
2004
+ RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
2005
+ RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
2006
+ RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
2007
+ RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
2008
+ RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
2009
+ RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
2010
+ RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
2011
+ RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
2012
+ RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
2013
+ RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
2014
+ RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
2015
+ RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
2016
+ RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
2017
+ RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
2018
+ RA Yoshikawa H., Danchin A.;
2019
+ RT "The complete genome sequence of the Gram-positive bacterium Bacillus
2020
+ RT subtilis.";
2021
+ RL Nature 390:249-256(1997).
2022
+ RN [4]
2023
+ RP SEQUENCE REVISION TO 208.
2024
+ RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
2025
+ RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
2026
+ RA Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
2027
+ RT "From a consortium sequence to a unified sequence: the Bacillus
2028
+ RT subtilis 168 reference genome a decade later.";
2029
+ RL Microbiology 155:1758-1775(2009).
2030
+ RN [5]
2031
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-461.
2032
+ RC STRAIN=168 / JH642;
2033
+ RX MEDLINE=91093215; PubMed=1898729;
2034
+ RA Hulett F.M., Kim M.E., Bookstein C., Kapp N.V., Edwards C.W.,
2035
+ RA Wyckoff H.W.;
2036
+ RT "Bacillus subtilis alkaline phosphatases III and IV. Cloning,
2037
+ RT sequencing, and comparisons of deduced amino acid sequence with
2038
+ RT Escherichia coli alkaline phosphatase three-dimensional structure.";
2039
+ RL J. Biol. Chem. 266:1077-1084(1991).
2040
+ RN [6]
2041
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-142.
2042
+ RC STRAIN=168 / JH642;
2043
+ RX MEDLINE=91092508; PubMed=2125017; DOI=10.1016/0378-1119(90)90346-S;
2044
+ RA Kapp N.V., Edwards C.W., Chesnut R.S., Hulett F.M.;
2045
+ RT "The Bacillus subtilis phoAIV gene: effects of in vitro inactivation
2046
+ RT on total alkaline phosphatase production.";
2047
+ RL Gene 96:95-100(1990).
2048
+ RN [7]
2049
+ RP PROTEIN SEQUENCE OF 42-63.
2050
+ RX MEDLINE=90130309; PubMed=2105301;
2051
+ RA Hulett F.M., Bookstein C., Jensen K.;
2052
+ RT "Evidence for two structural genes for alkaline phosphatase in
2053
+ RT Bacillus subtilis.";
2054
+ RL J. Bacteriol. 172:735-740(1990).
2055
+ RN [8]
2056
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 433-461.
2057
+ RC STRAIN=168 / Marburg;
2058
+ RX MEDLINE=94193548; PubMed=8144469;
2059
+ RA Beall B.W., Moran C.P. Jr.;
2060
+ RT "Cloning and characterization of spoVR, a gene from Bacillus subtilis
2061
+ RT involved in spore cortex formation.";
2062
+ RL J. Bacteriol. 176:2003-2012(1994).
2063
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
2064
+ CC phosphate.
2065
+ CC -!- COFACTOR: Binds 1 magnesium ion.
2066
+ CC -!- COFACTOR: Binds 2 zinc ions.
2067
+ CC -!- SUBUNIT: Monomer.
2068
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
2069
+ CC -----------------------------------------------------------------------
2070
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
2071
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
2072
+ CC -----------------------------------------------------------------------
2073
+ DR EMBL; U02550; AAA18323.1; -; Unassigned_DNA.
2074
+ DR EMBL; Y14082; CAA74486.1; -; Genomic_DNA.
2075
+ DR EMBL; AL009126; CAB12780.2; -; Genomic_DNA.
2076
+ DR EMBL; L26337; AAA22812.1; -; Genomic_DNA.
2077
+ DR PIR; B69676; B69676.
2078
+ DR RefSeq; NP_388822.1; -.
2079
+ DR HSSP; P00634; 1AJA.
2080
+ DR GeneID; 936265; -.
2081
+ DR GenomeReviews; AL009126_GR; BSU09410.
2082
+ DR KEGG; bsu:BSU09410; -.
2083
+ DR NMPDR; fig|224308.1.peg.941; -.
2084
+ DR SubtiList; BG10183; phoA.
2085
+ DR HOGENOM; P19406; -.
2086
+ DR OMA; P19406; YTIARGY.
2087
+ DR BioCyc; BSUB224308:BSU0941-MON; -.
2088
+ DR BRENDA; 3.1.3.1; 150.
2089
+ DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:EC.
2090
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
2091
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
2092
+ DR GO; GO:0008152; P:metabolic process; IEA:InterPro.
2093
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
2094
+ DR InterPro; IPR001952; Alkaline_phosphatase.
2095
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
2096
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
2097
+ DR Pfam; PF00245; Alk_phosphatase; 1.
2098
+ DR PRINTS; PR00113; ALKPHPHTASE.
2099
+ DR SMART; SM00098; alkPPc; 1.
2100
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
2101
+ PE 1: Evidence at protein level;
2102
+ KW Complete proteome; Direct protein sequencing; Hydrolase; Magnesium;
2103
+ KW Metal-binding; Phosphoprotein; Signal; Zinc.
2104
+ FT SIGNAL 1 41
2105
+ FT CHAIN 42 461 Alkaline phosphatase 4.
2106
+ FT /FTId=PRO_0000024011.
2107
+ FT ACT_SITE 108 108 Phosphoserine intermediate (By
2108
+ FT similarity).
2109
+ FT METAL 58 58 Magnesium (By similarity).
2110
+ FT METAL 58 58 Zinc 2 (By similarity).
2111
+ FT METAL 161 161 Magnesium (By similarity).
2112
+ FT METAL 282 282 Magnesium (By similarity).
2113
+ FT METAL 287 287 Zinc 1 (By similarity).
2114
+ FT METAL 291 291 Zinc 1 (By similarity).
2115
+ FT METAL 329 329 Zinc 2 (By similarity).
2116
+ FT METAL 330 330 Zinc 2 (By similarity).
2117
+ FT METAL 423 423 Zinc 1 (By similarity).
2118
+ FT CONFLICT 50 50 R -> K (in Ref. 7; AA sequence).
2119
+ FT CONFLICT 208 208 D -> N (in Ref. 1; AAA18323, 2; CAA74486
2120
+ FT and 5).
2121
+ SQ SEQUENCE 461 AA; 50274 MW; A2AD9309026889FE CRC64;
2122
+ MKKMSLFQNM KSKLLPIAAV SVLTAGIFAG AELQQTEKAS AKKQDKAEIR NVIVMIGDGM
2123
+ GTPYIRAYRS MKNNGDTPNN PKLTEFDRNL TGMMMTHPDD PDYNITDSAA AGTALATGVK
2124
+ TYNNAIGVDK NGKKVKSVLE EAKQQGKSTG LVATSEINHA TPAAYGAHNE SRKNMDQIAN
2125
+ SYMDDKIKGK HKIDVLLGGG KSYFNRKDRN LTKEFKQAGY SYVTTKQALK KNKDQQVLGL
2126
+ FADGGLAKAL DRDSKTPSLK DMTVSAIDRL NQNKKGFFLM VEGSQIDWAA HDNDTVGAMS
2127
+ EVKDFEQAYK AAIEFAKKDK HTLVIATADH TTGGFTIGAN GEKNWHAEPI LSAKKTPEFM
2128
+ AKKISEGKPV KDVLARYANL KVTSEEIKSV EAAAQADKSK GASKAIIKIF NTRSNSGWTS
2129
+ TDHTGEEVPV YAYGPGKEKF RGLINNTDQA NIIFKILKTG K
2130
+ //
2131
+ ID PPB3_BACSU Reviewed; 462 AA.
2132
+ AC P19405; O05498;
2133
+ DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
2134
+ DT 07-JUL-2009, sequence version 4.
2135
+ DT 07-JUL-2009, entry version 80.
2136
+ DE RecName: Full=Alkaline phosphatase 3;
2137
+ DE EC=3.1.3.1;
2138
+ DE AltName: Full=Alkaline phosphatase III;
2139
+ DE Short=APase III;
2140
+ DE Flags: Precursor;
2141
+ GN Name=phoB; Synonyms=phoAIII; OrderedLocusNames=BSU05740;
2142
+ OS Bacillus subtilis.
2143
+ OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
2144
+ OX NCBI_TaxID=1423;
2145
+ RN [1]
2146
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
2147
+ RC STRAIN=168;
2148
+ RX MEDLINE=91093215; PubMed=1898729;
2149
+ RA Hulett F.M., Kim M.E., Bookstein C., Kapp N.V., Edwards C.W.,
2150
+ RA Wyckoff H.W.;
2151
+ RT "Bacillus subtilis alkaline phosphatases III and IV. Cloning,
2152
+ RT sequencing, and comparisons of deduced amino acid sequence with
2153
+ RT Escherichia coli alkaline phosphatase three-dimensional structure.";
2154
+ RL J. Biol. Chem. 266:1077-1084(1991).
2155
+ RN [2]
2156
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
2157
+ RC STRAIN=168 / JH642;
2158
+ RX MEDLINE=97346038; PubMed=9202461;
2159
+ RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
2160
+ RA Ogasawara N.;
2161
+ RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of
2162
+ RT the Bacillus subtilis chromosome.";
2163
+ RL Microbiology 143:1861-1866(1997).
2164
+ RN [3]
2165
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
2166
+ RC STRAIN=168;
2167
+ RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
2168
+ RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
2169
+ RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
2170
+ RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
2171
+ RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
2172
+ RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
2173
+ RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
2174
+ RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
2175
+ RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
2176
+ RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
2177
+ RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
2178
+ RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
2179
+ RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
2180
+ RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
2181
+ RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
2182
+ RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
2183
+ RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
2184
+ RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
2185
+ RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
2186
+ RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
2187
+ RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
2188
+ RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
2189
+ RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
2190
+ RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
2191
+ RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
2192
+ RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
2193
+ RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
2194
+ RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
2195
+ RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
2196
+ RA Yoshikawa H., Danchin A.;
2197
+ RT "The complete genome sequence of the Gram-positive bacterium Bacillus
2198
+ RT subtilis.";
2199
+ RL Nature 390:249-256(1997).
2200
+ RN [4]
2201
+ RP SEQUENCE REVISION TO 334.
2202
+ RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
2203
+ RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
2204
+ RA Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
2205
+ RT "From a consortium sequence to a unified sequence: the Bacillus
2206
+ RT subtilis 168 reference genome a decade later.";
2207
+ RL Microbiology 155:1758-1775(2009).
2208
+ RN [5]
2209
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
2210
+ RC STRAIN=168;
2211
+ RX MEDLINE=90299794; PubMed=2113910;
2212
+ RA Bookstein C., Edwards C.W., Kapp N.V., Hulett F.M.;
2213
+ RT "The Bacillus subtilis 168 alkaline phosphatase III gene: impact of a
2214
+ RT phoAIII mutation on total alkaline phosphatase synthesis.";
2215
+ RL J. Bacteriol. 172:3730-3737(1990).
2216
+ RN [6]
2217
+ RP PROTEIN SEQUENCE OF 33-62.
2218
+ RX MEDLINE=90130309; PubMed=2105301;
2219
+ RA Hulett F.M., Bookstein C., Jensen K.;
2220
+ RT "Evidence for two structural genes for alkaline phosphatase in
2221
+ RT Bacillus subtilis.";
2222
+ RL J. Bacteriol. 172:735-740(1990).
2223
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
2224
+ CC phosphate.
2225
+ CC -!- COFACTOR: Binds 1 magnesium ion.
2226
+ CC -!- COFACTOR: Binds 2 zinc ions.
2227
+ CC -!- SUBUNIT: Monomer.
2228
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
2229
+ CC -----------------------------------------------------------------------
2230
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
2231
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
2232
+ CC -----------------------------------------------------------------------
2233
+ DR EMBL; D88802; BAA19698.1; -; Genomic_DNA.
2234
+ DR EMBL; AL009126; CAB12393.2; -; Genomic_DNA.
2235
+ DR EMBL; M33634; AAA22658.1; -; Genomic_DNA.
2236
+ DR PIR; C69676; C69676.
2237
+ DR RefSeq; NP_388455.1; -.
2238
+ DR HSSP; P00634; 1AJA.
2239
+ DR GeneID; 938004; -.
2240
+ DR GenomeReviews; AL009126_GR; BSU05740.
2241
+ DR KEGG; bsu:BSU05740; -.
2242
+ DR NMPDR; fig|224308.1.peg.574; -.
2243
+ DR SubtiList; BG10697; phoB.
2244
+ DR HOGENOM; P19405; -.
2245
+ DR OMA; P19405; SEITHAT.
2246
+ DR BioCyc; BSUB224308:BSU0574-MON; -.
2247
+ DR BRENDA; 3.1.3.1; 150.
2248
+ DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:EC.
2249
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
2250
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
2251
+ DR GO; GO:0008152; P:metabolic process; IEA:InterPro.
2252
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
2253
+ DR InterPro; IPR001952; Alkaline_phosphatase.
2254
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
2255
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
2256
+ DR Pfam; PF00245; Alk_phosphatase; 1.
2257
+ DR PRINTS; PR00113; ALKPHPHTASE.
2258
+ DR SMART; SM00098; alkPPc; 1.
2259
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
2260
+ PE 1: Evidence at protein level;
2261
+ KW Complete proteome; Direct protein sequencing; Hydrolase; Magnesium;
2262
+ KW Metal-binding; Phosphoprotein; Signal; Zinc.
2263
+ FT SIGNAL 1 32
2264
+ FT CHAIN 33 462 Alkaline phosphatase 3.
2265
+ FT /FTId=PRO_0000024010.
2266
+ FT ACT_SITE 101 101 Phosphoserine intermediate (By
2267
+ FT similarity).
2268
+ FT METAL 52 52 Magnesium (By similarity).
2269
+ FT METAL 52 52 Zinc 2 (By similarity).
2270
+ FT METAL 154 154 Magnesium (By similarity).
2271
+ FT METAL 275 275 Magnesium (By similarity).
2272
+ FT METAL 280 280 Zinc 1 (By similarity).
2273
+ FT METAL 284 284 Zinc 1 (By similarity).
2274
+ FT METAL 322 322 Zinc 2 (By similarity).
2275
+ FT METAL 323 323 Zinc 2 (By similarity).
2276
+ FT METAL 419 419 Zinc 1 (By similarity).
2277
+ FT CONFLICT 215 215 Y -> S (in Ref. 1).
2278
+ FT CONFLICT 234 235 FA -> LP (in Ref. 1).
2279
+ FT CONFLICT 334 334 G -> S (in Ref. 2; BAA19698).
2280
+ SQ SEQUENCE 462 AA; 50494 MW; CB0F8FB855D17231 CRC64;
2281
+ MKKFPKKLLP IAVLSSIAFS SLASGSVPEA SAQEKKKGNQ DEIKNVIVLI GDGMGVSYTS
2282
+ AYRYLKDNKK TKVVEPTAFD QYLVGQQTTY PDDPEQNVTD SAAAATAMSA GIKTYNNAIA
2283
+ VDNDGSEAKT VLEAAKEKGK ATGLVATSEI THATPASFGS HDHSRKNMNS IADDYFDEMV
2284
+ NGKHKIDVLL GGGKSNFDRK DRNLIKEFKK AGYSYVDDRK DMLKNKDSQV LGLFADGGLP
2285
+ KKIDRTKDIP SLKDMTNTAI KKLNKDKDGF FLMVEGSQID WAGHDNDIVG AMSEMEDFEQ
2286
+ AYKAAIDFAK KDKHTLVVAT ADHSTGGYSI GADGIYNWFS EPIKAAKRTP DFMAEKIADG
2287
+ ADVEKTLKTY IDQKKLALTK AEIQSVEEAA KSKEVLDIDN AIENIFNKRS HTGWTTGGHT
2288
+ GEDVPVYAYG PSSETFAGQI DNTEIAKNVF KALQYNIKIN DK
2289
+ //
2290
+ ID PPBT_RAT Reviewed; 524 AA.
2291
+ AC P08289; P14055; P70707;
2292
+ DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
2293
+ DT 01-MAY-1992, sequence version 2.
2294
+ DT 28-JUL-2009, entry version 88.
2295
+ DE RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme;
2296
+ DE EC=3.1.3.1;
2297
+ DE AltName: Full=AP-TNAP;
2298
+ DE AltName: Full=TNSALP;
2299
+ DE AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme;
2300
+ DE Flags: Precursor;
2301
+ GN Name=Alpl;
2302
+ OS Rattus norvegicus (Rat).
2303
+ OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
2304
+ OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
2305
+ OC Muroidea; Muridae; Murinae; Rattus.
2306
+ OX NCBI_TaxID=10116;
2307
+ RN [1]
2308
+ RP NUCLEOTIDE SEQUENCE [MRNA].
2309
+ RC TISSUE=Placenta;
2310
+ RX MEDLINE=88124833; PubMed=3422431; DOI=10.1073/pnas.85.2.319;
2311
+ RA Thiede M.A., Yoon K., Golub E.E., Noda M., Rodan G.A.;
2312
+ RT "Structure and expression of rat osteosarcoma (ROS 17/2.8) alkaline
2313
+ RT phosphatase: product of a single copy gene.";
2314
+ RL Proc. Natl. Acad. Sci. U.S.A. 85:319-323(1988).
2315
+ RN [2]
2316
+ RP NUCLEOTIDE SEQUENCE [MRNA].
2317
+ RC STRAIN=Wistar; TISSUE=Liver;
2318
+ RX MEDLINE=88183256; PubMed=2895632;
2319
+ RA Misumi Y., Tashiro K., Hattori M., Sakaki Y., Ikehara Y.;
2320
+ RT "Primary structure of rat liver alkaline phosphatase deduced from its
2321
+ RT cDNA.";
2322
+ RL Biochem. J. 249:661-668(1988).
2323
+ RN [3]
2324
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
2325
+ RC STRAIN=Sprague-Dawley; TISSUE=Liver;
2326
+ RX MEDLINE=89289705; PubMed=2544423;
2327
+ RX DOI=10.1111/j.1432-1033.1989.tb14822.x;
2328
+ RA Toh Y., Yamamoto M., Endo H., Misumi Y., Ikehara Y.;
2329
+ RT "Isolation and characterization of a rat liver alkaline phosphatase
2330
+ RT gene. A single gene with two promoters.";
2331
+ RL Eur. J. Biochem. 182:231-237(1989).
2332
+ RN [4]
2333
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
2334
+ RC TISSUE=Kidney;
2335
+ RX PubMed=15489334; DOI=10.1101/gr.2596504;
2336
+ RG The MGC Project Team;
2337
+ RT "The status, quality, and expansion of the NIH full-length cDNA
2338
+ RT project: the Mammalian Gene Collection (MGC).";
2339
+ RL Genome Res. 14:2121-2127(2004).
2340
+ RN [5]
2341
+ RP PROTEIN SEQUENCE OF 18-47, AND GPI-ANCHOR.
2342
+ RC TISSUE=Liver;
2343
+ RX MEDLINE=88198083; PubMed=2834351;
2344
+ RA Ogata S., Hayashi Y., Yasutake K., Ikehara Y.;
2345
+ RT "Chemical identification of lipid components in the membranous form of
2346
+ RT rat liver alkaline phosphatase.";
2347
+ RL J. Biochem. 102:1609-1615(1987).
2348
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
2349
+ CC phosphate.
2350
+ CC -!- COFACTOR: Binds 1 magnesium ion (By similarity).
2351
+ CC -!- COFACTOR: Binds 2 zinc ions (By similarity).
2352
+ CC -!- SUBUNIT: Homodimer.
2353
+ CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
2354
+ CC -!- MISCELLANEOUS: In most mammals there are four different isozymes:
2355
+ CC placental, placental-like, intestinal and tissue non-specific
2356
+ CC (liver/bone/kidney).
2357
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
2358
+ CC -----------------------------------------------------------------------
2359
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
2360
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
2361
+ CC -----------------------------------------------------------------------
2362
+ DR EMBL; Y00714; CAA68703.1; -; mRNA.
2363
+ DR EMBL; J03572; AAA41845.1; -; mRNA.
2364
+ DR EMBL; X16028; CAA34160.1; -; Genomic_DNA.
2365
+ DR EMBL; X16029; CAA34160.1; JOINED; Genomic_DNA.
2366
+ DR EMBL; X16030; CAA34160.1; JOINED; Genomic_DNA.
2367
+ DR EMBL; X16031; CAA34160.1; JOINED; Genomic_DNA.
2368
+ DR EMBL; X16032; CAA34160.1; JOINED; Genomic_DNA.
2369
+ DR EMBL; X16033; CAA34160.1; JOINED; Genomic_DNA.
2370
+ DR EMBL; X16034; CAA34160.1; JOINED; Genomic_DNA.
2371
+ DR EMBL; X16035; CAA34160.1; JOINED; Genomic_DNA.
2372
+ DR EMBL; X16036; CAA34160.1; JOINED; Genomic_DNA.
2373
+ DR EMBL; X16037; CAA34160.1; JOINED; Genomic_DNA.
2374
+ DR EMBL; X16038; CAA34160.1; JOINED; Genomic_DNA.
2375
+ DR EMBL; BC088399; AAH88399.1; -; mRNA.
2376
+ DR IPI; IPI00327143; -.
2377
+ DR PIR; A28114; A28114.
2378
+ DR PIR; S00289; S00289.
2379
+ DR RefSeq; NP_037191.1; -.
2380
+ DR UniGene; Rn.82764; -.
2381
+ DR HSSP; P05187; 1EW2.
2382
+ DR GlycoSuiteDB; P08289; -.
2383
+ DR PhosphoSite; P08289; -.
2384
+ DR Ensembl; ENSRNOT00000019004; ENSRNOP00000019004; ENSRNOG00000013954; Rattus norvegicus.
2385
+ DR GeneID; 25586; -.
2386
+ DR KEGG; rno:25586; -.
2387
+ DR NMPDR; fig|10116.3.peg.24200; -.
2388
+ DR UCSC; NM_013059; rat.
2389
+ DR RGD; 2100; Alpl.
2390
+ DR HOVERGEN; P08289; -.
2391
+ DR OMA; P08289; MISPFLV.
2392
+ DR BRENDA; 3.1.3.1; 248.
2393
+ DR NextBio; 607251; -.
2394
+ DR ArrayExpress; P08289; -.
2395
+ DR GermOnline; ENSRNOG00000013954; Rattus norvegicus.
2396
+ DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
2397
+ DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
2398
+ DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:RGD.
2399
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
2400
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
2401
+ DR GO; GO:0008152; P:metabolic process; IEA:InterPro.
2402
+ DR GO; GO:0051384; P:response to glucocorticoid stimulus; IDA:RGD.
2403
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
2404
+ DR InterPro; IPR001952; Alkaline_phosphatase.
2405
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
2406
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
2407
+ DR Pfam; PF00245; Alk_phosphatase; 1.
2408
+ DR PRINTS; PR00113; ALKPHPHTASE.
2409
+ DR SMART; SM00098; alkPPc; 1.
2410
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
2411
+ PE 1: Evidence at protein level;
2412
+ KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
2413
+ KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
2414
+ KW Phosphoprotein; Signal; Zinc.
2415
+ FT SIGNAL 1 17
2416
+ FT CHAIN 18 501 Alkaline phosphatase, tissue-nonspecific
2417
+ FT isozyme.
2418
+ FT /FTId=PRO_0000024027.
2419
+ FT PROPEP 502 524 Removed in mature form (Potential).
2420
+ FT /FTId=PRO_0000024028.
2421
+ FT ACT_SITE 110 110 Phosphoserine intermediate.
2422
+ FT METAL 60 60 Magnesium (Potential).
2423
+ FT METAL 60 60 Zinc 2 (Potential).
2424
+ FT METAL 173 173 Magnesium (Potential).
2425
+ FT METAL 332 332 Magnesium (Potential).
2426
+ FT METAL 337 337 Zinc 1 (Potential).
2427
+ FT METAL 341 341 Zinc 1 (Potential).
2428
+ FT METAL 378 378 Zinc 2 (Potential).
2429
+ FT METAL 379 379 Zinc 2 (Potential).
2430
+ FT METAL 454 454 Zinc 1 (Potential).
2431
+ FT LIPID 501 501 GPI-anchor amidated serine (Potential).
2432
+ FT CARBOHYD 140 140 N-linked (GlcNAc...) (Potential).
2433
+ FT CARBOHYD 230 230 N-linked (GlcNAc...) (Potential).
2434
+ FT CARBOHYD 271 271 N-linked (GlcNAc...) (Potential).
2435
+ FT CARBOHYD 303 303 N-linked (GlcNAc...) (Potential).
2436
+ FT CARBOHYD 430 430 N-linked (GlcNAc...) (Potential).
2437
+ FT CONFLICT 12 12 T -> P (in Ref. 1; AAA41845).
2438
+ FT CONFLICT 116 116 A -> Y (in Ref. 2).
2439
+ FT CONFLICT 193 193 P -> R (in Ref. 1; AAA41845).
2440
+ FT CONFLICT 234 234 V -> E (in Ref. 2; CAA68703).
2441
+ FT CONFLICT 254 254 S -> T (in Ref. 2; CAA68703).
2442
+ FT CONFLICT 331 331 V -> E (in Ref. 2; CAA68703).
2443
+ FT CONFLICT 374 374 V -> L (in Ref. 2; CAA68703).
2444
+ FT CONFLICT 380 388 SHVFTFGGY -> HPTFSRLVA (in Ref. 2).
2445
+ FT CONFLICT 391 391 R -> Q (in Ref. 2).
2446
+ FT CONFLICT 463 463 A -> C (in Ref. 2; CAA68703).
2447
+ FT CONFLICT 474 474 V -> I (in Ref. 2; CAA68703).
2448
+ SQ SEQUENCE 524 AA; 57659 MW; BD75A4B87117DF03 CRC64;
2449
+ MILPFLVLAI GTCLTNSFVP EKEKDPSYWR QQAQETLKNA LKLQKLNTNV AKNIIMFLGD
2450
+ GMGVSTVTAA RILKGQLHHN TGEETRLEMD KFPFVALSKT YNTNAQVPDS AGTATAYLCG
2451
+ VKANEGTVGV SAATERTRCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSAAYAH
2452
+ SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIKDIDVIMG GGRKYMYPKN RTDVEYELDE
2453
+ KARGTRLDGL DLISIWKSFK PRHKHSHYVW NRTELLALDP SRVDYLLGLF EPGDMQYELN
2454
+ RNNLTDPSLS EMVEVALRIL TKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDEAIG
2455
+ KAGTMTSQKD TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MVSDTDKKPF TAILYGNGPG
2456
+ YKVVDGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFAKGPMAHL LHGVHEQNYI
2457
+ PHVMAYASCI GANLDHCAWA SSASSPSPGA LLLPLALFPL RTLF
2458
+ //
2459
+ ID PPB_YEAST Reviewed; 566 AA.
2460
+ AC P11491; Q03374;
2461
+ DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
2462
+ DT 15-JUL-1998, sequence version 2.
2463
+ DT 28-JUL-2009, entry version 96.
2464
+ DE RecName: Full=Repressible alkaline phosphatase;
2465
+ DE EC=3.1.3.1;
2466
+ DE Flags: Precursor;
2467
+ GN Name=PHO8; OrderedLocusNames=YDR481C; ORFNames=D8035.24;
2468
+ OS Saccharomyces cerevisiae (Baker's yeast).
2469
+ OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
2470
+ OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
2471
+ OX NCBI_TaxID=4932;
2472
+ RN [1]
2473
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
2474
+ RC STRAIN=P-28-24C;
2475
+ RX MEDLINE=88084440; PubMed=3319783; DOI=10.1016/0378-1119(87)90036-9;
2476
+ RA Kaneko Y., Hayashi N., Toh-e A., Banno I., Oshima Y.;
2477
+ RT "Structural characteristics of the PHO8 gene encoding repressible
2478
+ RT alkaline phosphatase in Saccharomyces cerevisiae.";
2479
+ RL Gene 58:137-148(1987).
2480
+ RN [2]
2481
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
2482
+ RC STRAIN=ATCC 204508 / S288c;
2483
+ RX MEDLINE=97313263; PubMed=9169867;
2484
+ RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
2485
+ RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
2486
+ RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
2487
+ RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
2488
+ RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
2489
+ RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
2490
+ RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
2491
+ RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
2492
+ RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
2493
+ RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
2494
+ RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
2495
+ RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
2496
+ RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
2497
+ RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
2498
+ RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
2499
+ RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
2500
+ RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
2501
+ RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
2502
+ RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
2503
+ RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
2504
+ RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
2505
+ RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
2506
+ RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
2507
+ RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
2508
+ RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
2509
+ RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
2510
+ RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
2511
+ RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
2512
+ RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
2513
+ RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
2514
+ RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
2515
+ RA Mewes H.-W., Zollner A., Zaccaria P.;
2516
+ RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
2517
+ RL Nature 387:75-78(1997).
2518
+ RN [3]
2519
+ RP PROTEIN SEQUENCE OF 1-10, TOPOLOGY, AND SUBCELLULAR LOCATION.
2520
+ RX MEDLINE=90005428; PubMed=2676517;
2521
+ RA Klionsky D.J., Emr S.D.;
2522
+ RT "Membrane protein sorting: biosynthesis, transport and processing of
2523
+ RT yeast vacuolar alkaline phosphatase.";
2524
+ RL EMBO J. 8:2241-2250(1989).
2525
+ RN [4]
2526
+ RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
2527
+ RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
2528
+ RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
2529
+ RA Dephoure N., O'Shea E.K., Weissman J.S.;
2530
+ RT "Global analysis of protein expression in yeast.";
2531
+ RL Nature 425:737-741(2003).
2532
+ RN [5]
2533
+ RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASS
2534
+ RP SPECTROMETRY.
2535
+ RX PubMed=17330950; DOI=10.1021/pr060559j;
2536
+ RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
2537
+ RA Elias J.E., Gygi S.P.;
2538
+ RT "Large-scale phosphorylation analysis of alpha-factor-arrested
2539
+ RT Saccharomyces cerevisiae.";
2540
+ RL J. Proteome Res. 6:1190-1197(2007).
2541
+ RN [6]
2542
+ RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123 AND
2543
+ RP THR-128, AND MASS SPECTROMETRY.
2544
+ RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
2545
+ RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
2546
+ RT "A multidimensional chromatography technology for in-depth
2547
+ RT phosphoproteome analysis.";
2548
+ RL Mol. Cell. Proteomics 7:1389-1396(2008).
2549
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
2550
+ CC phosphate.
2551
+ CC -!- COFACTOR: Binds 1 magnesium ion (By similarity).
2552
+ CC -!- COFACTOR: Binds 2 zinc ions (By similarity).
2553
+ CC -!- INTERACTION:
2554
+ CC P40016:RPN3; NbExp=1; IntAct=EBI-13762, EBI-15927;
2555
+ CC P10591:SSA1; NbExp=1; IntAct=EBI-13762, EBI-8591;
2556
+ CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Single-pass membrane
2557
+ CC protein (Potential). Note=Lysosome-like vacuoles.
2558
+ CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD
2559
+ CC medium.
2560
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
2561
+ CC -----------------------------------------------------------------------
2562
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
2563
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
2564
+ CC -----------------------------------------------------------------------
2565
+ DR EMBL; M21134; AAA34871.1; -; Genomic_DNA.
2566
+ DR EMBL; U33050; AAB64930.1; -; Genomic_DNA.
2567
+ DR PIR; S69648; S69648.
2568
+ DR RefSeq; NP_010769.1; -.
2569
+ DR HSSP; P00634; 1KH5.
2570
+ DR IntAct; P11491; 4.
2571
+ DR PeptideAtlas; P11491; -.
2572
+ DR Ensembl; YDR481C; YDR481C; YDR481C; Saccharomyces cerevisiae.
2573
+ DR GeneID; 852092; -.
2574
+ DR GenomeReviews; Z71256_GR; YDR481C.
2575
+ DR KEGG; sce:YDR481C; -.
2576
+ DR NMPDR; fig|4932.3.peg.1542; -.
2577
+ DR CYGD; YDR481c; -.
2578
+ DR SGD; S000002889; PHO8.
2579
+ DR HOGENOM; P11491; -.
2580
+ DR OMA; P11491; SEITHAT.
2581
+ DR BRENDA; 3.1.3.1; 250.
2582
+ DR NextBio; 970421; -.
2583
+ DR ArrayExpress; P11491; -.
2584
+ DR GermOnline; YDR481C; Saccharomyces cerevisiae.
2585
+ DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
2586
+ DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
2587
+ DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:SGD.
2588
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
2589
+ DR GO; GO:0005515; F:protein binding; IPI:IntAct.
2590
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
2591
+ DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA:SGD.
2592
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
2593
+ DR InterPro; IPR001952; Alkaline_phosphatase.
2594
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
2595
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
2596
+ DR Pfam; PF00245; Alk_phosphatase; 1.
2597
+ DR PRINTS; PR00113; ALKPHPHTASE.
2598
+ DR SMART; SM00098; alkPPc; 1.
2599
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
2600
+ PE 1: Evidence at protein level;
2601
+ KW Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase;
2602
+ KW Magnesium; Membrane; Metal-binding; Phosphoprotein; Transmembrane;
2603
+ KW Vacuole; Zinc.
2604
+ FT CHAIN 1 ? Repressible alkaline phosphatase.
2605
+ FT /FTId=PRO_0000024017.
2606
+ FT PROPEP ? 566 Removed in mature form.
2607
+ FT /FTId=PRO_0000024018.
2608
+ FT TOPO_DOM 1 33 Cytoplasmic.
2609
+ FT TRANSMEM 34 59 Potential.
2610
+ FT TOPO_DOM 60 ? Vacuolar.
2611
+ FT ACT_SITE 123 123 Phosphoserine intermediate (By
2612
+ FT similarity).
2613
+ FT METAL 75 75 Magnesium (By similarity).
2614
+ FT METAL 75 75 Zinc 2 (By similarity).
2615
+ FT METAL 174 174 Magnesium (By similarity).
2616
+ FT METAL 176 176 Magnesium (By similarity).
2617
+ FT METAL 325 325 Magnesium (By similarity).
2618
+ FT METAL 330 330 Zinc 1 (By similarity).
2619
+ FT METAL 334 334 Zinc 1 (By similarity).
2620
+ FT METAL 373 373 Zinc 2 (By similarity).
2621
+ FT METAL 374 374 Zinc 2 (By similarity).
2622
+ FT METAL 484 484 Zinc 1 (By similarity).
2623
+ FT MOD_RES 121 121 Phosphothreonine.
2624
+ FT MOD_RES 123 123 Phosphoserine.
2625
+ FT MOD_RES 128 128 Phosphothreonine.
2626
+ FT CARBOHYD 268 268 N-linked (GlcNAc...).
2627
+ FT CARBOHYD 401 401 N-linked (GlcNAc...).
2628
+ FT CONFLICT 5 5 T -> R (in Ref. 1; AAA34871).
2629
+ FT CONFLICT 55 55 S -> T (in Ref. 1; AAA34871).
2630
+ FT CONFLICT 59 59 L -> I (in Ref. 1; AAA34871).
2631
+ FT CONFLICT 132 132 C -> S (in Ref. 1; AAA34871).
2632
+ FT CONFLICT 271 271 L -> F (in Ref. 1; AAA34871).
2633
+ FT CONFLICT 447 447 D -> E (in Ref. 1; AAA34871).
2634
+ SQ SEQUENCE 566 AA; 63004 MW; 9FA2E87B068FF0DB CRC64;
2635
+ MMTHTLPSEQ TRLVPGSDSS SRPKKRRISK RSKIIVSTVV CIGLLLVLVQ LAFPSSFALR
2636
+ SASHKKKNVI FFVTDGMGPA SLSMARSFNQ HVNDLPIDDI LTLDEHFIGS SRTRSSDSLV
2637
+ TDSAAGATAF ACALKSYNGA IGVDPHHRPC GTVLEAAKLA GYLTGLVVTT RITDATPASF
2638
+ SSHVDYRWQE DLIATHQLGE YPLGRVVDLL MGGGRSHFYP QGEKASPYGH HGARKDGRDL
2639
+ IDEAQSNGWQ YVGDRKNFDS LLKSHGENVT LPFLGLFADN DIPFEIDRDE KEYPSLKEQV
2640
+ KVALGALEKA SNEDKDSNGF FLMVEGSRID HAGHQNDPAS QVREVLAFDE AFQYVLEFAE
2641
+ NSDTETVLVS TSDHETGGLV TSRQVTASYP QYVWYPQVLA NATHSGEFLK RKLVDFVHEH
2642
+ KGASSKIENF IKHEILEKDL GIYDYTDSDL ETLIHLDDNA NAIQDKLNDM VSFRAQIGWT
2643
+ THGHSAVDVN IYAYANKKAT WSYVLNNLQG NHENTEVGQF LENFLELNLN EVTDLIRDTK
2644
+ HTSDFDATEI ASEVQHYDEY YHELTN
2645
+ //
2646
+ ID APH4_DROME Reviewed; 596 AA.
2647
+ AC Q24238; B9EQR2; Q3KN28; Q8IMH0; Q8SXW6; Q9VA19;
2648
+ DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
2649
+ DT 28-MAR-2003, sequence version 3.
2650
+ DT 28-JUL-2009, entry version 73.
2651
+ DE RecName: Full=Alkaline phosphatase 4;
2652
+ DE EC=3.1.3.1;
2653
+ DE Flags: Precursor;
2654
+ GN Name=Aph-4; ORFNames=CG1462;
2655
+ OS Drosophila melanogaster (Fruit fly).
2656
+ OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
2657
+ OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
2658
+ OC Ephydroidea; Drosophilidae; Drosophila; Sophophora.
2659
+ OX NCBI_TaxID=7227;
2660
+ RN [1]
2661
+ RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
2662
+ RP AND DEVELOPMENTAL STAGE.
2663
+ RC TISSUE=Head;
2664
+ RX MEDLINE=20094770; PubMed=10628988;
2665
+ RA Yang M.Y., Wang Z., MacPherson M., Dow J.A.T., Kaiser K.;
2666
+ RT "A novel Drosophila alkaline phosphatase specific to the ellipsoid
2667
+ RT body of the adult brain and the lower Malpighian (renal) tubule.";
2668
+ RL Genetics 154:285-297(2000).
2669
+ RN [2]
2670
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
2671
+ RC STRAIN=Berkeley;
2672
+ RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
2673
+ RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
2674
+ RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
2675
+ RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
2676
+ RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
2677
+ RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
2678
+ RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
2679
+ RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
2680
+ RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
2681
+ RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
2682
+ RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
2683
+ RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
2684
+ RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
2685
+ RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
2686
+ RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
2687
+ RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
2688
+ RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
2689
+ RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
2690
+ RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
2691
+ RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
2692
+ RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
2693
+ RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
2694
+ RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
2695
+ RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
2696
+ RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
2697
+ RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
2698
+ RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
2699
+ RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
2700
+ RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
2701
+ RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
2702
+ RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
2703
+ RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
2704
+ RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
2705
+ RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
2706
+ RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
2707
+ RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
2708
+ RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
2709
+ RT "The genome sequence of Drosophila melanogaster.";
2710
+ RL Science 287:2185-2195(2000).
2711
+ RN [3]
2712
+ RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
2713
+ RX MEDLINE=22426069; PubMed=12537572;
2714
+ RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
2715
+ RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
2716
+ RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
2717
+ RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
2718
+ RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
2719
+ RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
2720
+ RA Lewis S.E.;
2721
+ RT "Annotation of the Drosophila melanogaster euchromatic genome: a
2722
+ RT systematic review.";
2723
+ RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
2724
+ RN [4]
2725
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
2726
+ RC STRAIN=Berkeley; TISSUE=Head;
2727
+ RX MEDLINE=22426066; PubMed=12537569;
2728
+ RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
2729
+ RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
2730
+ RA Rubin G.M., Celniker S.E.;
2731
+ RT "A Drosophila full-length cDNA resource.";
2732
+ RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
2733
+ RN [5]
2734
+ RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
2735
+ RC STRAIN=Berkeley; TISSUE=Testis;
2736
+ RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E.,
2737
+ RA George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
2738
+ RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
2739
+ CC -!- FUNCTION: Important role in neural and renal epithelial function.
2740
+ CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
2741
+ CC phosphate.
2742
+ CC -!- COFACTOR: Binds 1 magnesium ion (By similarity).
2743
+ CC -!- COFACTOR: Binds 2 zinc ions (By similarity).
2744
+ CC -!- SUBUNIT: Homodimer (By similarity).
2745
+ CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor (By
2746
+ CC similarity).
2747
+ CC -!- ALTERNATIVE PRODUCTS:
2748
+ CC Event=Alternative splicing; Named isoforms=2;
2749
+ CC Name=A;
2750
+ CC IsoId=Q24238-1; Sequence=Displayed;
2751
+ CC Name=B;
2752
+ CC IsoId=Q24238-2; Sequence=VSP_007002;
2753
+ CC Note=No experimental confirmation available;
2754
+ CC -!- TISSUE SPECIFICITY: Ellipsoid body ring neurons in the adult brain
2755
+ CC and in the lower Malpighian tubule and ureter.
2756
+ CC -!- DEVELOPMENTAL STAGE: Highest abundance during larval stage (prior
2757
+ CC to the secretion of pupal cuticle) and adult stage.
2758
+ CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
2759
+ CC -!- SEQUENCE CAUTION:
2760
+ CC Sequence=CAA67052.1; Type=Frameshift; Positions=538;
2761
+ CC -----------------------------------------------------------------------
2762
+ CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
2763
+ CC Distributed under the Creative Commons Attribution-NoDerivs License
2764
+ CC -----------------------------------------------------------------------
2765
+ DR EMBL; X98402; CAA67052.1; ALT_FRAME; mRNA.
2766
+ DR EMBL; AE014297; AAF57106.1; -; Genomic_DNA.
2767
+ DR EMBL; AE014297; AAN14265.1; -; Genomic_DNA.
2768
+ DR EMBL; AY075544; AAL68351.1; -; mRNA.
2769
+ DR EMBL; BT023911; ABA81845.1; -; mRNA.
2770
+ DR EMBL; BT057987; ACM16697.1; -; mRNA.
2771
+ DR RefSeq; NP_524601.2; -.
2772
+ DR RefSeq; NP_733413.1; -.
2773
+ DR UniGene; Dm.5439; -.
2774
+ DR HSSP; P05187; 1EW2.
2775
+ DR Ensembl; FBtr0085733; FBpp0085095; FBgn0016123; Drosophila melanogaster.
2776
+ DR GeneID; 43671; -.
2777
+ DR KEGG; dme:Dmel_CG1462; -.
2778
+ DR FlyBase; FBgn0016123; Aph-4.
2779
+ DR HOGENOM; Q24238; -.
2780
+ DR OMA; Q24238; KVARYVW.
2781
+ DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-014263-MON; -.
2782
+ DR BRENDA; 3.1.3.1; 48.
2783
+ DR NextBio; 835185; -.
2784
+ DR GermOnline; CG1462; Drosophila melanogaster.
2785
+ DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
2786
+ DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
2787
+ DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
2788
+ DR GO; GO:0004035; F:alkaline phosphatase activity; NAS:UniProtKB.
2789
+ DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
2790
+ DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
2791
+ DR GO; GO:0042045; P:epithelial fluid transport; IMP:UniProtKB.
2792
+ DR GO; GO:0008152; P:metabolic process; IEA:InterPro.
2793
+ DR GO; GO:0007399; P:nervous system development; IEP:UniProtKB.
2794
+ DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
2795
+ DR InterPro; IPR001952; Alkaline_phosphatase.
2796
+ DR InterPro; IPR018299; Alkaline_phosphatase_AS.
2797
+ DR Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
2798
+ DR Pfam; PF00245; Alk_phosphatase; 1.
2799
+ DR PRINTS; PR00113; ALKPHPHTASE.
2800
+ DR SMART; SM00098; alkPPc; 1.
2801
+ DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
2802
+ PE 2: Evidence at transcript level;
2803
+ KW Alternative splicing; Cell membrane; Complete proteome;
2804
+ KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
2805
+ KW Magnesium; Membrane; Metal-binding; Phosphoprotein; Signal;
2806
+ KW Transmembrane; Zinc.
2807
+ FT SIGNAL 1 20 Potential.
2808
+ FT CHAIN 21 570 Alkaline phosphatase 4.
2809
+ FT /FTId=PRO_0000024049.
2810
+ FT PROPEP 571 596 Removed in mature form.
2811
+ FT /FTId=PRO_0000024050.
2812
+ FT TRANSMEM 571 591 Potential.
2813
+ FT ACT_SITE 144 144 Phosphoserine intermediate (By
2814
+ FT similarity).
2815
+ FT METAL 93 93 Magnesium (By similarity).
2816
+ FT METAL 93 93 Zinc 2 (By similarity).
2817
+ FT METAL 202 202 Magnesium (By similarity).
2818
+ FT METAL 204 204 Magnesium (By similarity).
2819
+ FT METAL 369 369 Magnesium (By similarity).
2820
+ FT METAL 374 374 Zinc 1 (By similarity).
2821
+ FT METAL 378 378 Zinc 1 (By similarity).
2822
+ FT METAL 415 415 Zinc 2 (By similarity).
2823
+ FT METAL 416 416 Zinc 2 (By similarity).
2824
+ FT METAL 504 504 Zinc 1 (By similarity).
2825
+ FT LIPID 570 570 GPI-anchor amidated asparagine
2826
+ FT (Potential).
2827
+ FT CARBOHYD 262 262 N-linked (GlcNAc...) (Potential).
2828
+ FT CARBOHYD 297 297 N-linked (GlcNAc...) (Potential).
2829
+ FT CARBOHYD 401 401 N-linked (GlcNAc...) (Potential).
2830
+ FT CARBOHYD 464 464 N-linked (GlcNAc...) (Potential).
2831
+ FT CARBOHYD 470 470 N-linked (GlcNAc...) (Potential).
2832
+ FT DISULFID 539 550 By similarity.
2833
+ FT VAR_SEQ 1 94 Missing (in isoform B).
2834
+ FT /FTId=VSP_007002.
2835
+ FT CONFLICT 200 200 I -> N (in Ref. 4; AAL68351).
2836
+ FT CONFLICT 280 280 T -> S (in Ref. 5; ABA81845).
2837
+ FT CONFLICT 358 358 G -> D (in Ref. 1; CAA67052).
2838
+ FT CONFLICT 375 375 Q -> H (in Ref. 1; CAA67052).
2839
+ FT CONFLICT 495 496 AT -> EP (in Ref. 1; CAA67052).
2840
+ FT CONFLICT 570 570 N -> S (in Ref. 1; CAA67052).
2841
+ FT CONFLICT 573 573 T -> S (in Ref. 1; CAA67052).
2842
+ FT CONFLICT 593 594 GR -> CH (in Ref. 1; CAA67052 and 5;
2843
+ FT ABA81845).
2844
+ SQ SEQUENCE 596 AA; 65262 MW; 333F3345BEFBAEFB CRC64;
2845
+ MHCLVILGFL LGSLVAFSWA GVTTQPPPLI RTLSAGGDIG PQFDVGKTKE PEDAEFWHNV
2846
+ GLRQLEKTIK QAQRVKEDSY QKKARNIIIF IGDGMGISTI SAGRIYKGQY LKHGYGEEET
2847
+ LVFDDFPNTG MAKTYNVDKQ VPDSAGTATA IFSGSKTHYG AIGMDATRSK KNGQQGRVQS
2848
+ VMEWAQKEGK RTGVVTTTRI THATPAATYA HIYDRDWECD TEVPAESVGF HVDIARQLVE
2849
+ NAPGNRFNVI LGGGMSPMGI LNASEVKTTI FEGPTETICT RGDNRNLPAE WLAHHANDTV
2850
+ PPALVHNRKD LLNVNVKKVD HLMGLFRNNH ITYSIAREAG EPSLQEMTET ALGILERGDE
2851
+ SNGFVLLVEG GRIDQGHHMN YARAALHELY EFDLAIQAAV NNTDPDETLI LVTADHSHAV
2852
+ TFNGYALRGA DILGTANSHE KNDPMFYETI SYANGPGYWD HLANDSRPQN SSNMWMPLKH
2853
+ FTAEERAAPT YRHLATVPRK DETHGGEDVA VFAYGPGSSL IRGVFEQNYL AYVMSYAGCL
2854
+ GPAKDFDDSC EDHKDGQKDR PLDKPNPKRN GATVVGASLI PILTAATAAI LRGRGL
2855
+ //