bio 2.0.4 → 2.0.5
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- checksums.yaml +4 -4
- data/.github/workflows/ruby.yml +38 -0
- data/.gitignore +32 -0
- data/ChangeLog +287 -0
- data/Gemfile +3 -0
- data/LEGAL +2 -0
- data/README.rdoc +1 -1
- data/RELEASE_NOTES.rdoc +36 -0
- data/appveyor.yml +14 -13
- data/bioruby.gemspec +7 -10
- data/lib/bio/appl/blast/genomenet.rb +2 -1
- data/lib/bio/appl/pts1.rb +1 -1
- data/lib/bio/db/embl/uniprotkb.rb +52 -19
- data/lib/bio/version.rb +1 -1
- data/test/data/uniprot/P03589.uniprot +127 -0
- data/test/data/uniprot/P49144.uniprot +232 -0
- data/test/functional/bio/test_command.rb +2 -0
- data/test/network/bio/db/kegg/test_genes_hsa7422.rb +26 -12
- data/test/unit/bio/db/embl/test_uniprotkb_P03589.rb +378 -0
- data/test/unit/bio/db/embl/test_uniprotkb_P49144.rb +359 -0
- metadata +12 -15
- data/.travis.yml +0 -71
- data/gemfiles/Gemfile.travis-jruby1.8 +0 -6
- data/gemfiles/Gemfile.travis-jruby1.9 +0 -5
- data/gemfiles/Gemfile.travis-rbx +0 -10
- data/gemfiles/Gemfile.travis-ruby1.8 +0 -6
- data/gemfiles/Gemfile.travis-ruby1.9 +0 -5
- data/gemfiles/Gemfile.windows +0 -6
- data/gemfiles/modify-Gemfile.rb +0 -28
- data/gemfiles/prepare-gemspec.rb +0 -29
@@ -530,22 +530,43 @@ class UniProtKB < EMBLDB
|
|
530
530
|
# http://br.expasy.org/sprot/userman.html#OH_line
|
531
531
|
def oh
|
532
532
|
unless @data['OH']
|
533
|
-
|
534
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-
|
535
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-
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536
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-
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-
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-
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-
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-
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541
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-
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-
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543
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-
|
544
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-
|
545
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-
|
533
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+
oh = []
|
534
|
+
a = fetch('OH').split(/(NCBI\_TaxID\=)(\d+)(\;)/)
|
535
|
+
t = catch :error do
|
536
|
+
taxid = nil
|
537
|
+
host_name = nil
|
538
|
+
while x = a.shift
|
539
|
+
x = x.to_s.strip
|
540
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+
case x
|
541
|
+
when ''
|
542
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+
next
|
543
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+
when 'NCBI_TaxID='
|
544
|
+
if taxid then
|
545
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+
oh.push({'NCBI_TaxID' => taxid, 'HostName' => host_name})
|
546
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+
taxid = nil
|
547
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+
host_name = nil
|
548
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+
end
|
549
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+
taxid = a.shift
|
550
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+
throw :error, :missing_semicolon if a.shift != ';'
|
551
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+
else
|
552
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+
throw :error, :missing_taxid if host_name
|
553
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+
host_name = x
|
554
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+
host_name.sub!(/\.\z/, '')
|
555
|
+
end
|
556
|
+
end #while x...
|
557
|
+
if taxid then
|
558
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+
oh.push({'NCBI_TaxID' => taxid, 'HostName' => host_name})
|
559
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+
elsif host_name then
|
560
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+
throw :error, :missing_taxid_last
|
546
561
|
end
|
547
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-
|
548
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-
|
562
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+
nil
|
563
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+
end #t = catch...
|
564
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+
if t then
|
565
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+
raise ArgumentError,
|
566
|
+
["Error: Invalid OH line format (#{self.entry_id}):",
|
567
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+
$!, "\n", get('OH'), "\n"].join
|
568
|
+
end
|
569
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+
@data['OH'] = oh
|
549
570
|
end
|
550
571
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@data['OH']
|
551
572
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end
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@@ -922,6 +943,7 @@ class UniProtKB < EMBLDB
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922
943
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923
944
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924
945
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def cc_alternative_products(data)
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946
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+
return nil unless data
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925
947
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ap = data.join('')
|
926
948
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return ap unless ap
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927
949
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@@ -960,6 +982,7 @@ class UniProtKB < EMBLDB
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960
982
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961
983
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962
984
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def cc_biophysiochemical_properties(data)
|
985
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+
return nil unless data
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963
986
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data = data[0]
|
964
987
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965
988
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hash = {'Absorption' => {},
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@@ -995,6 +1018,7 @@ class UniProtKB < EMBLDB
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995
1018
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996
1019
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997
1020
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def cc_caution(data)
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1021
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+
return nil unless data
|
998
1022
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data.join('')
|
999
1023
|
end
|
1000
1024
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private :cc_caution
|
@@ -1004,6 +1028,7 @@ class UniProtKB < EMBLDB
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1004
1028
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#
|
1005
1029
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# CC P46527:CDKN1B; NbExp=1; IntAct=EBI-359815, EBI-519280;
|
1006
1030
|
def cc_interaction(data)
|
1031
|
+
return nil unless data
|
1007
1032
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str = data.join('')
|
1008
1033
|
it = str.scan(/(.+?); NbExp=(.+?); IntAct=(.+?);/)
|
1009
1034
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it.map {|ent|
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@@ -1059,6 +1084,7 @@ class UniProtKB < EMBLDB
|
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1059
1084
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1060
1085
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1061
1086
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def cc_pathway(data)
|
1087
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+
return nil unless data
|
1062
1088
|
data.map {|x| x.sub(/\.$/, '') }.map {|x|
|
1063
1089
|
x.split(/; | and |: /)
|
1064
1090
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}[0]
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@@ -1067,6 +1093,7 @@ class UniProtKB < EMBLDB
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1067
1093
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1068
1094
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1069
1095
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def cc_rna_editing(data)
|
1096
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+
return nil unless data
|
1070
1097
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data = data.join('')
|
1071
1098
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entry = {'Modified_positions' => [], 'Note' => ""}
|
1072
1099
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if data =~ /Modified_positions=(.+?)(\.|;)/
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@@ -1083,6 +1110,7 @@ class UniProtKB < EMBLDB
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1083
1110
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1084
1111
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1085
1112
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def cc_subcellular_location(data)
|
1113
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+
return nil unless data
|
1086
1114
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data.map {|x|
|
1087
1115
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x.split('. ').map {|y|
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1088
1116
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y.split('; ').map {|z|
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@@ -1101,6 +1129,7 @@ class UniProtKB < EMBLDB
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1101
1129
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#++
|
1102
1130
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1103
1131
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def cc_web_resource(data)
|
1132
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+
return nil unless data
|
1104
1133
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data.map {|x|
|
1105
1134
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entry = {'Name' => nil, 'Note' => nil, 'URL' => nil}
|
1106
1135
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x.split(';').each do |y|
|
@@ -1235,10 +1264,14 @@ class UniProtKB < EMBLDB
|
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1235
1264
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begin
|
1236
1265
|
ftlines.each do |line|
|
1237
1266
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if /^FT +([^\s]+) +(([^\s]+)\:)?([\<\?]?[0-9]+|\?)(?:\.\.([\>\?]?[0-9]+|\?))?\s*$/ =~ line
|
1238
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-
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-
|
1240
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-
|
1241
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-
|
1267
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+
f_name = $1.to_s
|
1268
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+
f_from = "#{$2}#{$4}"
|
1269
|
+
f_to = $5.to_s
|
1270
|
+
f_to = f_from if f_to.empty?
|
1271
|
+
cur_ft = [f_name, # Feature Name
|
1272
|
+
f_from, # From
|
1273
|
+
f_to, # To
|
1274
|
+
[] # Qualifiers
|
1242
1275
|
]
|
1243
1276
|
table.push cur_ft
|
1244
1277
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cont = false
|
data/lib/bio/version.rb
CHANGED
@@ -10,7 +10,7 @@
|
|
10
10
|
module Bio
|
11
11
|
|
12
12
|
# BioRuby version (Array containing Integer)
|
13
|
-
BIORUBY_VERSION = [2, 0,
|
13
|
+
BIORUBY_VERSION = [2, 0, 5].extend(Comparable).freeze
|
14
14
|
|
15
15
|
# Extra version specifier (String or nil).
|
16
16
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# Existance of the value indicates development version.
|
@@ -0,0 +1,127 @@
|
|
1
|
+
ID 1A_AMVLE Reviewed; 1126 AA.
|
2
|
+
AC P03589;
|
3
|
+
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
|
4
|
+
DT 21-JUL-1986, sequence version 1.
|
5
|
+
DT 22-FEB-2023, entry version 78.
|
6
|
+
DE RecName: Full=Replication protein 1a;
|
7
|
+
DE Includes:
|
8
|
+
DE RecName: Full=ATP-dependent helicase;
|
9
|
+
DE EC=3.6.4.-;
|
10
|
+
DE Includes:
|
11
|
+
DE RecName: Full=Methyltransferase;
|
12
|
+
DE EC=2.1.1.-;
|
13
|
+
GN ORFNames=ORF1a;
|
14
|
+
OS Alfalfa mosaic virus (strain 425 / isolate Leiden).
|
15
|
+
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
|
16
|
+
OC Martellivirales; Bromoviridae; Alfamovirus.
|
17
|
+
OX NCBI_TaxID=12322;
|
18
|
+
OH NCBI_TaxID=4045; Apium graveolens (Celery).
|
19
|
+
OH NCBI_TaxID=83862; Astragalus glycyphyllos (Wild liquorice).
|
20
|
+
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
|
21
|
+
OH NCBI_TaxID=41386; Caryopteris incana.
|
22
|
+
OH NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
|
23
|
+
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
|
24
|
+
OH NCBI_TaxID=35936; Lablab purpureus (Hyacinth bean) (Dolichos lablab).
|
25
|
+
OH NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
|
26
|
+
OH NCBI_TaxID=3864; Lens culinaris (Lentil) (Cicer lens).
|
27
|
+
OH NCBI_TaxID=3869; Lupinus.
|
28
|
+
OH NCBI_TaxID=145753; Malva parviflora (Little mallow) (Cheeseweed mallow).
|
29
|
+
OH NCBI_TaxID=3879; Medicago sativa (Alfalfa).
|
30
|
+
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
|
31
|
+
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
|
32
|
+
OH NCBI_TaxID=23113; Philadelphus.
|
33
|
+
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
|
34
|
+
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
|
35
|
+
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
|
36
|
+
OH NCBI_TaxID=157662; Teramnus repens.
|
37
|
+
OH NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
|
38
|
+
OH NCBI_TaxID=85293; Viburnum opulus (High-bush cranberry).
|
39
|
+
OH NCBI_TaxID=3916; Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
|
40
|
+
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
|
41
|
+
RN [1]
|
42
|
+
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|
43
|
+
RX PubMed=6298738; DOI=10.1093/nar/11.5.1253;
|
44
|
+
RA Cornelissen B.J.C., Brederode F.T., Moormann R.J.M., Bol J.F.;
|
45
|
+
RT "Complete nucleotide sequence of alfalfa mosaic virus RNA 1.";
|
46
|
+
RL Nucleic Acids Res. 11:1253-1265(1983).
|
47
|
+
CC -!- FUNCTION: Involved in the virus replication. Contains a helicase domain
|
48
|
+
CC and a methyltransferase domain. The methyltransferase domain is
|
49
|
+
CC probably involved in viral RNA capping. Involved in the formation of ER
|
50
|
+
CC membrane spherular invaginations in which RNA replication complexes
|
51
|
+
CC form (By similarity). {ECO:0000250}.
|
52
|
+
CC -!- SUBUNIT: Interacts with RNA-directed RNA polymerase 2a. {ECO:0000250}.
|
53
|
+
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
|
54
|
+
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
|
55
|
+
CC -!- SIMILARITY: Belongs to the bromoviridae replication protein 1a family.
|
56
|
+
CC {ECO:0000305}.
|
57
|
+
CC ---------------------------------------------------------------------------
|
58
|
+
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
|
59
|
+
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
|
60
|
+
CC ---------------------------------------------------------------------------
|
61
|
+
DR EMBL; L00163; AAA46289.1; -; Genomic_RNA.
|
62
|
+
DR PIR; A04197; WMFM12.
|
63
|
+
DR RefSeq; NP_041192.1; NC_001495.1.
|
64
|
+
DR SMR; P03589; -.
|
65
|
+
DR GeneID; 962667; -.
|
66
|
+
DR KEGG; vg:962667; -.
|
67
|
+
DR Proteomes; UP000000358; Genome.
|
68
|
+
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
|
69
|
+
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
|
70
|
+
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
|
71
|
+
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
|
72
|
+
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
|
73
|
+
DR GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
|
74
|
+
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
|
75
|
+
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
|
76
|
+
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
|
77
|
+
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
|
78
|
+
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
|
79
|
+
DR InterPro; IPR027417; P-loop_NTPase.
|
80
|
+
DR Pfam; PF01443; Viral_helicase1; 1.
|
81
|
+
DR Pfam; PF01660; Vmethyltransf; 1.
|
82
|
+
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
|
83
|
+
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
|
84
|
+
DR PROSITE; PS51657; PSRV_HELICASE; 1.
|
85
|
+
PE 3: Inferred from homology;
|
86
|
+
KW ATP-binding; Helicase; Host endoplasmic reticulum; Host membrane;
|
87
|
+
KW Hydrolase; Membrane; Methyltransferase; Nucleotide-binding;
|
88
|
+
KW Reference proteome; Transferase.
|
89
|
+
FT CHAIN 1..1126
|
90
|
+
FT /note="Replication protein 1a"
|
91
|
+
FT /id="PRO_0000083254"
|
92
|
+
FT DOMAIN 90..278
|
93
|
+
FT /note="Alphavirus-like MT"
|
94
|
+
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
|
95
|
+
FT DOMAIN 806..963
|
96
|
+
FT /note="(+)RNA virus helicase ATP-binding"
|
97
|
+
FT DOMAIN 964..1125
|
98
|
+
FT /note="(+)RNA virus helicase C-terminal"
|
99
|
+
FT REGION 69..406
|
100
|
+
FT /note="Methyltransferase"
|
101
|
+
FT REGION 834..1094
|
102
|
+
FT /note="ATP-dependent helicase"
|
103
|
+
FT BINDING 838..845
|
104
|
+
FT /ligand="ATP"
|
105
|
+
FT /ligand_id="ChEBI:CHEBI:30616"
|
106
|
+
FT /evidence="ECO:0000255"
|
107
|
+
SQ SEQUENCE 1126 AA; 125828 MW; BF5A8019B47D4CBF CRC64;
|
108
|
+
MNADAQSTDA SLSMREPLSH ASIQEMLRRV VEKQAADDTT AIGKVFSEAG RAYAQDALPS
|
109
|
+
DKGEVLKISF SLDATQQNIL RANFPGRRTV FSNSSSSSHC FAAAHRLLET DFVYRCFGNT
|
110
|
+
VDSIIDLGGN FVSHMKVKRH NVHCCCPILD ARDGARLTER ILSLKSYVRK HPEIVGEADY
|
111
|
+
CMDTFQKCSR RADYAFAIHS TSDLDVGELA CSLDQKGVMK FICTMMVDAD MLIHNEGEIP
|
112
|
+
NFNVRWEIDR KKDLIHFDFI DEPNLGYSHR FSLLKHYLTY NAVDLGHAAY RIERKQDFGG
|
113
|
+
VMVIDLTYSL GFVPKMPHSN GRSCAWYNRV KGQMVVHTVN EGYYHHSYQT AVRRKVLVDK
|
114
|
+
KVLTRVTEVA FRQFRPNADA HSAIQSIATM LSSSTNHTII GGVTLISGKP LSPDDYIPVA
|
115
|
+
TTIYYRVKKL YNAIPEMLSL LDKGERLSTD AVLKGSEGPM WYSGPTFLSA LDKVNVPGDF
|
116
|
+
VAKALLSLPK RDLKSLFSRS ATSHSERTPV RDESPIRCTD GVFYPIRMLL KCLGSDKFES
|
117
|
+
VTITDPRSNT ETTVDLYQSF QKKIETVFSF ILGKIDGPSP LISDPVYFQS LEDVYYAEWH
|
118
|
+
QGNAIDASNY ARTLLDDIRK QKEESLKAKA KEVEDAQKLN RAILQVHAYL EAHPDGGKIE
|
119
|
+
GLGLSSQFIA KIPELAIPTP KPLPEFEKNA ETGEILRINP HSDAILEAID YLKSTSANSI
|
120
|
+
ITLNKLGDHC QWTTKGLDVV WAGDDKRRAF IPKKNTWVGP TARSYPLAKY ERAMSKDGYV
|
121
|
+
TLRWDGEVLD ANCVRSLSQY EIVFVDQSCV FASAEAIIPS LEKALGLEAH FSVTIVDGVA
|
122
|
+
GCGKTTNIKQ IARSSGRDVD LILTSNRSSA DELKETIDCS PLTKLHYIRT CDSYLMSASA
|
123
|
+
VKAQRLIFDE CFLQHAGLVY AAATLAGCSE VIGFGDTEQI PFVSRNPSFV FRHHKLTGKV
|
124
|
+
ERKLITWRSP ADATYCLEKY FYKNKKPVKT NSRVLRSIEV VPINSPVSVE RNTNALYLCH
|
125
|
+
TQAEKAVLKA QTHLKGCDNI FTTHEAQGKT FDNVYFCRLT RTSTSLATGR DPINGPCNGL
|
126
|
+
VALSRHKKTF KYFTIAHDSD DVIYNACRDA GNTDDSILAR SYNHNF
|
127
|
+
//
|
@@ -0,0 +1,232 @@
|
|
1
|
+
ID 5HT1B_RABIT Reviewed; 390 AA.
|
2
|
+
AC P49144;
|
3
|
+
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
|
4
|
+
DT 01-FEB-1996, sequence version 1.
|
5
|
+
DT 22-FEB-2023, entry version 127.
|
6
|
+
DE RecName: Full=5-hydroxytryptamine receptor 1B;
|
7
|
+
DE Short=5-HT-1B;
|
8
|
+
DE Short=5-HT1B;
|
9
|
+
DE AltName: Full=Serotonin 1D beta receptor;
|
10
|
+
DE Short=5-HT-1D-beta;
|
11
|
+
DE AltName: Full=Serotonin receptor 1B;
|
12
|
+
GN Name=HTR1B;
|
13
|
+
OS Oryctolagus cuniculus (Rabbit).
|
14
|
+
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
|
15
|
+
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
|
16
|
+
OX NCBI_TaxID=9986;
|
17
|
+
RN [1]
|
18
|
+
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
|
19
|
+
RC TISSUE=Liver;
|
20
|
+
RX PubMed=8543023; DOI=10.1016/0014-5793(95)01308-3;
|
21
|
+
RA Harwood G.S., Lockyer M., Giles H., Fairweather N.;
|
22
|
+
RT "Cloning and characterisation of the rabbit 5-HT1D alpha and 5-HT1D beta
|
23
|
+
RT receptors.";
|
24
|
+
RL FEBS Lett. 377:73-76(1995).
|
25
|
+
RN [2]
|
26
|
+
RP NUCLEOTIDE SEQUENCE.
|
27
|
+
RC STRAIN=New Zealand white; TISSUE=Saphenous vein;
|
28
|
+
RA Wurch T., Cathala C., Palmer C., Valentin J.P., John G., Colpaert F.C.,
|
29
|
+
RA Pauwels P.J.;
|
30
|
+
RT "Molecular cloning and identification of a rabbit saphenous vein 5-HT 1DB
|
31
|
+
RT receptor gene.";
|
32
|
+
RL Neurosci. Res. Commun. 18:155-162(1996).
|
33
|
+
RN [3]
|
34
|
+
RP NUCLEOTIDE SEQUENCE.
|
35
|
+
RC STRAIN=New Zealand white;
|
36
|
+
RX PubMed=8878052; DOI=10.1007/bf00171053;
|
37
|
+
RA Bard J.A., Kucharewicz S.A., Zgombick J.M., Weinshank R.L., Branchek T.A.,
|
38
|
+
RA Cohen M.L.;
|
39
|
+
RT "Differences in ligand binding profiles between cloned rabbit and human 5-
|
40
|
+
RT HT1D alpha and 5-HT1D beta receptors: ketanserin and methiothepin
|
41
|
+
RT distinguish rabbit 5-HT1D receptor subtypes.";
|
42
|
+
RL Naunyn Schmiedebergs Arch. Pharmacol. 354:237-244(1996).
|
43
|
+
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
|
44
|
+
CC (serotonin). Also functions as a receptor for various alkaloids and
|
45
|
+
CC psychoactive substances. Ligand binding causes a conformation change
|
46
|
+
CC that triggers signaling via guanine nucleotide-binding proteins (G
|
47
|
+
CC proteins) and modulates the activity of down-stream effectors, such as
|
48
|
+
CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
|
49
|
+
CC Arrestin family members inhibit signaling via G proteins and mediate
|
50
|
+
CC activation of alternative signaling pathways. Regulates the release of
|
51
|
+
CC 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and
|
52
|
+
CC thereby affects neural activity, nociceptive processing, pain
|
53
|
+
CC perception, mood and behavior. Besides, plays a role in
|
54
|
+
CC vasoconstriction of cerebral arteries.
|
55
|
+
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
|
56
|
+
CC {ECO:0000250}.
|
57
|
+
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
|
58
|
+
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
|
59
|
+
CC transmembrane helices. {ECO:0000250}.
|
60
|
+
CC -!- PTM: Phosphorylated. {ECO:0000250}.
|
61
|
+
CC -!- PTM: Palmitoylated. {ECO:0000250}.
|
62
|
+
CC -!- MISCELLANEOUS: A residue in the 7th transmembrane region ('Thr-355' in
|
63
|
+
CC human, 'Asn-351' in mouse and rat) is important for species-specific
|
64
|
+
CC sensitivity to various agonists. {ECO:0000250}.
|
65
|
+
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
|
66
|
+
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
|
67
|
+
CC ---------------------------------------------------------------------------
|
68
|
+
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
|
69
|
+
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
|
70
|
+
CC ---------------------------------------------------------------------------
|
71
|
+
DR EMBL; Z50163; CAA90531.1; -; Genomic_DNA.
|
72
|
+
DR EMBL; X89731; CAA61883.1; -; mRNA.
|
73
|
+
DR EMBL; U60826; AAB58467.1; -; Genomic_DNA.
|
74
|
+
DR PIR; S58126; S58126.
|
75
|
+
DR PIR; S68422; S68422.
|
76
|
+
DR RefSeq; NP_001076259.1; NM_001082790.1.
|
77
|
+
DR AlphaFoldDB; P49144; -.
|
78
|
+
DR SMR; P49144; -.
|
79
|
+
DR STRING; 9986.ENSOCUP00000016295; -.
|
80
|
+
DR BindingDB; P49144; -.
|
81
|
+
DR ChEMBL; CHEMBL5717; -.
|
82
|
+
DR GlyCosmos; P49144; 2 sites, No reported glycans.
|
83
|
+
DR GeneID; 100009594; -.
|
84
|
+
DR KEGG; ocu:100009594; -.
|
85
|
+
DR CTD; 3351; -.
|
86
|
+
DR eggNOG; KOG3656; Eukaryota.
|
87
|
+
DR InParanoid; P49144; -.
|
88
|
+
DR OrthoDB; 2999405at2759; -.
|
89
|
+
DR TreeFam; TF316350; -.
|
90
|
+
DR PRO; PR:P49144; -.
|
91
|
+
DR Proteomes; UP000001811; Unplaced.
|
92
|
+
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
|
93
|
+
DR GO; GO:0045202; C:synapse; IEA:GOC.
|
94
|
+
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
|
95
|
+
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
|
96
|
+
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
|
97
|
+
DR GO; GO:0046849; P:bone remodeling; IEA:InterPro.
|
98
|
+
DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
|
99
|
+
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
|
100
|
+
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
|
101
|
+
DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
|
102
|
+
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
|
103
|
+
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
|
104
|
+
DR CDD; cd15333; 7tmA_5-HT1B_1D; 1.
|
105
|
+
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
|
106
|
+
DR InterPro; IPR002147; 5HT1B_rcpt.
|
107
|
+
DR InterPro; IPR002231; 5HT_rcpt.
|
108
|
+
DR InterPro; IPR000276; GPCR_Rhodpsn.
|
109
|
+
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
|
110
|
+
DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
|
111
|
+
DR PANTHER; PTHR24248:SF66; OCTOPAMINE RECEPTOR BETA-3R; 1.
|
112
|
+
DR Pfam; PF00001; 7tm_1; 1.
|
113
|
+
DR PRINTS; PR00513; 5HT1BRECEPTR.
|
114
|
+
DR PRINTS; PR01101; 5HTRECEPTOR.
|
115
|
+
DR PRINTS; PR00237; GPCRRHODOPSN.
|
116
|
+
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
|
117
|
+
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
|
118
|
+
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
|
119
|
+
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
|
120
|
+
PE 2: Evidence at transcript level;
|
121
|
+
KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
|
122
|
+
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
|
123
|
+
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
|
124
|
+
FT CHAIN 1..390
|
125
|
+
FT /note="5-hydroxytryptamine receptor 1B"
|
126
|
+
FT /id="PRO_0000068920"
|
127
|
+
FT TOPO_DOM 1..49
|
128
|
+
FT /note="Extracellular"
|
129
|
+
FT /evidence="ECO:0000250"
|
130
|
+
FT TRANSMEM 50..75
|
131
|
+
FT /note="Helical; Name=1"
|
132
|
+
FT /evidence="ECO:0000250"
|
133
|
+
FT TOPO_DOM 76..84
|
134
|
+
FT /note="Cytoplasmic"
|
135
|
+
FT /evidence="ECO:0000250"
|
136
|
+
FT TRANSMEM 85..110
|
137
|
+
FT /note="Helical; Name=2"
|
138
|
+
FT /evidence="ECO:0000250"
|
139
|
+
FT TOPO_DOM 111..123
|
140
|
+
FT /note="Extracellular"
|
141
|
+
FT /evidence="ECO:0000250"
|
142
|
+
FT TRANSMEM 124..145
|
143
|
+
FT /note="Helical; Name=3"
|
144
|
+
FT /evidence="ECO:0000250"
|
145
|
+
FT TOPO_DOM 146..165
|
146
|
+
FT /note="Cytoplasmic"
|
147
|
+
FT /evidence="ECO:0000250"
|
148
|
+
FT TRANSMEM 166..187
|
149
|
+
FT /note="Helical; Name=4"
|
150
|
+
FT /evidence="ECO:0000250"
|
151
|
+
FT TOPO_DOM 188..205
|
152
|
+
FT /note="Extracellular"
|
153
|
+
FT /evidence="ECO:0000250"
|
154
|
+
FT TRANSMEM 206..228
|
155
|
+
FT /note="Helical; Name=5"
|
156
|
+
FT /evidence="ECO:0000250"
|
157
|
+
FT TOPO_DOM 229..315
|
158
|
+
FT /note="Cytoplasmic"
|
159
|
+
FT /evidence="ECO:0000250"
|
160
|
+
FT TRANSMEM 316..336
|
161
|
+
FT /note="Helical; Name=6"
|
162
|
+
FT /evidence="ECO:0000250"
|
163
|
+
FT TOPO_DOM 337..349
|
164
|
+
FT /note="Extracellular"
|
165
|
+
FT /evidence="ECO:0000250"
|
166
|
+
FT TRANSMEM 350..371
|
167
|
+
FT /note="Helical; Name=7"
|
168
|
+
FT /evidence="ECO:0000250"
|
169
|
+
FT TOPO_DOM 372..390
|
170
|
+
FT /note="Cytoplasmic"
|
171
|
+
FT /evidence="ECO:0000250"
|
172
|
+
FT REGION 260..282
|
173
|
+
FT /note="Disordered"
|
174
|
+
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
|
175
|
+
FT MOTIF 146..148
|
176
|
+
FT /note="DRY motif; important for ligand-induced conformation
|
177
|
+
FT changes and signaling"
|
178
|
+
FT /evidence="ECO:0000250"
|
179
|
+
FT MOTIF 365..369
|
180
|
+
FT /note="NPxxY motif; important for ligand-induced
|
181
|
+
FT conformation changes and signaling"
|
182
|
+
FT /evidence="ECO:0000250"
|
183
|
+
FT BINDING 129
|
184
|
+
FT /ligand="ergotamine"
|
185
|
+
FT /ligand_id="ChEBI:CHEBI:190463"
|
186
|
+
FT /ligand_note="agonist"
|
187
|
+
FT /evidence="ECO:0000250|UniProtKB:P28222"
|
188
|
+
FT BINDING 134
|
189
|
+
FT /ligand="ergotamine"
|
190
|
+
FT /ligand_id="ChEBI:CHEBI:190463"
|
191
|
+
FT /ligand_note="agonist"
|
192
|
+
FT /evidence="ECO:0000250|UniProtKB:P28222"
|
193
|
+
FT BINDING 201
|
194
|
+
FT /ligand="ergotamine"
|
195
|
+
FT /ligand_id="ChEBI:CHEBI:190463"
|
196
|
+
FT /ligand_note="agonist"
|
197
|
+
FT /evidence="ECO:0000250|UniProtKB:P28222"
|
198
|
+
FT SITE 355
|
199
|
+
FT /note="Important for species-specific agonist sensitivity"
|
200
|
+
FT /evidence="ECO:0000250"
|
201
|
+
FT LIPID 388
|
202
|
+
FT /note="S-palmitoyl cysteine"
|
203
|
+
FT /evidence="ECO:0000255"
|
204
|
+
FT CARBOHYD 24
|
205
|
+
FT /note="N-linked (GlcNAc...) asparagine"
|
206
|
+
FT /evidence="ECO:0000255"
|
207
|
+
FT CARBOHYD 32
|
208
|
+
FT /note="N-linked (GlcNAc...) asparagine"
|
209
|
+
FT /evidence="ECO:0000255"
|
210
|
+
FT DISULFID 122..199
|
211
|
+
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
|
212
|
+
FT CONFLICT 5
|
213
|
+
FT /note="G -> S (in Ref. 1 and 3)"
|
214
|
+
FT /evidence="ECO:0000305"
|
215
|
+
FT CONFLICT 7
|
216
|
+
FT /note="Q -> R (in Ref. 1 and 3)"
|
217
|
+
FT /evidence="ECO:0000305"
|
218
|
+
FT CONFLICT 14
|
219
|
+
FT /note="Missing (in Ref. 1 and 3)"
|
220
|
+
FT /evidence="ECO:0000305"
|
221
|
+
FT CONFLICT 171
|
222
|
+
FT /note="R -> A (in Ref. 1 and 3)"
|
223
|
+
FT /evidence="ECO:0000305"
|
224
|
+
SQ SEQUENCE 390 AA; 43496 MW; C22EBC077C6C897D CRC64;
|
225
|
+
MEEPGAQCAP PLAAGSQIAV PQANLSAAHS HNCSAEGYIY QDSIALPWKV LLVLLLALFT
|
226
|
+
LATTLSNAFV VATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV
|
227
|
+
VCDLWLSSDI TCCTASIMHL CVIALDRYWA ITDAVEYSAK RTPKRAAIMI RLVWVFSICI
|
228
|
+
SLPPFFWRQA KAEEEVSECL VNTDHVLYTV YSTVGAFYLP TLLLIALYGR IYVEARSRIL
|
229
|
+
KQTPNRTGKR LTRAQLITDS PGSTTSVTSI NSRAPDVPSE SGSPVYVNQV KVRVSDALLE
|
230
|
+
KKKLMAARER KATKTLGIIL GVFIVCWLPF FIISLVMPIC KDACWFHQAI FDFFTWLGYV
|
231
|
+
NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
|
232
|
+
//
|
@@ -187,8 +187,10 @@ module Bio
|
|
187
187
|
return
|
188
188
|
end
|
189
189
|
assert_equal('', str.to_s.strip)
|
190
|
+
assert_equal('', err.to_s.strip)
|
190
191
|
str, err = Bio::Command.query_command_open3(ary, @data)
|
191
192
|
assert_equal(@sorted, str.to_s.strip.split(/\s+/))
|
193
|
+
assert_equal('', err.to_s.strip)
|
192
194
|
end
|
193
195
|
end #class FuncTestCommandQuery
|
194
196
|
|
@@ -38,7 +38,8 @@ module Bio
|
|
38
38
|
"H01457 Diabetic retinopathy",
|
39
39
|
"H01459 Diabetic neuropathy",
|
40
40
|
"H01529 Avascular necrosis of femoral head",
|
41
|
-
"H01709 Glucocorticoid-induced osteonecrosis"
|
41
|
+
"H01709 Glucocorticoid-induced osteonecrosis",
|
42
|
+
"H02559 Microvascular complications of diabetes"]
|
42
43
|
|
43
44
|
assert_equal(expected, @obj.diseases_as_strings)
|
44
45
|
end
|
@@ -48,41 +49,54 @@ module Bio
|
|
48
49
|
"H01457"=>"Diabetic retinopathy",
|
49
50
|
"H01459"=>"Diabetic neuropathy",
|
50
51
|
"H01529"=>"Avascular necrosis of femoral head",
|
51
|
-
"H01709"=>"Glucocorticoid-induced osteonecrosis"
|
52
|
+
"H01709"=>"Glucocorticoid-induced osteonecrosis",
|
53
|
+
"H02559"=>"Microvascular complications of diabetes"}
|
52
54
|
assert_equal(expected, @obj.diseases_as_hash)
|
53
55
|
end
|
54
56
|
|
55
57
|
def test_drug_targets_as_strings
|
56
58
|
expected = ["Abicipar pegol: D11517",
|
57
|
-
"Aflibercept: D09574",
|
58
|
-
"Aflibercept beta: D10819",
|
59
|
-
"Bevacizumab: D06409",
|
59
|
+
"Aflibercept: D09574<JP/US>",
|
60
|
+
"Aflibercept beta: D10819<JP>",
|
61
|
+
"Bevacizumab: D06409<JP/US>",
|
60
62
|
"Bevasiranib sodium: D08874",
|
61
|
-
"Brolucizumab: D11083",
|
62
|
-
"
|
63
|
+
"Brolucizumab: D11083<JP/US>",
|
64
|
+
"Dilpacimab: D11642",
|
65
|
+
"Emvododstat: D11890",
|
66
|
+
"Faricimab: D11516<JP/US>",
|
63
67
|
"Navicixizumab: D11126",
|
64
68
|
"Pegaptanib: D05386",
|
65
|
-
"Ranibizumab: D05697",
|
69
|
+
"Ranibizumab: D05697<JP/US>",
|
70
|
+
"Tarcocimab: D12507",
|
71
|
+
"Tarcocimab tedromer: D12508",
|
66
72
|
"Vanucizumab: D11244"]
|
67
73
|
assert_equal(expected, @obj.drug_targets_as_strings)
|
68
74
|
end
|
69
75
|
|
70
76
|
def test_networks_as_strings
|
71
|
-
expected = ["
|
72
|
-
"nt06124 Chemokine signaling (virus)",
|
77
|
+
expected = ["nt06124 Chemokine signaling (viruses)",
|
73
78
|
"nt06164 Kaposi sarcoma-associated herpesvirus (KSHV)",
|
74
|
-
"nt06214 PI3K signaling",
|
75
79
|
"nt06219 JAK-STAT signaling",
|
76
80
|
"nt06224 CXCR signaling",
|
77
81
|
"nt06225 HIF-1 signaling",
|
82
|
+
"nt06227 Nuclear receptor signaling",
|
78
83
|
"nt06262 Pancreatic cancer",
|
79
84
|
"nt06264 Renal cell carcinoma",
|
85
|
+
"nt06360 Cushing syndrome",
|
86
|
+
"nt06526 MAPK signaling",
|
87
|
+
"nt06528 Calcium signaling",
|
88
|
+
"nt06530 PI3K signaling",
|
80
89
|
"N00079 HIF-1 signaling pathway",
|
81
90
|
"N00080 Loss of VHL to HIF-1 signaling pathway",
|
82
91
|
"N00081 Mutation-inactivated VHL to HIF-1 signaling pathway",
|
83
92
|
"N00095 ERBB2-overexpression to EGF-Jak-STAT signaling pathway",
|
84
93
|
"N00157 KSHV vGPCR to GNB/G-ERK signaling pathway",
|
85
|
-
"
|
94
|
+
"N00317 AhR signaling pathway",
|
95
|
+
"N01412 Metals to HTF-1 signaling pathway",
|
96
|
+
"N01592 GF-RTK-RAS-ERK signaling pathway",
|
97
|
+
"N01641 RTK-PLCG-ITPR signaling pathway",
|
98
|
+
"N01656 GF-RTK-PI3K signaling pathway",
|
99
|
+
"N01658 GF-RTK-RAS-PI3K signaling pathway"]
|
86
100
|
assert_equal(expected, @obj.networks_as_strings)
|
87
101
|
end
|
88
102
|
|