ID K0IT51_MARZI Unreviewed; 302 AA.
AC K0IT51;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Melanocyte-stimulating hormone receptor {ECO:0000256|ARBA:ARBA00020454, ECO:0000256|RuleBase:RU361244};
DE Short=MSH-R {ECO:0000256|RuleBase:RU361244};
DE AltName: Full=Melanocortin receptor 1 {ECO:0000256|ARBA:ARBA00031491, ECO:0000256|RuleBase:RU361244};
GN Name=Mc1r {ECO:0000313|EMBL:BAM45479.1};
OS Martes zibellina (Sable).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Guloninae; Martes.
OX NCBI_TaxID=36722 {ECO:0000313|EMBL:BAM45479.1};
RN [1] {ECO:0000313|EMBL:BAM45479.1}
RP NUCLEOTIDE SEQUENCE.
RA Ishida K., Sato J.J., Kinoshita G., Hosoda T., Kryukov A.P., Suzuki H.;
RT "Evolutionary history of the sable (Martes zibellina brachyura) on Hokkaido
RT inferred from mitochondrial Cytb and nuclear Mc1r and Tcf25 gene
RT sequences.";
RL Acta Theriol. 58:13-24(2013).
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. {ECO:0000256|RuleBase:RU361244}.
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:0000256|ARBA:ARBA00023466}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361244}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361244}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
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DR EMBL; AB725461; BAM45479.1; -; Genomic_DNA.
DR AlphaFoldDB; K0IT51; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR22750:SF2; MELANOCYTE-STIMULATING HORMONE RECEPTOR; 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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 {ECO:0000256|RuleBase:RU361244};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU000688};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361244};
KW Receptor {ECO:0000256|RuleBase:RU000688, ECO:0000313|EMBL:BAM45479.1};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361244}.
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 172..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 220..244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 264..285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT DOMAIN 55..283
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 33408 MW; 88F0103CCE6259C4 CRC64;
MSVQGPQRRL LGSLNSTPPA TPPLRPPTNQ TGPQFLEVSV PDGLFLGLGL VSVLENVLVV
AAIAKNRSLH SPMYYFICCL AVSDLLVSVS NVLEMAVVQQ LDDAIDVLVC GAMVSSLCFL
GAIAVDRYIS IFYALRYHSI VTLARAWRAI SAIWLAGVLS GTLFIAYHNH VAVLLCLVSF
FVAMLVLMVG LYVHMLARAC QHARRIARLR KRQRPARQGF SLKGTATLTV LLGIFFLCWG
PFFLHLSLMV LCPQHPICGC VFKNFNLFLT LIICNSIVDP LIYAFRSQEL RKTLQEVVLC
SW
//
