CCKAR_CANLF
ID CCKAR_CANLF Reviewed; 428 AA.
AC Q5D0K2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 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=Gall bladder;
RX PubMed=15765098; DOI=10.1038/sj.bjp.0706196;
RA Morton M.F., Pyati J., Dai H., Li L., Moreno V., Shankley N.P.;
RT "Molecular cloning, expression and pharmacological characterization of the
RT canine cholecystokinin 1 receptor.";
RL Br. J. Pharmacol. 145:374-384(2005).
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; AY934643; AAX12114.1; -; mRNA.
DR RefSeq; NP_001012664.1; NM_001012646.2.
DR AlphaFoldDB; Q5D0K2; -.
DR SMR; Q5D0K2; -.
DR STRING; 9615.ENSCAFP00000059499; -.
DR PaxDb; Q5D0K2; -.
DR GeneID; 488846; -.
DR KEGG; cfa:488846; -.
DR CTD; 886; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; Q5D0K2; -.
DR OMA; DNSTGHM; -.
DR OrthoDB; 1042780at2759; -.
DR TreeFam; TF315303; -.
DR Reactome; R-CFA-416476; G alpha (q) signalling events.
DR Proteomes; UP000002254; Chromosome 3.
DR Bgee; ENSCAFG00000029430; Expressed in pancreas and 12 other tissues.
DR GO; GO:0005887; C:integral component of 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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046883; P:regulation of hormone secretion; IBA:GO_Central.
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..428
FT /note="Cholecystokinin receptor type A"
FT /id="PRO_0000247314"
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..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..373
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 250..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 387
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 10
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 428 AA; 47836 MW; ED61C36912549D52 CRC64;
MEVADSLLGN GSDVPPPCEL GLENETLVCL EQPRAAKEWQ PAVQILLYSL IFLLSVLGNT
LVITVLIRNK RMRTVTNIFL LSLAVSDLML CLFCMPFNLI PNLLKDFIFG SAVCKTTTYF
MGTSVSVSTF NLVAISLERY GAICKPLQSR VWQTKSHALK VIATTWCLSF TIMTPYPIYS
NLVPFTKTNN QTANMCRFLL PNDVMQQSWH TFLLLILFLI PGIVMMVAYG LISLELYQGI
KFDAIQKKSA RDRNPSTGSS GRYEDGDGCY LQKARPRRRL ELRQLSTPGS GRLNRIRSTS
STANLMAKKR VIRMLMVIVV LFFLCWMPIF SANAWRAYDT ASAERRLSGT PISFILLLSY
TSSCVNPIIY CFMNKRFRLG FLATFPCCPH PGPPGPRGEV GEEEEGRTTG ASLSRYSYSH
MSASAPGP
