MSHR_HORSE
ID MSHR_HORSE Reviewed; 317 AA.
AC P79166; Q95MP3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Melanocyte-stimulating hormone receptor;
DE Short=MSH-R;
DE AltName: Full=Melanocortin receptor 1;
DE Short=MC1-R;
GN Name=MC1R;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-83.
RX PubMed=11353392; DOI=10.1007/s003350020017;
RA Rieder S., Taourit S., Mariat D., Langlois B., Guerin G.;
RT "Mutations in the agouti (ASIP), the extension (MC1R), and the brown
RT (TYRP1) loci and their association to coat color phenotypes in horses
RT (Equus caballus).";
RL Mamm. Genome 12:450-455(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-308, AND VARIANT PHE-83.
RX PubMed=8995760; DOI=10.1007/s003359900264;
RA Marklund L., Moller M.J., Sandberg K., Andersson L.;
RT "A missense mutation in the gene for melanocyte-stimulating hormone
RT receptor (MC1R) is associated with the chestnut coat color in horses.";
RL Mamm. Genome 7:895-899(1996).
CC -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH (By
CC similarity). The activity of this receptor is mediated by G proteins
CC which activate adenylate cyclase (By similarity). 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 -!- 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; AF288357; AAK70924.1; -; Genomic_DNA.
DR EMBL; X98012; CAA66641.1; -; Genomic_DNA.
DR RefSeq; NP_001108006.1; NM_001114534.1.
DR AlphaFoldDB; P79166; -.
DR SMR; P79166; -.
DR PaxDb; P79166; -.
DR GeneID; 100136907; -.
DR KEGG; ecb:100136907; -.
DR CTD; 4157; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; P79166; -.
DR OMA; FFCTTLV; -.
DR OrthoDB; 981062at2759; -.
DR TreeFam; TF332646; -.
DR Proteomes; UP000002281; Unplaced.
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:0004980; F:melanocyte-stimulating hormone receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Melanocyte-stimulating hormone receptor"
FT /id="PRO_0000069817"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 315
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 83
FT /note="S -> F (in chesnut color)"
FT /evidence="ECO:0000269|PubMed:11353392,
FT ECO:0000269|PubMed:8995760"
SQ SEQUENCE 317 AA; 35213 MW; 011B644FEBAF8E09 CRC64;
MPLQGPQRRL LGSLNSTLPA TPYLGLTTNQ TEPPCLEVSI PDGLFLSLGL VSLVENVLVV
TAIAKNRNLH SPMYYFICCL AVSDLLVSMS NVLEMAILLL LEAGVLATQA SVLQQLDNII
DVLICGSMVS SLCFLGSIAV DRYISIFYAL RYHSIMMLPR VWRAIVAIWV VSVLSSTLFI
AYYNHTAVLL CLVTFFVAML VLMAVLYVHM LARACQHARG IARLHKRQHP IHQGFGLKGA
ATLTILLGVF FLCWGPFFLH LSLLILCPQH PTCGCVFKNF KLFLTLILCS AIVDPLIYAF
RSQELRKTLQ EVLLCSW
