MSHR_SHEEP
ID MSHR_SHEEP Reviewed; 317 AA.
AC O19037;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
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; Y13965; CAA74298.1; -; Genomic_DNA.
DR RefSeq; NP_001269457.1; NM_001282528.1.
DR AlphaFoldDB; O19037; -.
DR SMR; O19037; -.
DR Ensembl; ENSOART00020005369; ENSOARP00020004424; ENSOARG00020003524.
DR GeneID; 102099064; -.
DR KEGG; oas:102099064; -.
DR CTD; 4157; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 981062at2759; -.
DR Proteomes; UP000002356; Unplaced.
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:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0070914; P:UV-damage excision repair; IEA:Ensembl.
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_0000069851"
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; 34919 MW; AF67F718E249E1B0 CRC64;
MPVLGSQRRL LGSLNCTPPA TLPLTLAPNR TGPQCLEVSI PDGLFLSLGL VSLVENVLVV
AAIAKNRNLH SPMYYFICCL AMSDLLVSVS NVLETAVMLL LEAGVLATRA AVVQQLDNVI
DVLICSSMVS SLCFLGAIAV DRYISIFYAL RYHSVVTLPR AWRIIAAIWV ASILTSVLSI
TYYNHTVVLL CLVGFFIAML ALMAVLYVHM LARACQHARG IARLQKRQRP IHQGFGLKGA
ATLTILLGVF FLCWGPFFLH LSLIVLCPQH PTCGCIFKNF NLFLALIICN AIVDPLIYAF
RSQELRKTLQ EVLQCSW
