MSHR_MOUSE
ID MSHR_MOUSE Reviewed; 315 AA.
AC Q01727; Q75NA3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Melanocyte-stimulating hormone receptor;
DE Short=MSH-R;
DE AltName: Full=Melanocortin receptor 1;
DE Short=MC1-R;
GN Name=Mc1r; Synonyms=Msh-r;
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], AND FUNCTION.
RC TISSUE=Skin;
RX PubMed=1325670; DOI=10.1126/science.1325670;
RA Mountjoy K.G., Robbins L.S., Mortrud M., Cone R.D.;
RT "The cloning of a family of genes that encode the melanocortin receptors.";
RL Science 257:1248-1251(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MSM/Ms;
RX PubMed=15653560; DOI=10.1093/jhered/esi022;
RA Wada A., Kunieda T., Nishimura M., Kakizoe-Ishida Y., Watanabe N.,
RA Ohkawa K., Tsudzuki M.;
RT "A nucleotide substitution responsible for the tawny coat color mutation
RT carried by the MSKR inbred strain of mice.";
RL J. Hered. 96:145-149(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH
CC (PubMed:1325670). The activity of this receptor is mediated by G
CC proteins which activate adenylate cyclase (PubMed:1325670). Mediates
CC melanogenesis, the production of eumelanin (black/brown) and
CC phaeomelanin (red/yellow), via regulation of cAMP signaling in
CC melanocytes (By similarity). {ECO:0000250|UniProtKB:Q01726,
CC ECO:0000269|PubMed:1325670}.
CC -!- SUBUNIT: Interacts with MGRN1, but does not undergo MGRN1-mediated
CC ubiquitination; this interaction competes with GNAS-binding and thus
CC inhibits agonist-induced cAMP production. Interacts with OPN3; the
CC interaction results in a decrease in MC1R-mediated cAMP signaling and
CC ultimately a decrease in melanin production in melanocytes.
CC {ECO:0000250|UniProtKB:Q01726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01726};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X65635; CAA46589.1; -; mRNA.
DR EMBL; AB177607; BAD16659.1; -; Genomic_DNA.
DR EMBL; AB177608; BAD16660.1; -; Genomic_DNA.
DR EMBL; AB306322; BAG85190.1; -; Genomic_DNA.
DR EMBL; CH466525; EDL11741.1; -; Genomic_DNA.
DR EMBL; BC119294; AAI19295.1; -; mRNA.
DR EMBL; BC119296; AAI19297.1; -; mRNA.
DR CCDS; CCDS22756.1; -.
DR PIR; S25581; S25581.
DR RefSeq; NP_032585.2; NM_008559.2.
DR AlphaFoldDB; Q01727; -.
DR SMR; Q01727; -.
DR BioGRID; 201338; 2.
DR STRING; 10090.ENSMUSP00000095929; -.
DR BindingDB; Q01727; -.
DR ChEMBL; CHEMBL4077; -.
DR GuidetoPHARMACOLOGY; 282; -.
DR GlyGen; Q01727; 2 sites.
DR PhosphoSitePlus; Q01727; -.
DR PaxDb; Q01727; -.
DR PRIDE; Q01727; -.
DR Antibodypedia; 54873; 373 antibodies from 34 providers.
DR DNASU; 17199; -.
DR Ensembl; ENSMUST00000098324; ENSMUSP00000095929; ENSMUSG00000074037.
DR GeneID; 17199; -.
DR KEGG; mmu:17199; -.
DR UCSC; uc009nvs.2; mouse.
DR CTD; 4157; -.
DR MGI; MGI:99456; Mc1r.
DR VEuPathDB; HostDB:ENSMUSG00000074037; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; Q01727; -.
DR OMA; FFCTTLV; -.
DR OrthoDB; 981062at2759; -.
DR PhylomeDB; Q01727; -.
DR TreeFam; TF332646; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 17199; 5 hits in 111 CRISPR screens.
DR ChiTaRS; Mc1r; mouse.
DR PRO; PR:Q01727; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q01727; protein.
DR Bgee; ENSMUSG00000074037; Expressed in hair follicle and 9 other tissues.
DR ExpressionAtlas; Q01727; baseline and differential.
DR Genevisible; Q01727; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0004977; F:melanocortin receptor activity; IDA:BHF-UCL.
DR GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:BHF-UCL.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IEA:Ensembl.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0070914; P:UV-damage excision repair; ISO:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001671; Melcrt_ACTH_rcpt.
DR InterPro; IPR000761; MSH_rcpt.
DR PANTHER; PTHR22750:SF2; PTHR22750:SF2; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00534; MCRFAMILY.
DR PRINTS; PR00536; MELNOCYTESHR.
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 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..315
FT /note="Melanocyte-stimulating hormone receptor"
FT /id="PRO_0000069834"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..264
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 313
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 101
FT /note="A -> V (in Ref. 1; CAA46589)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="A -> V (in Ref. 1; CAA46589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 35226 MW; 9240C7D02B336235 CRC64;
MSTQEPQKSL LGSLNSNATS HLGLATNQSE PWCLYVSIPD GLFLSLGLVS LVENVLVVIA
ITKNRNLHSP MYYFICCLAL SDLMVSVSIV LETTIILLLE AGILVARVAL VQQLDNLIDV
LICGSMVSSL CFLGIIAIDR YISIFYALRY HSIVTLPRAR RAVVGIWMVS IVSSTLFITY
YKHTAVLLCL VTFFLAMLAL MAILYAHMFT RACQHAQGIA QLHKRRRSIR QGFCLKGAAT
LTILLGIFFL CWGPFFLHLL LIVLCPQHPT CSCIFKNFNL FLLLIVLSST VDPLIYAFRS
QELRMTLKEV LLCSW
