MCHR1_RAT
ID MCHR1_RAT Reviewed; 353 AA.
AC P97639; A0A140TAD3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 4.
DT 03-AUG-2022, entry version 154.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9531978; DOI=10.1016/s0167-4889(97)00135-3;
RA Lakaye B., Minet A., Zorzi W., Grisar T.;
RT "Cloning of the rat brain cDNA encoding for the SLC-1 G protein-coupled
RT receptor reveals the presence of an intron in the gene.";
RL Biochim. Biophys. Acta 1401:216-220(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-300.
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 [5]
RP FUNCTION.
RX PubMed=10559938; DOI=10.1038/12978;
RA Lembo P.M.C., Grazzini E., Cao J., Hubatsch D.A., Pelletier M., Hoffert C.,
RA St Onge S., Pou C., Labrecque J., Groblewski T., O'Donnell D., Payza K.,
RA Ahmad S., Walker P.;
RT "The receptor for the orexigenic peptide melanin-concentrating hormone is a
RT G-protein-coupled receptor.";
RL Nat. Cell Biol. 1:267-271(1999).
RN [6]
RP FUNCTION.
RX PubMed=10421368; DOI=10.1038/22321;
RA Saito Y., Nothacker H.P., Wang Z., Lin S.H., Leslie F., Civelli O.;
RT "Molecular characterization of the melanin-concentrating-hormone
RT receptor.";
RL Nature 400:265-269(1999).
CC -!- FUNCTION: Receptor for melanin-concentrating hormone, coupled to G
CC proteins that inhibit adenylyl cyclase. {ECO:0000269|PubMed:10421368,
CC ECO:0000269|PubMed:10559938}.
CC -!- SUBUNIT: Interacts with NCDN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: High level in the brain, moderate amounts in the
CC eye and skeletal muscle, and small amounts in tongue and pituitary.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF008650; AAC27977.1; -; mRNA.
DR EMBL; AABR07058532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473950; EDM15736.1; -; Genomic_DNA.
DR EMBL; U77953; AAC14588.1; -; Genomic_DNA.
DR RefSeq; NP_113946.1; NM_031758.1.
DR AlphaFoldDB; P97639; -.
DR SMR; P97639; -.
DR IntAct; P97639; 1.
DR MINT; P97639; -.
DR STRING; 10116.ENSRNOP00000025564; -.
DR BindingDB; P97639; -.
DR ChEMBL; CHEMBL1075228; -.
DR GuidetoPHARMACOLOGY; 280; -.
DR GlyGen; P97639; 3 sites.
DR PhosphoSitePlus; P97639; -.
DR PaxDb; P97639; -.
DR Ensembl; ENSRNOT00000025564; ENSRNOP00000025564; ENSRNOG00000018895.
DR GeneID; 83567; -.
DR KEGG; rno:83567; -.
DR UCSC; RGD:619841; rat.
DR CTD; 2847; -.
DR RGD; 619841; Mchr1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154272; -.
DR InParanoid; P97639; -.
DR OMA; KSKFHGC; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P97639; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:P97639; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000018895; Expressed in cerebral cortex and 5 other tissues.
DR GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042562; F:hormone binding; IDA:RGD.
DR GO; GO:0030273; F:melanin-concentrating hormone receptor activity; IDA:RGD.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..353
FT /note="Melanin-concentrating hormone receptor 1"
FT /id="PRO_0000069739"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..116
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..204
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..294
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 353 AA; 39063 MW; F6EEB2DF381084A9 CRC64;
MDLQTSLLST GPNASNISDG QDNLTLPGSP PRTGSVSYIN IIMPSVFGTI CLLGIVGNST
VIFAVVKKSK LHWCSNVPDI FIINLSVVDL LFLLGMPFMI HQLMGNGVWH FGETMCTLIT
AMDANSQFTS TYILTAMTID RYLATVHPIS STKFRKPSMA TLVICLLWAL SFISITPVWL
YARLIPFPGG AVGCGIRLPN PDTDLYWFTL YQFFLAFALP FVVITAAYVK ILQRMTSSVA
PASQRSIRLR TKRVTRTAIA ICLVFFVCWA PYYVLQLTQL SISRPTLTFV YLYNAAISLG
YANSCLNPFV YIVLCETFRK RLVLSVKPAA QGQLRTVSNA QTADEERTES KGT
