ID   MSHR_LEORO              Reviewed;         318 AA.
AC   Q864I3;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Leontopithecus rosalia (Golden lion tamarin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Leontopithecus.
OX   NCBI_TaxID=30588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 490;
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; AY205114; AAP30988.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q864I3; -.
DR   SMR; Q864I3; -.
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; Membrane;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..318
FT                   /note="Melanocyte-stimulating hormone receptor"
FT                   /id="PRO_0000069825"
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   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  35080 MW;  2BB2132178306471 CRC64;
     MPMQGAQRKL LGSLNSTPTA TSNLGLAANR TGAPCLELPI PNGLFLSLGL VSLVENVLVV
     AAIAKNRNLH SSMYCFICCL ALSDLLVSGS NMLETAVILL LEAGVLATRA SVVQQLHNTI
     DVLTCSSMLC SLCFLGAIAV DRYISIFYAL RYHSIMTLPR AQRAVAAIWV ASVLSSTLFI
     TYYDHAAVLL CLMVFFLAML VLMAVLYVHM LARARQHAQG IIRLHKRQPP AHKGFGLRGA
     ATLTILLGIF FLCWGPFFLC LTLVVFCPQH LTCNCIFKNF KVFLTLIICN TIIDPLIYAF
     RSQELRRMLK EVLGRGRW