GASR_RAT
ID GASR_RAT Reviewed; 452 AA.
AC P30553;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 138.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1528881; DOI=10.1073/pnas.89.18.8691;
RA Wank S.A., Pisegna J.R., de Weerth A.;
RT "Brain and gastrointestinal cholecystokinin receptor family: structure and
RT functional expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8691-8695(1992).
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; M99418; AAA40925.1; -; mRNA.
DR PIR; A46195; A46195.
DR RefSeq; NP_037297.1; NM_013165.2.
DR AlphaFoldDB; P30553; -.
DR SMR; P30553; -.
DR STRING; 10116.ENSRNOP00000024077; -.
DR BindingDB; P30553; -.
DR ChEMBL; CHEMBL3508; -.
DR DrugCentral; P30553; -.
DR GuidetoPHARMACOLOGY; 77; -.
DR GlyGen; P30553; 3 sites.
DR iPTMnet; P30553; -.
DR PhosphoSitePlus; P30553; -.
DR PaxDb; P30553; -.
DR GeneID; 25706; -.
DR KEGG; rno:25706; -.
DR UCSC; RGD:2290; rat.
DR CTD; 887; -.
DR RGD; 2290; Cckbr.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P30553; -.
DR OrthoDB; 1042780at2759; -.
DR PhylomeDB; P30553; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR PRO; PR:P30553; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0004951; F:cholecystokinin receptor activity; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0015054; F:gastrin receptor activity; IMP:RGD.
DR GO; GO:0017046; F:peptide hormone binding; ISO:RGD.
DR GO; GO:0031741; F:type B gastrin/cholecystokinin receptor binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0002209; P:behavioral defense response; IMP:RGD.
DR GO; GO:0038188; P:cholecystokinin signaling pathway; ISO:RGD.
DR GO; GO:0007586; P:digestion; IEP:RGD.
DR GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0044849; P:estrous cycle; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001696; P:gastric acid secretion; ISO:RGD.
DR GO; GO:0048732; P:gland development; ISO:RGD.
DR GO; GO:0001821; P:histamine secretion; IMP:RGD.
DR GO; GO:0045851; P:pH reduction; ISO:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0090274; P:positive regulation of somatostatin secretion; IMP:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IMP:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
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..452
FT /note="Gastrin/cholecystokinin type B receptor"
FT /id="PRO_0000069478"
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..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..360
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..378
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 413
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..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 452 AA; 48957 MW; 006D811A6AA065C6 CRC64;
MELLKLNRSV QGPGPGSGSS LCRPGVSLLN SSSAGNLSCD PPRIRGTGTR ELEMAIRITL
YAVIFLMSVG GNVLIIVVLG LSRRLRTVTN AFLLSLAVSD LLLAVACMPF TLLPNLMGTF
IFGTVICKAI SYLMGVSVSV STLNLVAIAL ERYSAICRPL QARVWQTRSH AARVILATWL
LSGLLMVPYP VYTMVQPVGP RVLQCMHRWP SARVQQTWSV LLLLLLFFIP GVVIAVAYGL
ISRELYLGLH FDGENDSETQ SRARNQGGLP GGAAPGPVHQ NGGCRPVTSV AGEDSDGCCV
QLPRSRLEMT TLTTPTPGPV PGPRPNQAKL LAKKRVVRML LVIVLLFFLC WLPVYSVNTW
RAFDGPGAQR ALSGAPISFI HLLSYVSACV NPLVYCFMHR RFRQACLDTC ARCCPRPPRA
RPQPLPDEDP PTPSIASLSR LSYTTISTLG PG
