MCHR1_MOUSE
ID MCHR1_MOUSE Reviewed; 353 AA.
AC Q8JZL2; Q3UY93; Q8K3M8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 3.
DT 03-AUG-2022, entry version 151.
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 {ECO:0000303|PubMed:11159839};
DE AltName: Full=Somatostatin receptor-like protein;
GN Name=Mchr1; Synonyms=Gpr24, Slc1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Tail;
RX PubMed=11159839; DOI=10.1210/endo.142.2.7981;
RA Kokkotou E.G., Tritos N.A., Mastaitis J.W., Slieker L., Maratos-Flier E.;
RT "Melanin-concentrating hormone receptor is a target of leptin action in the
RT mouse brain.";
RL Endocrinology 142:680-686(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE
RP PROMOTER USAGE.
RC STRAIN=129/SvJ;
RX PubMed=15093132; DOI=10.1016/j.bbaexp.2004.01.006;
RA Lakaye B., Adamantidis A., Coumans B., Grisar T.;
RT "Promoter characterization of the mouse melanin-concentrating hormone
RT receptor 1.";
RL Biochim. Biophys. Acta 1678:1-6(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
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.
CC -!- SUBUNIT: Interacts with NCDN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=Q8JZL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8JZL2-2; Sequence=VSP_059222;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the brain. Expression in
CC brain is negatively regulated by leptin. Also found in the epithelium
CC of the tongue and kidney. {ECO:0000269|PubMed:11159839}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF498247; AAM22964.1; -; mRNA.
DR EMBL; AF498248; AAM22965.1; -; mRNA.
DR EMBL; AY049011; AAL06069.1; -; Genomic_DNA.
DR EMBL; AY049011; AAL06070.1; -; Genomic_DNA.
DR EMBL; AK134867; BAE22319.1; -; mRNA.
DR EMBL; AC102334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128286; AAI28287.1; -; mRNA.
DR CCDS; CCDS49675.1; -. [Q8JZL2-1]
DR RefSeq; NP_660114.1; NM_145132.2. [Q8JZL2-1]
DR AlphaFoldDB; Q8JZL2; -.
DR SMR; Q8JZL2; -.
DR STRING; 10090.ENSMUSP00000126191; -.
DR ChEMBL; CHEMBL4730; -.
DR GlyGen; Q8JZL2; 3 sites.
DR iPTMnet; Q8JZL2; -.
DR PhosphoSitePlus; Q8JZL2; -.
DR jPOST; Q8JZL2; -.
DR PaxDb; Q8JZL2; -.
DR PRIDE; Q8JZL2; -.
DR ProteomicsDB; 292275; -. [Q8JZL2-1]
DR ProteomicsDB; 292276; -. [Q8JZL2-2]
DR Antibodypedia; 300; 325 antibodies from 33 providers.
DR DNASU; 207911; -.
DR Ensembl; ENSMUST00000166855; ENSMUSP00000126191; ENSMUSG00000050164. [Q8JZL2-1]
DR GeneID; 207911; -.
DR KEGG; mmu:207911; -.
DR UCSC; uc007wwh.2; mouse. [Q8JZL2-1]
DR CTD; 2847; -.
DR MGI; MGI:2180756; Mchr1.
DR VEuPathDB; HostDB:ENSMUSG00000050164; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154272; -.
DR InParanoid; Q8JZL2; -.
DR OMA; KSKFHGC; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; Q8JZL2; -.
DR TreeFam; TF315737; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR BioGRID-ORCS; 207911; 5 hits in 75 CRISPR screens.
DR PRO; PR:Q8JZL2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8JZL2; protein.
DR Bgee; ENSMUSG00000050164; Expressed in lumbar subsegment of spinal cord and 71 other tissues.
DR GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0097730; C:non-motile cilium; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0030273; F:melanin-concentrating hormone receptor activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0060259; P:regulation of feeding behavior; TAS:BHF-UCL.
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 Alternative promoter usage; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..353
FT /note="Melanin-concentrating hormone receptor 1"
FT /id="PRO_0000069736"
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 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"
FT VAR_SEQ 1..27
FT /note="MDLQASLLSTGPNASNISDGQDNFTLA -> MRGQQEGRHGRLSASRSEGGS
FT HLLFLSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15093132"
FT /id="VSP_059222"
SQ SEQUENCE 353 AA; 39120 MW; D85D186EB1A4AEF9 CRC64;
MDLQASLLST GPNASNISDG QDNFTLAGPP PRTRSVSYIN IIMPSVFGTI CLLGIVGNST
VIFAVVKKSK LHWCSNVPDI FIINLSVVDL LFLLGMPFMI HQLMGNGVWH FGETMCTLIT
AMDANSQFTS TYILTAMAID RYLATVHPIS STKFRKPSMA TLVICLLWAL SFISITPVWL
YARLIPFPGG AVGCGIRLPN PDTDLYWFTL YQFFLAFALP FVVITAAYVK ILQRMTSSVA
PASQRSIRLR TKRVTRTAIA ICLVFFVCWA PYYVLQLTQL SISRPTLTFV YLYNAAISLG
YANSCLNPFV YIVLCETFRK RLVLSVKPAA QGQLRTVSNA QTADEERTES KGT
