ID B7TVL1_PERPL Unreviewed; 268 AA.
AC B7TVL1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 22-FEB-2023, entry version 59.
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:ACK76634.1};
OS Peromyscus polionotus niveiventris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Peromyscus.
OX NCBI_TaxID=423565 {ECO:0000313|EMBL:ACK76634.1};
RN [1] {ECO:0000313|EMBL:ACK76634.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N_1 {ECO:0000313|EMBL:ACK76634.1};
RX PubMed=18832078; DOI=10.1093/molbev/msn218;
RA Steiner C.C., Rompler H., Boettger L.M., Schoneberg T., Hoekstra H.E.;
RT "The genetic basis of phenotypic convergence in beach mice: similar pigment
RT patterns but different genes.";
RL Mol. Biol. Evol. 26:35-45(2008).
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 Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361244}.
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DR EMBL; FJ389421; ACK76634.1; -; Genomic_DNA.
DR AlphaFoldDB; B7TVL1; -.
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|RuleBase:RU000688};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361244};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
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 23..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 55..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 214..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT DOMAIN 34..268
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACK76634.1"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:ACK76634.1"
SQ SEQUENCE 268 AA; 29704 MW; 3218ACF1AACF2825 CRC64;
PHLGLATNQT GPWCLQVSVP DGLFLSLGLV SLVENVLVVI AITKNRNLHS PMYSFICCLA
LSDLMVSISL VLETAIILLL EAGALVTRAA LVQQLDNVID VLICGSMVSS LCFLGVIAID
RYISIFYALR YHSIVTLPRA RRAIVGIWVA SIFFSTLFIT YYNHTAVLIC LVTFFLAMLA
LMAILYVHML TRAYQHAQGI AQLQKRQGST RQGFCLKGAA TLTIILGIFF LCWGPFFLHL
TLIVLCPQHP TCSCIFKNFN LYLVLIIF
//