ID G9CTS8_TAPPI Unreviewed; 277 AA.
AC G9CTS8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
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};
DE Flags: Fragment;
GN Name=MC1R {ECO:0000313|EMBL:AEU10915.1};
OS Tapirus pinchaque (Mountain tapir).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Tapiridae; Tapirus.
OX NCBI_TaxID=30582 {ECO:0000313|EMBL:AEU10915.1};
RN [1] {ECO:0000313|EMBL:AEU10915.1}
RP NUCLEOTIDE SEQUENCE.
RA Steiner C.C., Ryder O.A.;
RT "Molecular phylogeny and evolution of the Perissodactyla.";
RL Zool. J. Linn. Soc. 163:1289-1303(2011).
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; JF718946; AEU10915.1; -; Genomic_DNA.
DR AlphaFoldDB; G9CTS8; -.
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:AEU10915.1};
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 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 47..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 91..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 159..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 207..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT DOMAIN 27..270
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEU10915.1"
FT NON_TER 277
FT /evidence="ECO:0000313|EMBL:AEU10915.1"
SQ SEQUENCE 277 AA; 30753 MW; B65A8E8B5DDE1A0B CRC64;
NQTGHWCMEV LIPDGLFLSL GLVSLVENVL VVAAITKNRN LHSPMYYFIC CLAVSDLLVS
VSNVLDTAIL LLLEAGTLAI RASVVQQLDD VIDVLICGSM VSSLCFLGAI AVDRYISIFY
ALRYHSIVTL PRAWHAITAI WVASVLSSTL FIAYYNHTAV LLCLVSFFVA MLALMAVLYL
HMLARACQHA RGIARLHKRQ HPVHQSFGLK GAATLTILMG IFFLCWGPFF LHLLLILLCP
QHPTCGCVFK NFKLFLTLII CNAIIDPLIY AFRSQEL
//
