ID A0A2R8ZVR1_PANPA Unreviewed; 428 AA.
AC A0A2R8ZVR1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Cholecystokinin receptor type A {ECO:0000256|ARBA:ARBA00022044};
DE AltName: Full=Cholecystokinin-1 receptor {ECO:0000256|ARBA:ARBA00030703};
GN Name=CCKAR {ECO:0000313|Ensembl:ENSPPAP00000009049.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000009049.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000009049.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000009049.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00025653}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
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DR EMBL; AJFE02094220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003826891.1; XM_003826843.1.
DR AlphaFoldDB; A0A2R8ZVR1; -.
DR STRING; 9597.ENSPPAP00000009049; -.
DR Ensembl; ENSPPAT00000031689.1; ENSPPAP00000009049.1; ENSPPAG00000027751.1.
DR GeneID; 100995235; -.
DR KEGG; pps:100995235; -.
DR CTD; 886; -.
DR GeneTree; ENSGT01100000263563; -.
DR OMA; SNISPPC; -.
DR OrthoDB; 3686620at2759; -.
DR Proteomes; UP000240080; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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 CDD; cd15978; 7tmA_CCK-AR; 1.
DR Gene3D; 4.10.670.10; Cholecystokinin A receptor, N-terminal domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
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 PANTHER; PTHR24238:SF77; CHOLECYSTOKININ RECEPTOR TYPE A; 1.
DR PANTHER; PTHR24238; G-PROTEIN COUPLED RECEPTOR; 1.
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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..370
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 248..272
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 COMPBIAS 410..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 47912 MW; A6E8FAA2B81EE7A0 CRC64;
MDVVDSLLVN GSNITPPCEL GLENETLFCL DQPRPSKEWQ PAVQILLYSL IFLLSVLGNT
LVITVLIRNK RMRTVTNIFL LSLAVSDLML CLFCMPFNLI PNLLKDFIFG SAVCKTTTYF
MGTSVSVSTF NLVAISLERY GAICKPLQSR VWQTKSHALK VIAATWCLSF TIMTPYPIYS
NLVPFTKNNN QTANMCRFLL PNDVMQQSWH TFLLLILFLI PGIVMMVAYG LISLELYQGI
KFEASQKKSA KERKPSTTSS GKYEDSDGCY LQKTRPPRKL ELRQLSTGSS SRANRIRSNS
SAANLMAKKR VIRMLIVIVV LFFLCWMPIF SANAWRAYDT ASAERRLSGT PISFILLLSY
TSSCVNPIIY CFMNKRFRLG FMATFPCCPN PGPPGARGEV GEEEEGRTTG ASLSRFSYSH
MSASAPPQ
//
