ID   MSHR_CEBAL              Reviewed;         316 AA.
AC   Q864G9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 70.
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   Cebus albifrons (White-fronted capuchin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Cebinae; Cebus.
OX   NCBI_TaxID=9514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 1;
RX   PubMed=12687585; DOI=10.1002/ajpa.10169;
RA   Mundy N.I., Kelly J.;
RT   "Evolution of a pigmentation gene, the melanocortin-1 receptor, in
RT   primates.";
RL   Am. J. Phys. Anthropol. 121:67-80(2003).
CC   -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The
CC       activity of this receptor is mediated by G proteins which activate
CC       adenylate cyclase. Mediates melanogenesis, the production of eumelanin
CC       (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP
CC       signaling in melanocytes. {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; AY205128; AAP31002.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q864G9; -.
DR   SMR; Q864G9; -.
DR   PRIDE; Q864G9; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IEA:InterPro.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:UniProt.
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; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..316
FT                   /note="Melanocyte-stimulating hormone receptor"
FT                   /id="PRO_0000069801"
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..210
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..239
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..265
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..316
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           314
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   316 AA;  34757 MW;  F4EC6E7C387559A7 CRC64;
     MPMQGAQRKL LGSLNSTPTA TSNLGLAANH TGAPCLEVSI PDGLFLSLGL VSLVENMLVV
     AAIAKNRNLH SPMYCFICCL ALSDLLVSGS NMLETAVVVL LEAGALATRA SVVQQLHNTI
     DVLTYSSMLC SLCFVGAIAV DRYISIFYAL RYHSIMTLPR VQRVIAAIWV ASVTSSTLFI
     TYYEHVVALL CLVVFLTMLV LMAVLYVHML ARACQHAQGI TRLHKRQPPA HQGFGLRGAA
     TLTILLGIFF LCWGPFFLHL TLVVFCPQHL TCSCIFKNFK VFLTLIICNT IIDPLIYAFR
     SQELCRTLKE VLLCSW