ID   MSHR_RANTA              Reviewed;         317 AA.
AC   P56448;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=MSHR;
OS   Rangifer tarandus (Reindeer) (Cervus tarandus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Odocoileinae; Rangifer.
OX   NCBI_TaxID=9870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10628296; DOI=10.1111/j.1601-5223.1999.00039.x;
RA   Klungland H., Roed K.H., Nesbo C.L., Jakobsen K.S., Vage D.I.;
RT   "The melanocyte-stimulating hormone receptor (MC1-R) gene as a tool in
RT   evolutionary studies of artiodactyles.";
RL   Hereditas 131:39-46(1999).
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; Y13959; CAA74293.1; -; Genomic_DNA.
DR   AlphaFoldDB; P56448; -.
DR   SMR; P56448; -.
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   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..317
FT                   /note="Melanocyte-stimulating hormone receptor"
FT                   /id="PRO_0000069843"
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"
SQ   SEQUENCE   317 AA;  34895 MW;  E634FE7B4A8AEA3C CRC64;
     MPVLGSQRRL LGSLNCTPPA TFPLMLAPNR TGPQCLEVSI PNGLFLSLGL VSLVENVLVV
     AAIAKNSNLH SPMYYFICCL AVSDLLVSVS NVLETAVMLL LEAGALAARA AVVQQLDNVI
     DVLICGSMVS SLCFLGAIAV DRYISIFYAL RYHSVVTLPR AWRIIAAIWV ASILTSLLFI
     TYYNHTVVLL CLVGFFIAML ALMAVLYVHM LARACQHARG IARLQKRQRP IHRGFGLKGA
     ATLTILLGVF FLCWGPFFLH LSLIVLCPQH PTCGCIFKNF NLFLALIICN AIVDPLIYAF
     RSQELRKTLQ EVLQCSW