MCHR1_HUMAN
ID MCHR1_HUMAN Reviewed; 422 AA.
AC Q99705; B2RBX6; Q5R3J1; Q96S47; Q9BV08;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Melanin-concentrating hormone receptor 1;
DE Short=MCH receptor 1;
DE Short=MCH-R1;
DE Short=MCHR-1;
DE AltName: Full=G-protein coupled receptor 24;
DE AltName: Full=MCH-1R;
DE Short=MCH1R;
DE Short=MCHR;
DE AltName: Full=SLC-1;
DE AltName: Full=Somatostatin receptor-like protein;
GN Name=MCHR1; Synonyms=GPR24, SLC1;
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].
RX PubMed=10441476; DOI=10.1006/bbrc.1999.1104;
RA Shimomura Y., Mori M., Sugo T., Ishibashi Y., Abe M., Kurokawa T., Onda H.,
RA Nishimura O., Sumino Y., Fujino M.;
RT "Isolation and identification of melanin-concentrating hormone as the
RT endogenous ligand of the SLC-1 receptor.";
RL Biochem. Biophys. Res. Commun. 261:622-626(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-25; VAL-28; ASP-32; HIS-210;
RP MET-305; GLN-317; SER-377 AND MET-411, AND CHARACTERIZATION OF VARIANT
RP ASP-32.
RX PubMed=15941924; DOI=10.1530/eje.1.01917;
RA Wermter A.-K., Reichwald K., Buech T., Geller F., Platzer C., Huse K.,
RA Hess C., Remschmidt H., Gudermann T., Preibisch G., Siegfried W.,
RA Goldschmidt H.-P., Li W.-D., Price R.A., Biebermann H., Krude H.,
RA Vollmert C., Wichmann H.-E., Illig T., Soerensen T.I.A., Astrup A.,
RA Larsen L.H., Pedersen O., Eberle D., Clement K., Blundell J., Wabitsch M.,
RA Schaefer H., Platzer M., Hinney A., Hebebrand J.;
RT "Mutation analysis of the MCHR1 gene in human obesity.";
RL Eur. J. Endocrinol. 152:851-862(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-32.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-32.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-32.
RC TISSUE=Brain;
RA King M.M., 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 (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-32.
RC TISSUE=Brain;
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].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-32.
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-32.
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-422.
RX PubMed=8977118; DOI=10.1016/s0014-5793(96)01160-x;
RA Kolakowski L.F. Jr., Jung B.P., Nguyen T., Johnson M.P., Lynch K.R.,
RA Cheng R., Heng H.H.Q., George S.R., O'Dowd B.F.;
RT "Characterization of a human gene related to genes encoding somatostatin
RT receptors.";
RL FEBS Lett. 398:253-258(1996).
RN [11]
RP FUNCTION.
RX PubMed=10421367; DOI=10.1038/22313;
RA Chambers J., Ames R.S., Bergsma D., Muir A., Fitzgerald L.R., Hervieu G.,
RA Dytko G.M., Foley J.J., Martin J., Liu W.S., Park J., Ellis C., Ganguly S.,
RA Konchar S., Cluderay J., Leslie R., Wilson S., Sarau H.M.;
RT "Melanin-concentrating hormone is the cognate ligand for the orphan G-
RT protein-coupled receptor SLC-1.";
RL Nature 400:261-265(1999).
RN [12]
RP INTERACTION WITH NCDN.
RX PubMed=16945926; DOI=10.1074/jbc.m602889200;
RA Francke F., Ward R.J., Jenkins L., Kellett E., Richter D., Milligan G.,
RA Baechner D.;
RT "Interaction of neurochondrin with the melanin-concentrating hormone
RT receptor 1 interferes with G protein-coupled signal transduction but not
RT agonist-mediated internalization.";
RL J. Biol. Chem. 281:32496-32507(2006).
RN [13]
RP VARIANTS HIS-250 AND GLN-317, AND CHARACTERIZATION OF VARIANT GLN-317.
RX PubMed=15166293; DOI=10.1038/oby.2004.89;
RA Gibson W.T., Pissios P., Trombly D.J., Luan J., Keogh J., Wareham N.J.,
RA Maratos-Flier E., O'Rahilly S., Farooqi I.S.;
RT "Melanin-concentrating hormone receptor mutations and human obesity:
RT functional analysis.";
RL Obes. Res. 12:743-749(2004).
RN [14]
RP VARIANT ARG-34, AND CHARACTERIZATION OF VARIANT ARG-34.
RX PubMed=15340116; DOI=10.1038/oby.2004.167;
RA Hawes B.E., Green B., O'Neill K., Fried S., Arreaza M.G., Qiu P.,
RA Simon J.S.;
RT "Identification and characterization of single-nucleotide polymorphisms in
RT MCH-R1 and MCH-R2.";
RL Obes. Res. 12:1327-1334(2004).
CC -!- FUNCTION: Receptor for melanin-concentrating hormone, coupled to both G
CC proteins that inhibit adenylyl cyclase and G proteins that activate
CC phosphoinositide hydrolysis. {ECO:0000269|PubMed:10421367}.
CC -!- SUBUNIT: Interacts with NCDN. {ECO:0000269|PubMed:16945926}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highest level in brain, particularly in the frontal
CC cortex and hypothalamus, lower levels in the liver and heart.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-6 or Met-70 is the
CC initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14587.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB063174; BAB60890.1; -; mRNA.
DR EMBL; AF490537; AAO14670.1; -; mRNA.
DR EMBL; CR456497; CAG30383.1; -; mRNA.
DR EMBL; BT006725; AAP35371.1; -; mRNA.
DR EMBL; AY562945; AAS72373.1; -; mRNA.
DR EMBL; AK314857; BAG37373.1; -; mRNA.
DR EMBL; Z86090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60388.1; -; Genomic_DNA.
DR EMBL; BC001736; AAH01736.1; -; mRNA.
DR EMBL; BC021146; AAH21146.1; -; mRNA.
DR EMBL; U71092; AAC14587.1; ALT_SEQ; Genomic_DNA.
DR PIR; JC7080; JC7080.
DR RefSeq; NP_005288.3; NM_005297.3.
DR AlphaFoldDB; Q99705; -.
DR SMR; Q99705; -.
DR STRING; 9606.ENSP00000249016; -.
DR BindingDB; Q99705; -.
DR ChEMBL; CHEMBL344; -.
DR DrugBank; DB00502; Haloperidol.
DR GuidetoPHARMACOLOGY; 280; -.
DR TCDB; 9.A.14.13.6; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q99705; 3 sites.
DR iPTMnet; Q99705; -.
DR PhosphoSitePlus; Q99705; -.
DR BioMuta; MCHR1; -.
DR DMDM; 33860175; -.
DR PaxDb; Q99705; -.
DR PeptideAtlas; Q99705; -.
DR PRIDE; Q99705; -.
DR Antibodypedia; 300; 325 antibodies from 33 providers.
DR DNASU; 2847; -.
DR Ensembl; ENST00000249016.5; ENSP00000249016.5; ENSG00000128285.5.
DR GeneID; 2847; -.
DR KEGG; hsa:2847; -.
DR UCSC; uc003ayz.4; human.
DR CTD; 2847; -.
DR DisGeNET; 2847; -.
DR GeneCards; MCHR1; -.
DR HGNC; HGNC:4479; MCHR1.
DR HPA; ENSG00000128285; Tissue enhanced (brain, endometrium).
DR MIM; 601751; gene.
DR neXtProt; NX_Q99705; -.
DR PharmGKB; PA28867; -.
DR VEuPathDB; HostDB:ENSG00000128285; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; Q99705; -.
DR OMA; KSKFHGC; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; Q99705; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; Q99705; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; Q99705; -.
DR SIGNOR; Q99705; -.
DR BioGRID-ORCS; 2847; 11 hits in 1062 CRISPR screens.
DR ChiTaRS; MCHR1; human.
DR GeneWiki; Melanin-concentrating_hormone_receptor_1; -.
DR GenomeRNAi; 2847; -.
DR Pharos; Q99705; Tchem.
DR PRO; PR:Q99705; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q99705; protein.
DR Bgee; ENSG00000128285; Expressed in endothelial cell and 114 other tissues.
DR ExpressionAtlas; Q99705; baseline and differential.
DR Genevisible; Q99705; HS.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042562; F:hormone binding; IEA:Ensembl.
DR GO; GO:0030273; F:melanin-concentrating hormone receptor activity; IEA:Ensembl.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; TAS:ProtInc.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007631; P:feeding behavior; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR008361; MCH_rcpt.
DR InterPro; IPR004047; MCHR1.
DR PANTHER; PTHR24229:SF91; PTHR24229:SF91; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01507; MCH1RECEPTOR.
DR PRINTS; PR01783; MCHRECEPTOR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..422
FT /note="Melanin-concentrating hormone receptor 1"
FT /id="PRO_0000069734"
FT TOPO_DOM 1..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..136
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..171
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..208
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..250
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..301
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..344
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..381
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 25
FT /note="T -> M (in dbSNP:rs117372135)"
FT /evidence="ECO:0000269|PubMed:15941924"
FT /id="VAR_026652"
FT VARIANT 28
FT /note="D -> V (in dbSNP:rs112405400)"
FT /evidence="ECO:0000269|PubMed:15941924"
FT /id="VAR_026653"
FT VARIANT 32
FT /note="N -> D (no significant functional differences;
FT dbSNP:rs133072)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15941924, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.8"
FT /id="VAR_016221"
FT VARIANT 34
FT /note="G -> R (no changes in receptor binding or functional
FT signaling; dbSNP:rs765971090)"
FT /evidence="ECO:0000269|PubMed:15340116"
FT /id="VAR_026654"
FT VARIANT 103
FT /note="G -> R (in dbSNP:rs11914085)"
FT /id="VAR_049417"
FT VARIANT 210
FT /note="R -> H (in dbSNP:rs750210146)"
FT /evidence="ECO:0000269|PubMed:15941924"
FT /id="VAR_026655"
FT VARIANT 250
FT /note="Y -> H"
FT /evidence="ECO:0000269|PubMed:15166293"
FT /id="VAR_026656"
FT VARIANT 305
FT /note="T -> M (in dbSNP:rs550313335)"
FT /evidence="ECO:0000269|PubMed:15941924"
FT /id="VAR_026657"
FT VARIANT 317
FT /note="R -> Q (in dbSNP:rs45439291)"
FT /evidence="ECO:0000269|PubMed:15166293,
FT ECO:0000269|PubMed:15941924"
FT /id="VAR_026658"
FT VARIANT 377
FT /note="P -> S (in dbSNP:rs539260735)"
FT /evidence="ECO:0000269|PubMed:15941924"
FT /id="VAR_026659"
FT VARIANT 411
FT /note="T -> M (in dbSNP:rs149604804)"
FT /evidence="ECO:0000269|PubMed:15941924"
FT /id="VAR_026660"
SQ SEQUENCE 422 AA; 45963 MW; 3986919A18183818 CRC64;
MSVGAMKKGV GRAVGLGGGS GCQATEEDPL PNCGACAPGQ GGRRWRLPQP AWVEGSSARL
WEQATGTGWM DLEASLLPTG PNASNTSDGP DNLTSAGSPP RTGSISYINI IMPSVFGTIC
LLGIIGNSTV IFAVVKKSKL HWCNNVPDIF IINLSVVDLL FLLGMPFMIH QLMGNGVWHF
GETMCTLITA MDANSQFTST YILTAMAIDR YLATVHPISS TKFRKPSVAT LVICLLWALS
FISITPVWLY ARLIPFPGGA VGCGIRLPNP DTDLYWFTLY QFFLAFALPF VVITAAYVRI
LQRMTSSVAP ASQRSIRLRT KRVTRTAIAI CLVFFVCWAP YYVLQLTQLS ISRPTLTFVY
LYNAAISLGY ANSCLNPFVY IVLCETFRKR LVLSVKPAAQ GQLRAVSNAQ TADEERTESK
GT
