ID Q66XZ9_HOLMA Unreviewed; 315 AA.
AC Q66XZ9;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 86.
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:AAT90223.1};
OS Holbrookia maculata (Lesser earless lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Phrynosomatidae; Phrynosomatinae; Holbrookia.
OX NCBI_TaxID=43597 {ECO:0000313|EMBL:AAT90223.1};
RN [1] {ECO:0000313|EMBL:AAT90223.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15446431;
RA Rosenblum E.B., Hoekstra H.E., Nachman M.W.;
RT "Adaptive reptile color variation and the evolution of the Mc1r gene.";
RL Evolution 58:1794-1808(2004).
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 -!- 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; AY586107; AAT90223.1; -; Genomic_DNA.
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; 2.
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; 2.
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|RuleBase:RU000688};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361244};
KW Receptor {ECO:0000256|RuleBase:RU000688, ECO:0000313|EMBL:AAT90223.1};
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..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 234..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 274..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT DOMAIN 55..296
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 315 AA; 35823 MW; A27572DE113DD231 CRC64;
MTVPSPLRTV PGSLNATLPS DLPINVTNET FCSTDWPVVI PNELFLTLGA LSFLENLLVV
AAIVKNRNLH SPMYYFICCL AVSDMLVSIS NVVETFFMLL IDHGVLVVRS STMQQMDNVM
DMLICSSLMS SLSFLSVIAI DRYITIFYAL RYHNIMTFQR AVMVIVAIWL VSSISSXXXX
XXXXXXXXXX XXXFFLSMVI LIMALYIHMF ALARQHARRI SSMQRKQNSP QFTSMKGAIT
LTILLGVFFV CWGPFFLHLI LILTCPTHPT CTCYFSYFSL YLILVICNSV VDPIIYAFRN
QELRRTLKEV VFCFW
//
