CCKAR_XENLA
ID CCKAR_XENLA Reviewed; 453 AA.
AC P70031;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cholecystokinin receptor;
DE AltName: Full=CCK-XLR;
GN Name=cckar;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8700154;
RA Schmitz F., Pratt D.S., Wu M.-J., Kolakowski L.F. Jr., Beinborn M.,
RA Kopin A.S.;
RT "Identification of cholecystokinin-B/gastrin receptor domains that confer
RT high gastrin affinity: utilization of a novel Xenopus laevis
RT cholecystokinin receptor.";
RL Mol. Pharmacol. 50:436-441(1996).
CC -!- FUNCTION: Receptor for cholecystokinin. This receptor mediates its
CC action by association with G proteins that activate a
CC phosphatidylinositol-calcium second messenger system. Has high affinity
CC for CCK-8 and low affinities for gastrin-17-I, CCK-4, and unsulfated
CC CCK-8.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Brain and stomach.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U49258; AAB09052.1; -; mRNA.
DR RefSeq; NP_001079277.1; NM_001085808.1.
DR AlphaFoldDB; P70031; -.
DR SMR; P70031; -.
DR GeneID; 378563; -.
DR KEGG; xla:378563; -.
DR CTD; 378563; -.
DR Xenbase; XB-GENE-5793825; cckbr.L.
DR OMA; NTTAHKC; -.
DR OrthoDB; 1042780at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 378563; Expressed in stomach and 2 other tissues.
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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR InterPro; IPR009126; Cholcskin_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01822; CCYSTOKININR.
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..453
FT /note="Cholecystokinin receptor"
FT /id="PRO_0000069227"
FT TOPO_DOM 1..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..94
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..131
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..261
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..379
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..403
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 401
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
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 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 453 AA; 51157 MW; 06217927B7482678 CRC64;
MESLRSLSNI SALHELLCRY SNLSGTLTWN LSSTNGTHNL TTANWPPWNL NCTPILDRKK
PSPSDLNLWV RIVMYSVIFL LSVFGNTLII IVLVMNKRLR TITNSFLLSL ALSDLMVAVL
CMPFTLIPNL MENFIFGEVI CRAAAYFMGL SVSVSTFNLV AISIERYSAI CNPLKSRVWQ
TRSHAYRVIA ATWVLSSIIM IPYLVYNKTV TFPMKDRRVG HQCRLVWPSK QVQQAWYVLL
LTILFFIPGV VMIVAYGLIS RELYRGIQFE MDLNKEAKAH KNGVSTPTTI PSGDEGDGCY
IQVTKRRNTM EMSTLTPSVC TKMDRARINN SEAKLMAKKR VIRMLIVIVA MFFICWMPIF
VANTWKAFDE LSAFNTLTGA PISFIHLLSY TSACVNPLIY CFMNKRFRKA FLGTFSSCIK
PCRNFRDTDE DIAATGASLS KFSYTTVSSL GPA
