MSHR_GORGO
ID MSHR_GORGO Reviewed; 316 AA.
AC Q864K9; Q2KP11; Q2KP12;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-93.
RC STRAIN=Isolate Snowflake, and Isolate Urko;
RA Roy R., Cantero M., Jimenez-Cervantes C., Garcia-Borron J.C., Montoliu L.;
RT "Analysis of 5' upstream regulatory sequences and LCR-like region of the
RT Gorilla tyrosinase locus.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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; AY205088; AAP30962.1; -; Genomic_DNA.
DR EMBL; AY875715; AAX82900.1; -; Genomic_DNA.
DR EMBL; AY875716; AAX82901.1; -; Genomic_DNA.
DR AlphaFoldDB; Q864K9; -.
DR SMR; Q864K9; -.
DR STRING; 9593.ENSGGOP00000019912; -.
DR eggNOG; KOG1375; Eukaryota.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q864K9; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
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..316
FT /note="Melanocyte-stimulating hormone receptor"
FT /id="PRO_0000069814"
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..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..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"
FT VARIANT 93
FT /note="V -> L (in Isolate Urko)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_028852"
SQ SEQUENCE 316 AA; 34692 MW; A35B4669EF3EC9D7 CRC64;
MAVQGSQRRL LGSLNSTPTA IPQLGLAANQ TGARCLEVSI PDGLFLSLGL VSLVENVLVV
ATIAKNRNLH SPMYCFICCL ALSDLLVSGS NVVDTLLLLL EAGALAARAA VLQQLDNVID
VITCSSMLSS LCFLGAIAVD RYISIFYALR YRSIVTLPRA RRAVAAIWVA SVLFSTLFIA
YYDHTAVLLC LVVFFLAMLV LMAVLYVHML ARACQHAQGI ARLHKRQRPV HKGFGLKGPV
TLTILLGIFF LCWGPFFLHL TLIVLCPEHP TCGCIFKNFN LFLALIICNA IIDPLIYAFH
SQELRRTLKE VLTCSW
