ID   MSHR_LEOCY              Reviewed;         310 AA.
AC   Q864I1;
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 chrysomelas (Golden-headed lion tamarin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Leontopithecus.
OX   NCBI_TaxID=57374;
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; AY205116; AAP30990.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q864I1; -.
DR   SMR; Q864I1; -.
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..310
FT                   /note="Melanocyte-stimulating hormone receptor"
FT                   /id="PRO_0000069824"
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..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..183
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..203
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..258
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..271
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..310
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   310 AA;  34196 MW;  34EBDB47DECF65AB CRC64;
     MPMQGAQRKL LGSLNSTPTA TSNLGLAANR TGAPCLELPI PDGLFLSLGL VSLVENVLVV
     AAIAKNRNLH SSMYCFICCL ALSDLLVSGS NMLEAGVLAT RASVVQQLHN TIDVLTCSSM
     LCSLCFLGAI AVDRYISIFY ALRYHSIMTL PRAQRAVAAI WVASVLSSTL FITYYDHAAV
     LLCLVVFFLA MLVLMAVLYV HMLAWACQHA QGIIRLHKRQ PPAHKGFGLR GAATLTILLG
     IFFLCWGPFF LRLTLVVFCP QHLTCNCIFK NFKVFLTLII CNTIIDPLIY AFRSQELRRT
     LKEVLGRGRW