swissparser 0.5.1

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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
+ //