CCKAR_RAT
ID CCKAR_RAT Reviewed; 444 AA.
AC P30551;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 148.
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 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], AND PROTEIN SEQUENCE OF 111-158; 270-314 AND
RP 392-402.
RC TISSUE=Pancreas;
RX PubMed=1313582; DOI=10.1073/pnas.89.7.3125;
RA Wank S.A., Harkins R., Jensen R.T., Shapira H., de Weerth A., Slattery T.;
RT "Purification, molecular cloning, and functional expression of the
RT cholecystokinin receptor from rat pancreas.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3125-3129(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=7654260; DOI=10.1006/bbrc.1995.2222;
RA Takata Y., Takiguchi S., Funakoshi A., Kono A.;
RT "Gene structure of rat cholecystokinin type-A receptor.";
RL Biochem. Biophys. Res. Commun. 213:958-966(1995).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=12916469; DOI=10.3109/10606820308249;
RA Ding X.Q., Dolu V., Hadac E.M., Schuetz M., Miller L.J.;
RT "Disulfide bond structure and accessibility of cysteines in the ectodomain
RT of the cholecystokinin receptor: specific mono-reactive receptor constructs
RT examine charge-sensitivity of loop regions.";
RL Recept. Channels 9:83-91(2003).
RN [4]
RP ANTAGONIST BINDING.
RX PubMed=8024583; DOI=10.1006/bbrc.1994.1856;
RA Mantamadiotis T., Baldwin G.S.;
RT "The seventh transmembrane domain of gastrin/CCK receptors contributes to
RT non-peptide antagonist binding.";
RL Biochem. Biophys. Res. Commun. 201:1382-1389(1994).
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.
CC {ECO:0000269|PubMed:7654260}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Pancreas and brain. Also expressed in the
CC gastrointestinal system and vagus nerve. {ECO:0000269|PubMed:7654260}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M88096; AAA40899.1; -; mRNA.
DR EMBL; D50608; BAA09170.1; -; Genomic_DNA.
DR PIR; A42685; A42685.
DR RefSeq; NP_036820.1; NM_012688.3.
DR AlphaFoldDB; P30551; -.
DR SMR; P30551; -.
DR STRING; 10116.ENSRNOP00000063137; -.
DR BindingDB; P30551; -.
DR ChEMBL; CHEMBL2871; -.
DR DrugCentral; P30551; -.
DR GuidetoPHARMACOLOGY; 76; -.
DR GlyGen; P30551; 3 sites.
DR iPTMnet; P30551; -.
DR PhosphoSitePlus; P30551; -.
DR PaxDb; P30551; -.
DR GeneID; 24889; -.
DR KEGG; rno:24889; -.
DR CTD; 886; -.
DR RGD; 2289; Cckar.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P30551; -.
DR PhylomeDB; P30551; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P30551; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0004951; F:cholecystokinin receptor activity; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0038188; P:cholecystokinin signaling pathway; ISO:RGD.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0007631; P:feeding behavior; IDA:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001696; P:gastric acid secretion; IDA:RGD.
DR GO; GO:0030073; P:insulin secretion; IDA:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0031016; P:pancreas development; IEP:RGD.
DR GO; GO:0030157; P:pancreatic juice secretion; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0090274; P:positive regulation of somatostatin secretion; IMP:RGD.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; IMP:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:RGD.
DR GO; GO:0046883; P:regulation of hormone secretion; IDA:RGD.
DR GO; GO:0043266; P:regulation of potassium ion transport; IDA:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IMP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IMP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0001659; P:temperature homeostasis; IMP:RGD.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..444
FT /note="Cholecystokinin receptor type A"
FT /id="PRO_0000069226"
FT TOPO_DOM 1..56
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..249
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..389
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 263..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 403
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:12916469"
FT DISULFID 129..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 444 AA; 49657 MW; B435BE7505C2FB11 CRC64;
MSHSPARQHL VESSRMDVVD SLLMNGSNIT PPCELGLENE TLFCLDQPQP SKEWQSALQI
LLYSIIFLLS VLGNTLVITV LIRNKRMRTV TNIFLLSLAV SDLMLCLFCM PFNLIPNLLK
DFIFGSAVCK TTTYFMGTSV SVSTFNLVAI SLERYGAICR PLQSRVWQTK SHALKVIAAT
WCLSFTIMTP YPIYSNLVPF TKNNNQTANM CRFLLPSDAM QQSWQTFLLL ILFLLPGIVM
VVAYGLISLE LYQGIKFDAS QKKSAKEKKP STGSSTRYED SDGCYLQKSR PPRKLELQQL
SSGSGGSRLN RIRSSSSAAN LIAKKRVIRM LIVIVVLFFL CWMPIFSANA WRAYDTVSAE
KHLSGTPISF ILLLSYTSSC VNPIIYCFMN KRFRLGFMAT FPCCPNPGPP GVRGEVGEEE
DGRTIRALLS RYSYSHMSTS APPP
