CCKAR_CAVPO
ID CCKAR_CAVPO Reviewed; 430 AA.
AC Q63931;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cholecystokinin receptor type A;
DE Short=CCK-A receptor;
DE Short=CCK-AR;
DE AltName: Full=Cholecystokinin-1 receptor;
DE Short=CCK1-R;
GN Name=CCKAR;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gall bladder, and Pancreas;
RX PubMed=7916580; DOI=10.1152/ajpgi.1993.265.6.g1116;
RA de Weerth A., Pisegna J.R., Wank S.A.;
RT "Guinea pig gallbladder and pancreas possess identical CCK-A receptor
RT subtypes: receptor cloning and expression.";
RL Am. J. Physiol. 265:G1116-G1121(1993).
CC -!- FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and
CC enzyme secretion, smooth muscle contraction of the gall bladder and
CC stomach. Has a 1000-fold higher affinity for CCK rather than for
CC gastrin. It modulates feeding and dopamine-induced behavior in the
CC central and peripheral nervous system. This receptor mediates its
CC action by association with G proteins that activate a
CC phosphatidylinositol-calcium second messenger system (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; S68242; AAB29504.1; -; mRNA.
DR PIR; I51898; I51898.
DR RefSeq; XP_003467450.1; XM_003467402.2.
DR AlphaFoldDB; Q63931; -.
DR SMR; Q63931; -.
DR STRING; 10141.ENSCPOP00000006355; -.
DR BindingDB; Q63931; -.
DR ChEMBL; CHEMBL3501; -.
DR DrugCentral; Q63931; -.
DR Ensembl; ENSCPOT00000007115; ENSCPOP00000006355; ENSCPOG00000007046.
DR GeneID; 100719593; -.
DR KEGG; cpoc:100719593; -.
DR CTD; 886; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244933; -.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; Q63931; -.
DR OrthoDB; 1042780at2759; -.
DR PRO; PR:Q63931; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000007046; Expressed in ovary and 2 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004951; F:cholecystokinin receptor activity; IEA:Ensembl.
DR GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR Gene3D; 4.10.670.10; -; 1.
DR InterPro; IPR009126; Cholcskin_rcpt.
DR InterPro; IPR000596; Cholcy_rcpt_A.
DR InterPro; IPR015276; CholecystokininA_recpt_N.
DR InterPro; IPR036472; CholecystokininA_recpt_N_sf.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF09193; CholecysA-Rec_N; 1.
DR PRINTS; PR01822; CCYSTOKININR.
DR PRINTS; PR00524; CCYSTOKNINAR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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..430
FT /note="Cholecystokinin receptor type A"
FT /id="PRO_0000069222"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..234
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..375
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 396..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 389
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 114..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 430 AA; 48211 MW; FC9F5D34032076C9 CRC64;
MDVVDSLFVN GSNITSACEL GFENETLFCL DRPRPSKEWQ PAVQILLYSL IFLLSVLGNT
LVITVLIRNK RMRTVTNIFL LSLAVSDLML CLFCMPFNLI PSLLKDFIFG SAVCKTTTYF
MGTSVSVSTF NLVAISLERY GAICKPLQSR VWQTKSHALK VIAATWCLSF TIMTPYPIYS
NLVPFTKNNN QTGNMCRFLL PNDVMQQTWH TFLLLILFLI PGIVMMVAYG LISLELYQGI
KFDAIQKKSA KERKTSTGSS GPMEDSDGCY LQKSRHPRKL ELRQLSPSSS GSNRINRIRS
SSSTANLMAK KRVIRMLIVI VVLFFLCWMP IFSANAWRAY DTVSAERHLS GTPISFILLL
SYTSSCVNPI IYCFMNKRFR LGFMATFPCC PNPGTPGVRG EMGEEEEGRT TGASLSRYSY
SHMSTSAPPP
