CCKAR_HUMAN
ID CCKAR_HUMAN Reviewed; 428 AA.
AC P32238; B2R9Z5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 205.
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; Synonyms=CCKRA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gall bladder;
RX PubMed=8503909; DOI=10.1006/bbrc.1993.1610;
RA Ulrich C.D., Ferber I., Holicky E., Hadac E., Buell G., Miller L.J.;
RT "Molecular cloning and functional expression of the human gallbladder
RT cholecystokinin A receptor.";
RL Biochem. Biophys. Res. Commun. 193:204-211(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8343165; DOI=10.1006/bbrc.1993.1894;
RA Wank S.A., de Weerth A., Pisegna J.R., Huppi K.;
RT "Molecular cloning, functional expression and chromosomal localization of
RT the human cholecystokinin type A receptor.";
RL Biochem. Biophys. Res. Commun. 194:811-818(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7557108; DOI=10.1016/0016-5085(95)90601-0;
RA Miller L.J., Holicky E.L., Ulrich C.D., Wieben E.D.;
RT "Abnormal processing of the human cholecystokinin receptor gene in
RT association with gallstones and obesity.";
RL Gastroenterology 109:1375-1380(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=10682840; DOI=10.1016/s0014-5793(00)01080-2;
RA Funakoshi A., Miyasaka K., Matsumoto H., Yamamori S., Takiguchi S.,
RA Kataoka K., Takata Y., Matsusue K., Kono A., Shimokata H.;
RT "Gene structure of human cholecystokinin (CCK) type-A receptor: body fat
RT content is related to CCK type-A receptor gene promoter polymorphism.";
RL FEBS Lett. 466:264-266(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Stomach;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP STRUCTURE BY NMR OF 1-47 IN COMPLEX WITH CCK.
RX PubMed=10555959; DOI=10.1021/bi991272l;
RA Pellegrini M., Mierke D.F.;
RT "Molecular complex of cholecystokinin-8 and N-terminus of the
RT cholecystokinin A receptor by NMR spectroscopy.";
RL Biochemistry 38:14775-14783(1999).
RN [10]
RP STRUCTURE BY NMR OF 329-357 IN COMPLEX WITH CCK.
RX PubMed=11300760; DOI=10.1021/bi002659n;
RA Giragossian C., Mierke D.F.;
RT "Intermolecular interactions between cholecystokinin-8 and the third
RT extracellular loop of the cholecystokinin A receptor.";
RL Biochemistry 40:3804-3809(2001).
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 -!- 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}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cholecystokinin receptor entry;
CC URL="https://en.wikipedia.org/wiki/Cholecystokinin_receptor";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13605; AAA35659.1; -; mRNA.
DR EMBL; L19315; AAA02819.1; -; mRNA.
DR EMBL; U23430; AAA91123.1; -; Genomic_DNA.
DR EMBL; U23427; AAA91123.1; JOINED; Genomic_DNA.
DR EMBL; U23428; AAA91123.1; JOINED; Genomic_DNA.
DR EMBL; U23429; AAA91123.1; JOINED; Genomic_DNA.
DR EMBL; D85606; BAA90879.1; -; Genomic_DNA.
DR EMBL; AY322549; AAP84362.1; -; mRNA.
DR EMBL; AK313978; BAG36692.1; -; mRNA.
DR EMBL; CH471069; EAW92850.1; -; Genomic_DNA.
DR EMBL; BC074987; AAH74987.1; -; mRNA.
DR CCDS; CCDS3438.1; -.
DR PIR; JN0692; JN0692.
DR RefSeq; NP_000721.1; NM_000730.2.
DR PDB; 1D6G; NMR; -; A=1-47.
DR PDB; 1HZN; NMR; -; A=329-357.
DR PDB; 7EZH; EM; 3.20 A; D=1-428.
DR PDB; 7EZK; EM; 3.10 A; D=1-428.
DR PDB; 7EZM; EM; 2.90 A; D=1-428.
DR PDB; 7F8U; X-ray; 2.80 A; A=37-240, A=302-375.
DR PDB; 7F8X; X-ray; 3.00 A; A=2-240, A=302-406.
DR PDB; 7F8Y; X-ray; 2.50 A; A=37-240, A=302-406.
DR PDB; 7MBX; EM; 1.95 A; R=2-428.
DR PDB; 7MBY; EM; 2.44 A; R=2-428.
DR PDBsum; 1D6G; -.
DR PDBsum; 1HZN; -.
DR PDBsum; 7EZH; -.
DR PDBsum; 7EZK; -.
DR PDBsum; 7EZM; -.
DR PDBsum; 7F8U; -.
DR PDBsum; 7F8X; -.
DR PDBsum; 7F8Y; -.
DR PDBsum; 7MBX; -.
DR PDBsum; 7MBY; -.
DR AlphaFoldDB; P32238; -.
DR SMR; P32238; -.
DR BioGRID; 107328; 1.
DR IntAct; P32238; 1.
DR MINT; P32238; -.
DR STRING; 9606.ENSP00000295589; -.
DR BindingDB; P32238; -.
DR ChEMBL; CHEMBL1901; -.
DR DrugBank; DB00403; Ceruletide.
DR DrugBank; DB08862; Cholecystokinin.
DR DrugBank; DB04856; Dexloxiglumide.
DR DrugBank; DB04867; Lintitript.
DR DrugCentral; P32238; -.
DR GuidetoPHARMACOLOGY; 76; -.
DR GlyGen; P32238; 3 sites.
DR iPTMnet; P32238; -.
DR PhosphoSitePlus; P32238; -.
DR BioMuta; CCKAR; -.
DR DMDM; 416772; -.
DR MassIVE; P32238; -.
DR MaxQB; P32238; -.
DR PaxDb; P32238; -.
DR PeptideAtlas; P32238; -.
DR PRIDE; P32238; -.
DR ProteomicsDB; 54844; -.
DR Antibodypedia; 3359; 455 antibodies from 37 providers.
DR DNASU; 886; -.
DR Ensembl; ENST00000295589.4; ENSP00000295589.3; ENSG00000163394.6.
DR GeneID; 886; -.
DR KEGG; hsa:886; -.
DR MANE-Select; ENST00000295589.4; ENSP00000295589.3; NM_000730.3; NP_000721.1.
DR UCSC; uc003gse.2; human.
DR CTD; 886; -.
DR DisGeNET; 886; -.
DR GeneCards; CCKAR; -.
DR HGNC; HGNC:1570; CCKAR.
DR HPA; ENSG00000163394; Group enriched (gallbladder, stomach).
DR MIM; 118444; gene.
DR neXtProt; NX_P32238; -.
DR OpenTargets; ENSG00000163394; -.
DR PharmGKB; PA26142; -.
DR VEuPathDB; HostDB:ENSG00000163394; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244933; -.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; P32238; -.
DR OMA; DNSTGHM; -.
DR OrthoDB; 1042780at2759; -.
DR PhylomeDB; P32238; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; P32238; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P32238; -.
DR SIGNOR; P32238; -.
DR BioGRID-ORCS; 886; 9 hits in 1068 CRISPR screens.
DR EvolutionaryTrace; P32238; -.
DR GeneWiki; Cholecystokinin_A_receptor; -.
DR GenomeRNAi; 886; -.
DR Pharos; P32238; Tclin.
DR PRO; PR:P32238; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P32238; protein.
DR Bgee; ENSG00000163394; Expressed in gall bladder and 44 other tissues.
DR Genevisible; P32238; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004951; F:cholecystokinin receptor activity; IDA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IPI:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0038188; P:cholecystokinin signaling pathway; IDA:GO_Central.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0046883; P:regulation of hormone secretion; IBA:GO_Central.
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 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Cholecystokinin receptor type A"
FT /id="PRO_0000069223"
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..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..373
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 248..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..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"
FT LIPID 387
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 TURN 5..11
FT /evidence="ECO:0007829|PDB:1D6G"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1D6G"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1D6G"
FT HELIX 40..68
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 75..104
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 111..144
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 155..172
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:7F8U"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 219..242
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 304..338
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 362..370
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 375..381
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:7MBX"
SQ SEQUENCE 428 AA; 47841 MW; A6E8FABDA805E610 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 GEEEEGGTTG ASLSRFSYSH
MSASVPPQ
