ID M3ZLE0_XIPMA Unreviewed; 319 AA.
AC M3ZLE0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 58.
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};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000003032.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000003032.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000003032.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; M3ZLE0; -.
DR STRING; 8083.ENSXMAP00000003032; -.
DR Ensembl; ENSXMAT00000003037.2; ENSXMAP00000003032.2; ENSXMAG00000003026.2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; M3ZLE0; -.
DR OMA; VTFFCTT; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
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 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 74..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 188..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 238..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361244"
FT DOMAIN 56..296
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 319 AA; 36236 MW; EDBD57FC6D7BD98E CRC64;
MDCSLRYLHV EFNPLTEIMD ENETNSTLGE RNLSSCVQIR IPQELFLALG IVSLVENILV
ILAIIRNRNL HSPMYYFICC LAVSDMLVSV SNVVETIFML LNDHGLLDVH PGMLRHLDNV
IDVMICSSVV SSLSFLCTIA ADRYITIFYA LRYHSIMTTQ RAVSIIAVVW LASVASSILF
IVYHTDNAVI VCLVTFFCIT LVFNAALYLH MFVLAHVHSR RITAFHKGRR QSTSMKGAIT
LTILLGVFIL CWGPFFLHLI LILACPTSPF CNCFFRNFNL FLILIICNSL IDPLIYAYRS
QELRKTLQEL VLCSWCFGM
//
