ID   GASR_MOUSE              Reviewed;         453 AA.
AC   P56481;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Gastrin/cholecystokinin type B receptor;
DE            Short=CCK-B receptor;
DE            Short=CCK-BR;
DE   AltName: Full=Cholecystokinin-2 receptor;
DE            Short=CCK2-R;
GN   Name=Cckbr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Kopin A.S.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=10860839; DOI=10.1006/bbrc.2000.2875;
RA   Lay J.M., Jenkins C., Friis-Hansen L., Samuelson L.C.;
RT   "Structure and developmental expression of the mouse CCK-B receptor gene.";
RL   Biochem. Biophys. Res. Commun. 272:837-842(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Receptor for gastrin and cholecystokinin. The CCK-B receptors
CC       occur throughout the central nervous system where they modulate
CC       anxiety, analgesia, arousal, and neuroleptic activity. This receptor
CC       mediates its 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; AF019371; AAB71863.1; -; mRNA.
DR   EMBL; AF264178; AAG09801.1; -; Genomic_DNA.
DR   EMBL; AF264177; AAG09801.1; JOINED; Genomic_DNA.
DR   EMBL; AK028325; BAC25881.1; -; mRNA.
DR   CCDS; CCDS21651.1; -.
DR   RefSeq; NP_031653.1; NM_007627.5.
DR   AlphaFoldDB; P56481; -.
DR   SMR; P56481; -.
DR   STRING; 10090.ENSMUSP00000033189; -.
DR   BindingDB; P56481; -.
DR   ChEMBL; CHEMBL2854; -.
DR   DrugCentral; P56481; -.
DR   GuidetoPHARMACOLOGY; 77; -.
DR   GlyCosmos; P56481; 3 sites, No reported glycans.
DR   GlyGen; P56481; 3 sites.
DR   iPTMnet; P56481; -.
DR   PhosphoSitePlus; P56481; -.
DR   PaxDb; 10090-ENSMUSP00000033189; -.
DR   ProteomicsDB; 267422; -.
DR   Antibodypedia; 11193; 391 antibodies from 37 providers.
DR   DNASU; 12426; -.
DR   Ensembl; ENSMUST00000033189.6; ENSMUSP00000033189.4; ENSMUSG00000030898.16.
DR   GeneID; 12426; -.
DR   KEGG; mmu:12426; -.
DR   UCSC; uc009iyd.1; mouse.
DR   AGR; MGI:99479; -.
DR   CTD; 887; -.
DR   MGI; MGI:99479; Cckbr.
DR   VEuPathDB; HostDB:ENSMUSG00000030898; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263563; -.
DR   HOGENOM; CLU_009579_6_3_1; -.
DR   InParanoid; P56481; -.
DR   OMA; NTTAHKC; -.
DR   OrthoDB; 3686620at2759; -.
DR   PhylomeDB; P56481; -.
DR   TreeFam; TF315303; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR   BioGRID-ORCS; 12426; 1 hit in 77 CRISPR screens.
DR   PRO; PR:P56481; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P56481; Protein.
DR   Bgee; ENSMUSG00000030898; Expressed in retrosplenial region and 56 other cell types or tissues.
DR   ExpressionAtlas; P56481; baseline and differential.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004951; F:cholecystokinin receptor activity; ISO:MGI.
DR   GO; GO:0015054; F:gastrin receptor activity; ISS:UniProtKB.
DR   GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR   GO; GO:0031741; F:type B gastrin/cholecystokinin receptor binding; ISO:MGI.
DR   GO; GO:0002209; P:behavioral defense response; ISO:MGI.
DR   GO; GO:0038188; P:cholecystokinin signaling pathway; ISO:MGI.
DR   GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0044849; P:estrous cycle; ISO:MGI.
DR   GO; GO:0001696; P:gastric acid secretion; IMP:MGI.
DR   GO; GO:0048732; P:gland development; IMP:MGI.
DR   GO; GO:0001821; P:histamine secretion; ISO:MGI.
DR   GO; GO:0045851; P:pH reduction; IMP:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:2000987; P:positive regulation of behavioral fear response; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:0090274; P:positive regulation of somatostatin secretion; ISO:MGI.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR   GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISO:MGI.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
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.
DR   Genevisible; P56481; MM.
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="Gastrin/cholecystokinin type B receptor"
FT                   /id="PRO_0000069475"
FT   TOPO_DOM        1..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..79
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..109
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..131
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..150
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..189
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..242
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..361
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..453
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          257..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           414
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        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        127..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   453 AA;  49172 MW;  DFD21432C323405C CRC64;
     MDLLKLNRSL QGPGPGSGSS LCRPGVSLLN SSSAGNLSCE TPRIRGTGTR ELELTIRITL
     YAVIFLMSVG GNVLIIVVLG LSRRLRTVTN AFLLSLAVSD LLLAVACMPF TLLPNLMGTF
     IFGTVICKAV SYLMGVSVSV STLNLAAIAL ERYSAICRPL QARVWQTRSH AARVILATWL
     LSGLLMVPYP VYTVVQPVGP RILQCMHLWP SERVQQMWSV LLLILLFFIP GVVMAVAYGL
     ISRELYLGLR FDGDNDSETQ SRVRNQGGLP GGAAAPGPVH QNGGCRHVTS LTGEDSDGCY
     VQLPRSRLEM TTLTTPTTGP GPGPRPNQAK LLAKKRVVRM LLVIVLLFFV CWLPVYSANT
     WRAFDGPGAR RALAGAPISF IHLLSYTSAC ANPLVYCFMH RRFRQACLDT CARCCPRPPR
     ARPRPLPDED PPTPSIASLS RLSYTTISTL GPG
//