CCKAR_RABIT
ID CCKAR_RABIT Reviewed; 427 AA.
AC O97772;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7918628; DOI=10.1016/0167-4781(94)90055-8;
RA Reuben M., Rising L., Prinz C., Hersey S., Sachs G.;
RT "Cloning and expression of the rabbit gastric CCK-A receptor.";
RL Biochim. Biophys. Acta 1219:321-327(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 (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}.
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; U86601; AAD11547.1; -; mRNA.
DR PIR; S50150; S50150.
DR RefSeq; NP_001075852.1; NM_001082383.1.
DR AlphaFoldDB; O97772; -.
DR SMR; O97772; -.
DR STRING; 9986.ENSOCUP00000011577; -.
DR PRIDE; O97772; -.
DR GeneID; 100009241; -.
DR KEGG; ocu:100009241; -.
DR CTD; 886; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; O97772; -.
DR OrthoDB; 1042780at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004951; F:cholecystokinin receptor activity; IEA:InterPro.
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..427
FT /note="Cholecystokinin receptor type A"
FT /id="PRO_0000069225"
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..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..372
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 391..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 386
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 427 AA; 47387 MW; 089FD10E2B86DB25 CRC64;
MDAVASLLGN ASGIPPPCEL GLDNETLFCL DQPPPSKEWQ PAVQILLYSL IFLLSVLGNT
LVITVLIRNK RMRTVTNIFL LSLAISDLML CLFCMPFNLI PNLLKDFIFG SALCKTTTYL
MGTSVSVSTL NLVAISLERY GAICKPLQSR VWQTKSHALK VIAATWCLSF AIMTPYPIYS
NLVPFTKTNN QTANMCRFLL PSDVMQQAWH TFLLLILFLI PGIVMMVAYG MISLELYQGI
KFDASQKKSA KERKASTGSG RFEDNDGCYL QRSKPTRQLE LQQLSGGGGG RVSRIRSSSS
AATLMAKKRV IRMLMVIVVL FFLCWMPIFS ANAWRAYDTV SAERRLSGTP ISFILLLSYT
SSCVNPIIYC FMNRRFRLGF MATFPCCPNP GPPGPRAEAG EEEEGRTTRA SLSRYSYSHM
SASAPPS
