ID GASR_PIG Reviewed; 452 AA.
AC A0A287A2K5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Gastrin/cholecystokinin type B receptor {ECO:0000250|UniProtKB:P32239};
DE Short=CCK-B receptor {ECO:0000250|UniProtKB:P32239};
DE Short=CCK-BR {ECO:0000305};
DE AltName: Full=Cholecystokinin-2 receptor {ECO:0000250|UniProtKB:P32239};
DE Short=CCK2-R {ECO:0000305};
GN Name=CCKBR {ECO:0000250|UniProtKB:P32239};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|Proteomes:UP000008227};
RN [1] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000312|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=29920282; DOI=10.1016/j.ejphar.2018.06.020;
RA Bugge A., Jansen P.G., Maria L., Sanni S.J., Clausen T.R.;
RT "Cloning and characterization of the porcine gastrin/cholecystokinin type 2
RT receptor.";
RL Eur. J. Pharmacol. 833:357-363(2018).
CC -!- FUNCTION: Receptor for gastrin and cholecystokinin (PubMed:29920282).
CC The CCK-B receptors occur throughout the central nervous system where
CC they modulate anxiety, analgesia, arousal, and neuroleptic activity
CC (Probable). This receptor mediates its action by association with G
CC proteins that activate a phosphatidylinositol-calcium second messenger
CC system (Probable). {ECO:0000269|PubMed:29920282, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521, ECO:0000255|RuleBase:RU000688}.
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DR EMBL; AEMK02000068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287A2K5; -.
DR SMR; A0A287A2K5; -.
DR STRING; 9823.ENSSSCP00000037961; -.
DR GlyCosmos; A0A287A2K5; 3 sites, No reported glycans.
DR PaxDb; 9823-ENSSSCP00000015561; -.
DR Ensembl; ENSSSCT00000058854.3; ENSSSCP00000037961.1; ENSSSCG00000033806.3.
DR Ensembl; ENSSSCT00015098979.1; ENSSSCP00015040869.1; ENSSSCG00015073549.1.
DR Ensembl; ENSSSCT00030005644.1; ENSSSCP00030002325.1; ENSSSCG00030004277.1.
DR Ensembl; ENSSSCT00035075837.1; ENSSSCP00035030912.1; ENSSSCG00035056757.1.
DR Ensembl; ENSSSCT00040047954.1; ENSSSCP00040020041.1; ENSSSCG00040035698.1.
DR Ensembl; ENSSSCT00045045005.1; ENSSSCP00045031220.1; ENSSSCG00045026416.1.
DR Ensembl; ENSSSCT00050095738.1; ENSSSCP00050041215.1; ENSSSCG00050070220.1.
DR Ensembl; ENSSSCT00055042008.1; ENSSSCP00055033450.1; ENSSSCG00055021358.1.
DR Ensembl; ENSSSCT00060035661.1; ENSSSCP00060015183.1; ENSSSCG00060026336.1.
DR Ensembl; ENSSSCT00065109109.1; ENSSSCP00065048957.1; ENSSSCG00065078630.1.
DR Ensembl; ENSSSCT00070000706.1; ENSSSCP00070000617.1; ENSSSCG00070000383.1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01100000263518; -.
DR InParanoid; A0A287A2K5; -.
DR OMA; NTTAHKC; -.
DR OrthoDB; 3686620at2759; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Chromosome 9.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR Bgee; ENSSSCG00000033806; Expressed in frontal cortex and 9 other cell types or tissues.
DR ExpressionAtlas; A0A287A2K5; baseline.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015054; F:gastrin receptor activity; IEA:InterPro.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR009126; Cholcskin_rcpt.
DR InterPro; IPR000314; Gastrin_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24243; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24243:SF45; GASTRIN_CHOLECYSTOKININ TYPE B RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01822; CCYSTOKININR.
DR PRINTS; PR00527; GASTRINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..452
FT /note="Gastrin/cholecystokinin type B receptor"
FT /id="PRO_0000445193"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..127
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..218
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 340..360
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..376
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..397
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 256..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 413
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P17124"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 452 AA; 48613 MW; 2C89EF4907435C08 CRC64;
MELLKLNRSL PGPGPGAALC RPEGPLLNGS GAGNLSCEPP RIRGAGTREL ELAVRITLYA
AIFLMSVAGN VLIIVVLGLS RRLRTVTNAF LLSLAVSDLL LAVACMPFTL LPNLMGTFIF
GTVVCKAVSY FMGVSVSVST LSLVAIALER YSAICRPLQA RVWQTRSHAA RVIVATWMLS
GLLMVPYPVY TAVQPAGPRV LQCMHRWPSA RIRQTWSVLL LLLLFFVPGV VMAVAYGLIS
RELYLGLRFD GDSDCESQSQ VGSQGGLPGG AGQGPAHPNG HCRSETRLAG EDGDGCYVQL
PRSRPALEMS ALTAPTPGPG SGPRPAQAKL LAKKRVVRML LVIVVLFFLC WLPVYSANTW
RAFDGPGAHR ALSGAPISFI HLLSYASACV NPLVYCFMHR RFRQACLDTC ARCCPRPPRA
RPRPLPDEDP PTPSIASLSR LSYTTISTLG PG
//
