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GASR_CANLF
ID   GASR_CANLF              Reviewed;         453 AA.
AC   P30552; O46376;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Gastrin/cholecystokinin type B receptor;
DE            Short=CCK-B receptor;
DE            Short=CCK-BR;
DE   AltName: Full=Cholecystokinin-2 receptor;
DE            Short=CCK2-R;
GN   Name=CCKBR;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric parietal cell;
RX   PubMed=1373504; DOI=10.1073/pnas.89.8.3605;
RA   Kopin A.S., Lee Y.-M., McBride E.W., Miller L.J., Lu M., Lin H.Y.,
RA   Kolakowski L.F. Jr., Beinborn M.;
RT   "Expression cloning and characterization of the canine parietal cell
RT   gastrin receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:3605-3609(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Song I., Blandizzi C., Brown D.R., Kang D.H., Todisco A., Delvalle J.,
RA   del Tacca M., Owyang C., Yamada T.;
RT   "Molecular cloning and structural analysis of the canine gastrin/CCK-B
RT   receptor gene.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for gastrin and cholecystokinin. The CCK-B receptors
CC       occur throughout the central nervous system where they modulate
CC       anxiety, analgesia, arousal, and neuroleptic activity. This receptor
CC       mediates its action by association with G proteins that activate a
CC       phosphatidylinositol-calcium second messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Parietal cells, pancreas, brain and various
CC       neoplastic tissues.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; M87834; AAA30847.1; -; mRNA.
DR   EMBL; AD001537; AAB87706.1; -; Genomic_DNA.
DR   PIR; S32817; S32817.
DR   RefSeq; NP_001013868.1; NM_001013846.1.
DR   AlphaFoldDB; P30552; -.
DR   SMR; P30552; -.
DR   BindingDB; P30552; -.
DR   ChEMBL; CHEMBL5595; -.
DR   Ensembl; ENSCAFT00000104931; ENSCAFP00000075359; ENSCAFG00000006402.
DR   Ensembl; ENSCAFT00030017531; ENSCAFP00030015312; ENSCAFG00030009352.
DR   Ensembl; ENSCAFT00040034737; ENSCAFP00040030249; ENSCAFG00040018649.
DR   Ensembl; ENSCAFT00845012829; ENSCAFP00845009998; ENSCAFG00845007238.
DR   VEuPathDB; HostDB:ENSCAFG00845007238; -.
DR   VGNC; VGNC:58286; CCKBR.
DR   GeneTree; ENSGT01050000244933; -.
DR   InParanoid; P30552; -.
DR   PRO; PR:P30552; -.
DR   Proteomes; UP000002254; Chromosome 21.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004951; F:cholecystokinin receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0015054; F:gastrin receptor activity; ISS:UniProtKB.
DR   GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR   GO; GO:0031741; F:type B gastrin/cholecystokinin receptor binding; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0001696; P:gastric acid secretion; IEA:Ensembl.
DR   GO; GO:0048732; P:gland development; IEA:Ensembl.
DR   GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   InterPro; IPR009126; Cholcskin_rcpt.
DR   InterPro; IPR000314; Gastrin_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01822; CCYSTOKININR.
DR   PRINTS; PR00527; GASTRINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..453
FT                   /note="Gastrin/cholecystokinin type B receptor"
FT                   /id="PRO_0000069473"
FT   TOPO_DOM        1..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..79
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..109
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..131
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..150
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..189
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..361
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..453
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          258..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           414
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P17124"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        127..206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   453 AA;  48519 MW;  0FAEB7B994B44E1F CRC64;
     MELLKLNRSA QGSGAGPGAS LCRAGGALLN SSGAGNLSCE PPRLRGAGTR ELELAIRVTL
     YAVIFLMSVG GNVLIIVVLG LSRRLRTVTN AFLLSLAVSD LLLAVACMPF TLLPNLMGTF
     IFGTVVCKAV SYLMGVSVSV STLSLVAIAL ERYSAICRPL QARVWQTRSH AARVIIATWM
     LSGLLMVPYP VYTAVQPAGG ARALQCVHRW PSARVRQTWS VLLLLLLFFV PGVVMAVAYG
     LISRELYLGL RFDEDSDSES RVRSQGGLRG GAGPGPAPPN GSCRPEGGLA GEDGDGCYVQ
     LPRSRQTLEL SALTAPTPGP GGGPRPYQAK LLAKKRVVRM LLVIVVLFFL CWLPLYSANT
     WRAFDSSGAH RALSGAPISF IHLLSYASAC VNPLVYCFMH RRFRQACLET CARCCPRPPR
     ARPRPLPDED PPTPSIASLS RLSYTTISTL GPG
 
 
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