GASR_HUMAN
ID GASR_HUMAN Reviewed; 447 AA.
AC P32239; A8K7P9; O75824; Q16144; Q92492; Q96LC6; Q9NYK7; Q9UBV1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Gastrin/cholecystokinin type B receptor {ECO:0000303|PubMed:8415658};
DE Short=CCK-B receptor {ECO:0000303|PubMed:8415658};
DE Short=CCK-BR;
DE AltName: Full=Cholecystokinin-2 receptor {ECO:0000303|PubMed:11926817};
DE Short=CCK2-R;
GN Name=CCKBR {ECO:0000312|HGNC:HGNC:1571}; Synonyms=CCKRB;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1280419; DOI=10.1016/0006-291x(92)91557-7;
RA Pisegna J.R., de Weerth A., Huppi K., Wank S.A.;
RT "Molecular cloning of the human brain and gastric cholecystokinin receptor:
RT structure, functional expression and chromosomal localization.";
RL Biochem. Biophys. Res. Commun. 189:296-303(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7681836; DOI=10.1016/s0021-9258(18)53076-3;
RA Lee Y.-M., Beinborn M., McBride E.W., Lu M., Kolakowski L.F. Jr.,
RA Kopin A.S.;
RT "The human brain cholecystokinin-B/gastrin receptor. Cloning and
RT characterization.";
RL J. Biol. Chem. 268:8164-8169(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8349705; DOI=10.1016/s0021-9258(17)46844-x;
RA Ito M., Matsui T., Taniguchi T., Tsukamoto T., Murayama T., Arima N.,
RA Nakata H., Chiba T., Chihara K.;
RT "Functional characterization of a human brain cholecystokinin-B receptor. A
RT trophic effect of cholecystokinin and gastrin.";
RL J. Biol. Chem. 268:18300-18305(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8415658; DOI=10.1073/pnas.90.19.9085;
RA Song I., Brown D.R., Wiltshire R.N., Gantz I., Trent J.M., Yamada T.;
RT "The human gastrin/cholecystokinin type B receptor gene: alternative splice
RT donor site in exon 4 generates two variant mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9085-9089(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=8185170; DOI=10.1111/j.1749-6632.1994.tb44076.x;
RA Herget T., Sethi T., Wu S.V., Walsh J.H., Rozengurt E.;
RT "Cholecystokinin stimulates Ca2+ mobilization and clonal growth in small
RT cell lung cancer through CCKA and CCKB/gastrin receptors.";
RL Ann. N. Y. Acad. Sci. 713:283-297(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Lung fibroblast;
RX PubMed=7848914;
RA Ito M., Iwata N., Taniguchi T., Murayama T., Chihara K., Matsui T.;
RT "Functional characterization of two cholecystokinin-B/gastrin receptor
RT isoforms: a preferential splice donor site in the human receptor gene.";
RL Cell Growth Differ. 5:1127-1135(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Stomach;
RX PubMed=7887934; DOI=10.1006/bbrc.1995.1328;
RA Miyake A.;
RT "A truncated isoform of human CCK-B/gastrin receptor generated by
RT alternative usage of a novel exon.";
RL Biochem. Biophys. Res. Commun. 208:230-237(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Colon cancer;
RX PubMed=10913157; DOI=10.1074/jbc.m005754200;
RA Hellmich M.R., Rui X.-L., Hellmich H.L., Fleming R.Y.D., Evers B.M.,
RA Townsend C.M. Jr.;
RT "Human colorectal cancers express a constitutively active cholecystokinin-
RT B/gastrin receptor that stimulates cell growth.";
RL J. Biol. Chem. 275:32122-32128(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND ALTERNATIVE SPLICING.
RC TISSUE=Peripheral blood;
RX PubMed=11495676; DOI=10.1016/s0167-0115(01)00281-6;
RA Schmitz F., Schrader H., Otte J.-M., Schmitz H., Stueber E., Herzig K.-H.,
RA Schmidt W.E.;
RT "Identification of CCK-B/gastrin receptor splice variants in human
RT peripheral blood mononuclear cells.";
RL Regul. Pept. 101:25-33(2001).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Pancreatic cancer;
RX PubMed=12429993;
RA Smith J.P., Verderame M.F., McLaughlin P., Martenis M., Ballard E.,
RA Zagon I.S.;
RT "Characterization of the CCK-C (cancer) receptor in human pancreatic
RT cancer.";
RL Int. J. Mol. Med. 10:689-694(2002).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Temporal cortex;
RA Tate S.N., Gray J., Denyer J., Stolz M., Foord S., Lee M.G.;
RT "Cloning and expression of the human temporal cortex cholecystokinin B
RT receptor.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
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 [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-447.
RX PubMed=9872672; DOI=10.1023/a:1009289625352;
RA O'Briant K.C., Ali S.Y., Weier H.-U.G., Bepler G.;
RT "An 84-kilobase physical map and repeat polymorphisms of the
RT gastrin/cholecystokinin brain receptor region at the junction of chromosome
RT segments 11p15.4 and 15.5.";
RL Chromosome Res. 6:415-418(1998).
RN [17]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-333 (ISOFORMS 1/3), AND FUNCTION.
RC TISSUE=Fetal brain;
RX PubMed=8221657;
RA Sethi T., Herget T., Wu S.V., Walsh J.H., Rozengurt E.;
RT "CCKA and CCKB receptors are expressed in small cell lung cancer lines and
RT mediate Ca2+ mobilization and clonal growth.";
RL Cancer Res. 53:5208-5213(1993).
RN [18]
RP CHROMOSOMAL LOCATION.
RX PubMed=8222757; DOI=10.1159/000133628;
RA Zimonjic D.B., Popescu N.C., Matsui T., Ito M., Chihara K.;
RT "Localization of the human cholecystokinin-B/gastrin receptor gene (CCKBR)
RT to chromosome 11p15.5-->p15.4 by fluorescence in situ hybridization.";
RL Cytogenet. Cell Genet. 65:184-185(1994).
RN [19]
RP STRUCTURE BY NMR OF 352-379.
RX PubMed=11926817; DOI=10.1021/bi0160009;
RA Giragossian C., Mierke D.F.;
RT "Intermolecular interactions between cholecystokinin-8 and the third
RT extracellular loop of the cholecystokinin-2 receptor.";
RL Biochemistry 41:4560-4566(2002).
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.
CC -!- FUNCTION: Isoform 2 is constitutively activated and may regulate cancer
CC cell proliferation via a gastrin-independent mechanism.
CC -!- INTERACTION:
CC P32239; PRO_0000010542 [P06307]: CCK; NbExp=2; IntAct=EBI-1753137, EBI-6624436;
CC P32239; Q9P121: NTM; NbExp=3; IntAct=EBI-1753137, EBI-4315078;
CC P32239; Q06124: PTPN11; NbExp=5; IntAct=EBI-1753137, EBI-297779;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P32239-1; Sequence=Displayed;
CC Name=2; Synonyms=CCK-C, CCK-BRi4sv;
CC IsoId=P32239-2; Sequence=VSP_033445;
CC Name=3; Synonyms=DeltaCCK-B;
CC IsoId=P32239-3; Sequence=VSP_033444;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain, pancreas, stomach,
CC the colon cancer cell line LoVo and the T-lymphoblastoma Jurkat, but
CC not in heart, placenta, liver, lung, skeletal muscle, kidney or the
CC stomach cancer cell line AGS. Expressed at high levels in the small
CC cell lung cancer cell line NCI-H510, at lower levels in NCI-H345, NCI-
CC H69 and GLC-28 cell lines, not expressed in GLC-19 cell line. Within
CC the stomach, expressed at high levels in the mucosa of the gastric
CC fundus and at low levels in the antrum and duodenum. Isoform 2 is
CC present in pancreatic cancer cells and colorectal cancer cells, but not
CC in normal pancreas or colonic mucosa. Isoform 3 is expressed in brain,
CC pancreas, stomach, the stomach cancer cell line AGS and the colon
CC cancer cell line LoVo. {ECO:0000269|PubMed:10913157,
CC ECO:0000269|PubMed:12429993, ECO:0000269|PubMed:7848914,
CC ECO:0000269|PubMed:7887934, ECO:0000269|PubMed:8185170,
CC ECO:0000269|PubMed:8349705}.
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; L04473; AAA35660.1; -; mRNA.
DR EMBL; L08112; AAA35657.1; -; mRNA.
DR EMBL; D13305; BAA02564.1; -; mRNA.
DR EMBL; L10822; AAC37528.1; -; Genomic_DNA.
DR EMBL; S70057; AAB30766.2; -; mRNA.
DR EMBL; D21219; BAA04759.2; -; Genomic_DNA.
DR EMBL; AF239668; AAF67174.1; -; mRNA.
DR EMBL; AY029770; AAK38351.1; -; mRNA.
DR EMBL; AF441129; AAN32829.1; -; mRNA.
DR EMBL; L07746; AAA91831.1; -; mRNA.
DR EMBL; AK292064; BAF84753.1; -; mRNA.
DR EMBL; AY322551; AAP84364.1; -; mRNA.
DR EMBL; BT006789; AAP35435.1; -; mRNA.
DR EMBL; BC000740; AAH00740.1; -; mRNA.
DR EMBL; AH006311; AAC27510.1; -; Genomic_DNA.
DR CCDS; CCDS7761.1; -. [P32239-1]
DR CCDS; CCDS86175.1; -. [P32239-2]
DR PIR; A47430; A47430.
DR PIR; I65231; I65231.
DR RefSeq; NP_001304958.1; NM_001318029.1.
DR RefSeq; NP_795344.1; NM_176875.3. [P32239-1]
DR RefSeq; XP_005253267.1; XM_005253210.1.
DR RefSeq; XP_016874005.1; XM_017018516.1. [P32239-3]
DR PDB; 1L4T; NMR; -; A=352-379.
DR PDB; 7F8V; EM; 3.30 A; R=2-418.
DR PDB; 7F8W; EM; 3.10 A; R=2-418.
DR PDBsum; 1L4T; -.
DR PDBsum; 7F8V; -.
DR PDBsum; 7F8W; -.
DR AlphaFoldDB; P32239; -.
DR SMR; P32239; -.
DR BioGRID; 107329; 20.
DR DIP; DIP-229N; -.
DR IntAct; P32239; 21.
DR MINT; P32239; -.
DR STRING; 9606.ENSP00000335544; -.
DR BindingDB; P32239; -.
DR ChEMBL; CHEMBL298; -.
DR DrugBank; DB08862; Cholecystokinin.
DR DrugBank; DB00183; Pentagastrin.
DR DrugCentral; P32239; -.
DR GuidetoPHARMACOLOGY; 77; -.
DR GlyGen; P32239; 3 sites.
DR iPTMnet; P32239; -.
DR PhosphoSitePlus; P32239; -.
DR BioMuta; CCKBR; -.
DR DMDM; 417029; -.
DR MassIVE; P32239; -.
DR PaxDb; P32239; -.
DR PeptideAtlas; P32239; -.
DR PRIDE; P32239; -.
DR ProteomicsDB; 54845; -. [P32239-1]
DR ProteomicsDB; 54846; -. [P32239-2]
DR ProteomicsDB; 54847; -. [P32239-3]
DR Antibodypedia; 11193; 363 antibodies from 37 providers.
DR DNASU; 887; -.
DR Ensembl; ENST00000334619.7; ENSP00000335544.2; ENSG00000110148.10. [P32239-1]
DR Ensembl; ENST00000525462.1; ENSP00000435534.1; ENSG00000110148.10. [P32239-2]
DR GeneID; 887; -.
DR KEGG; hsa:887; -.
DR MANE-Select; ENST00000334619.7; ENSP00000335544.2; NM_176875.4; NP_795344.1.
DR UCSC; uc001mcp.4; human. [P32239-1]
DR CTD; 887; -.
DR DisGeNET; 887; -.
DR GeneCards; CCKBR; -.
DR HGNC; HGNC:1571; CCKBR.
DR HPA; ENSG00000110148; Group enriched (brain, pancreas, stomach).
DR MIM; 118445; gene.
DR neXtProt; NX_P32239; -.
DR OpenTargets; ENSG00000110148; -.
DR PharmGKB; PA26143; -.
DR VEuPathDB; HostDB:ENSG00000110148; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244933; -.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; P32239; -.
DR OMA; NTTAHKC; -.
DR OrthoDB; 1042780at2759; -.
DR PhylomeDB; P32239; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; P32239; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR SignaLink; P32239; -.
DR SIGNOR; P32239; -.
DR BioGRID-ORCS; 887; 12 hits in 1066 CRISPR screens.
DR EvolutionaryTrace; P32239; -.
DR GeneWiki; Cholecystokinin_B_receptor; -.
DR GenomeRNAi; 887; -.
DR Pharos; P32239; Tclin.
DR PRO; PR:P32239; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P32239; protein.
DR Bgee; ENSG00000110148; Expressed in Brodmann (1909) area 10 and 113 other tissues.
DR ExpressionAtlas; P32239; baseline and differential.
DR Genevisible; P32239; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; TAS:ProtInc.
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:0015054; F:gastrin receptor activity; IDA:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IPI:GO_Central.
DR GO; GO:0031741; F:type B gastrin/cholecystokinin receptor binding; IDA:NTNU_SB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0038188; P:cholecystokinin signaling pathway; IDA:GO_Central.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001696; P:gastric acid secretion; IEA:Ensembl.
DR GO; GO:0048732; P:gland development; IEA:Ensembl.
DR GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR InterPro; IPR009126; Cholcskin_rcpt.
DR InterPro; IPR000314; Gastrin_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01822; CCYSTOKININR.
DR PRINTS; PR00527; GASTRINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..447
FT /note="Gastrin/cholecystokinin type B receptor"
FT /id="PRO_0000069474"
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..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..355
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 258..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 408
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"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7887934"
FT /id="VSP_033444"
FT VAR_SEQ 271
FT /note="G -> GGAGPREQNLGEAELWRATGPAGVGGTEMKVRVRRKLEMELSWERRS
FT GGDWAGDWGDSPFSLTAHPLCSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10913157,
FT ECO:0000303|PubMed:11495676, ECO:0000303|PubMed:12429993"
FT /id="VSP_033445"
FT VARIANT 37
FT /note="L -> F (in dbSNP:rs1805000)"
FT /id="VAR_014684"
FT VARIANT 77
FT /note="V -> G (in dbSNP:rs35816985)"
FT /id="VAR_049388"
FT VARIANT 125
FT /note="V -> I (in dbSNP:rs1805002)"
FT /id="VAR_014685"
FT VARIANT 215
FT /note="R -> H (in dbSNP:rs1805004)"
FT /id="VAR_014686"
FT VARIANT 319
FT /note="R -> Q (in dbSNP:rs1805001)"
FT /id="VAR_014687"
FT CONFLICT 64
FT /note="I -> T (in Ref. 8; AAF67174)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="L -> F (in Ref. 16; AAC27510)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="L -> M (in Ref. 16; AAC27510)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="L -> I (in Ref. 16; AAC27510)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> P (in Ref. 11; AAA91831)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="F -> S (in Ref. 12; BAF84753)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> V (in Ref. 11; AAA91831)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="E -> K (in Ref. 5; AAB30766)"
FT /evidence="ECO:0000305"
FT HELIX 56..80
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 88..116
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 124..156
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 168..185
FT /evidence="ECO:0007829|PDB:7F8W"
FT TURN 186..191
FT /evidence="ECO:0007829|PDB:7F8W"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 228..248
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 327..358
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 370..390
FT /evidence="ECO:0007829|PDB:7F8W"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:7F8W"
SQ SEQUENCE 447 AA; 48419 MW; BAEEFAD4C1F85915 CRC64;
MELLKLNRSV QGTGPGPGAS LCRPGAPLLN SSSVGNLSCE PPRIRGAGTR ELELAIRITL
YAVIFLMSVG GNMLIIVVLG LSRRLRTVTN AFLLSLAVSD LLLAVACMPF TLLPNLMGTF
IFGTVICKAV SYLMGVSVSV STLSLVAIAL ERYSAICRPL QARVWQTRSH AARVIVATWL
LSGLLMVPYP VYTVVQPVGP RVLQCVHRWP SARVRQTWSV LLLLLLFFIP GVVMAVAYGL
ISRELYLGLR FDGDSDSDSQ SRVRNQGGLP GAVHQNGRCR PETGAVGEDS DGCYVQLPRS
RPALELTALT APGPGSGSRP TQAKLLAKKR VVRMLLVIVV LFFLCWLPVY SANTWRAFDG
PGAHRALSGA PISFIHLLSY ASACVNPLVY CFMHRRFRQA CLETCARCCP RPPRARPRAL
PDEDPPTPSI ASLSRLSYTT ISTLGPG
