MSHR_VULLA
ID MSHR_VULLA Reviewed; 317 AA.
AC Q6A155; Q6A154;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 Vulpes lagopus (Arctic fox) (Alopex lagopus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=494514;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-5 AND CYS-280.
RA Vage D.;
RT "A MC1R mutation prevent expression of the winter white coat phenotype of
RT the arctic fox (Alopex lagopus).";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH (By
CC similarity). The activity of this receptor is mediated by G proteins
CC which activate adenylate cyclase (By similarity). Mediates
CC melanogenesis, the production of eumelanin (black/brown) and
CC phaeomelanin (red/yellow), via regulation of cAMP signaling in
CC melanocytes (By similarity). {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 -!- POLYMORPHISM: The variations in positions 5 and 280 are associated with
CC the expression of the winter white coat phenotype. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AJ786717; CAH10740.1; -; Genomic_DNA.
DR EMBL; AJ786718; CAH10741.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6A155; -.
DR SMR; Q6A155; -.
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_0000069787"
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"
FT VARIANT 5
FT /note="G -> C (in allele blue fox)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 280
FT /note="F -> C (in allele blue fox)"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 317 AA; 34887 MW; D130F6B6D9509C98 CRC64;
MSGQGPQRRL LGSLNATSPT TPHFKLAANQ TGPRCLEVSI PDGLFLSLGL VSVVENVLVV
AAIAKNRNLH SPMYYFIGCL AVSDLLVSVT NVLETAVMLL VEAGALAAQA AVVQQLDDII
DVLICGSMVS SLCFLGAIAV DRYLSIFYAL RYHSIVTLPR AWRAISAIWV ASVLSSTLFI
AYYNHTAVLL CLVSFFVAML VLMAVLYVHM LARARQHARG IARLRKRQHS VHQGFGLKGA
ATLTILLGIF FLCWGPFFLH LSLMVLCPQH PICGCVFQNF NLFLTLIICN SIIDPFIYAF
RSQELRKTLQ EVVLCSW
