CCKAR_MOUSE
ID CCKAR_MOUSE Reviewed; 436 AA.
AC O08786; Q8VCC7; Q9DBV6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
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 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 [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=9099891; DOI=10.1016/s0378-1119(96)00765-2;
RA Takata Y., Takiguchi S., Takaoka K., Funakoshi A., Miyasaka K., Kono A.;
RT "Mouse cholecystokinin type-A receptor gene and its structural analysis.";
RL Gene 187:267-271(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/SvJ;
RX PubMed=9245702; DOI=10.1006/bbrc.1997.7030;
RA Lacourse K.A., Lay J.M., Swanberg L.J., Jenkins C., Samuelson L.C.;
RT "Molecular structure of the mouse CCK-A receptor gene.";
RL Biochem. Biophys. Res. Commun. 236:630-635(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
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DR EMBL; AF015963; AAC07949.1; -; Genomic_DNA.
DR EMBL; AF015959; AAC07949.1; JOINED; Genomic_DNA.
DR EMBL; AF015960; AAC07949.1; JOINED; Genomic_DNA.
DR EMBL; AF015961; AAC07949.1; JOINED; Genomic_DNA.
DR EMBL; AF015962; AAC07949.1; JOINED; Genomic_DNA.
DR EMBL; D85605; BAA20068.1; -; Genomic_DNA.
DR EMBL; AK004730; BAB23512.1; -; mRNA.
DR EMBL; BC020534; AAH20534.1; -; mRNA.
DR CCDS; CCDS19293.1; -.
DR PIR; JC5599; JC5599.
DR RefSeq; NP_033957.1; NM_009827.2.
DR AlphaFoldDB; O08786; -.
DR SMR; O08786; -.
DR STRING; 10090.ENSMUSP00000031093; -.
DR BindingDB; O08786; -.
DR ChEMBL; CHEMBL2798; -.
DR DrugCentral; O08786; -.
DR GuidetoPHARMACOLOGY; 76; -.
DR GlyGen; O08786; 3 sites.
DR iPTMnet; O08786; -.
DR PhosphoSitePlus; O08786; -.
DR PaxDb; O08786; -.
DR PRIDE; O08786; -.
DR ProteomicsDB; 265371; -.
DR Antibodypedia; 3359; 455 antibodies from 37 providers.
DR DNASU; 12425; -.
DR Ensembl; ENSMUST00000031093; ENSMUSP00000031093; ENSMUSG00000029193.
DR GeneID; 12425; -.
DR KEGG; mmu:12425; -.
DR UCSC; uc008xlm.2; mouse.
DR CTD; 886; -.
DR MGI; MGI:99478; Cckar.
DR VEuPathDB; HostDB:ENSMUSG00000029193; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244933; -.
DR InParanoid; O08786; -.
DR OMA; DNSTGHM; -.
DR OrthoDB; 1042780at2759; -.
DR PhylomeDB; O08786; -.
DR TreeFam; TF315303; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 12425; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cckar; mouse.
DR PRO; PR:O08786; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O08786; protein.
DR Bgee; ENSMUSG00000029193; Expressed in epithelium of stomach and 55 other tissues.
DR ExpressionAtlas; O08786; baseline and differential.
DR Genevisible; O08786; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0004951; F:cholecystokinin receptor activity; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0038188; P:cholecystokinin signaling pathway; ISO:MGI.
DR GO; GO:0042755; P:eating behavior; ISO:MGI.
DR GO; GO:0007631; P:feeding behavior; ISO:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001696; P:gastric acid secretion; ISO:MGI.
DR GO; GO:0030073; P:insulin secretion; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0030157; P:pancreatic juice secretion; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0090274; P:positive regulation of somatostatin secretion; ISO:MGI.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; ISO:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0046883; P:regulation of hormone secretion; ISO:MGI.
DR GO; GO:0043266; P:regulation of potassium ion transport; ISO:MGI.
DR GO; GO:0009408; P:response to heat; ISO:MGI.
DR GO; GO:0042594; P:response to starvation; ISO:MGI.
DR GO; GO:0001659; P:temperature homeostasis; ISO:MGI.
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 1: Evidence at protein 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..436
FT /note="Cholecystokinin receptor type A"
FT /id="PRO_0000069224"
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..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..381
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 252..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 395
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"
FT CONFLICT 34
FT /note="Q -> H (in Ref. 3; BAB23512)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="N -> D (in Ref. 3; BAB23512)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="H -> P (in Ref. 4; AAH20534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48437 MW; EBB5D8453B792F79 CRC64;
MDVVDSLLMN GSNITPPCEL GLENETLFCL DQPQPSKEWQ SAVQILLYSF IFLLSVLGNT
LVITVLIRNK RMRTVTNIFL LSLAVSDLML CLFCMPFNLI PNLLKDFIFG SAVCKTTTYF
MGTSVSVSTF NLVAISLERY GAICRPLQSR VWQTKSHALK VIAATWCLSF TIMTPYPIYS
NLVPFTKNNN QTANMCRFLL PSDAMQQSWQ TFLLLILFLI PGVVMVVAYG LISLELYQGI
KFDASQKKSA KEKRLSSGGG GGGGSSSSRY EDSDGCYLQK SRPPRKLELQ QLSTSSSGGR
INRIRSSGSA ANLIAKKRVI RMLIVIVVLF FLCWMPIFSA NAWRAYDTVS AEKHLSGTPI
SFILLLSYTS SCVNPIIYCF MNKRFRLGFM ATFPCCPNPG PTGVRGEVGE EEDGRTIRAS
LSRYSYSHMS TSAPPH
