MREG_DANRE
ID MREG_DANRE Reviewed; 234 AA.
AC Q6GQM0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Melanoregulin;
GN Name=mreg; ORFNames=si:ch211-51m24.2, zgc:91968;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably functions as cargo-recognition protein that couples
CC cytoplasmic vesicles to the transport machinery. Contributes to
CC retrograde melanosome transport from the cell periphery to the center.
CC Overexpression causes accumulation of late endosomes and/or lysosomes
CC at the microtubule organising center (MTOC) at the center of the cell.
CC Probably binds cholesterol and requires the presence of cholesterol in
CC membranes to function in microtubule-mediated retrograde organelle
CC transport. Binds phosphatidylinositol 3-phosphate, phosphatidylinositol
CC 4-phosphate, phosphatidylinositol 5-phosphate and phosphatidylinositol
CC 3,5-bisphosphate. {ECO:0000250|UniProtKB:Q6NVG5}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q6NVG5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6NVG5}. Melanosome membrane
CC {ECO:0000250|UniProtKB:Q6NVG5}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q6NVG5}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q6NVG5}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q6NVG5}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q6NVG5}.
CC -!- SIMILARITY: Belongs to the melanoregulin family. {ECO:0000305}.
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DR EMBL; BX004850; CAK04972.1; -; Genomic_DNA.
DR EMBL; BC072722; AAH72722.1; -; mRNA.
DR RefSeq; NP_001002167.1; NM_001002167.1.
DR RefSeq; XP_005159406.1; XM_005159349.2.
DR AlphaFoldDB; Q6GQM0; -.
DR SMR; Q6GQM0; -.
DR STRING; 7955.ENSDARP00000116628; -.
DR PaxDb; Q6GQM0; -.
DR PRIDE; Q6GQM0; -.
DR Ensembl; ENSDART00000017535; ENSDARP00000009192; ENSDARG00000011076.
DR Ensembl; ENSDART00000147056; ENSDARP00000116628; ENSDARG00000011076.
DR GeneID; 431714; -.
DR KEGG; dre:431714; -.
DR ZFIN; ZDB-GENE-040704-1; zgc:91968.
DR eggNOG; ENOG502S05X; Eukaryota.
DR GeneTree; ENSGT00940000165323; -.
DR HOGENOM; CLU_105265_0_0_1; -.
DR InParanoid; Q6GQM0; -.
DR OMA; ARNKTRM; -.
DR OrthoDB; 1250643at2759; -.
DR PhylomeDB; Q6GQM0; -.
DR TreeFam; TF334733; -.
DR PRO; PR:Q6GQM0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000011076; Expressed in pigment cell and 15 other tissues.
DR ExpressionAtlas; Q6GQM0; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0031300; C:intrinsic component of organelle membrane; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0032400; P:melanosome localization; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; IEA:InterPro.
DR GO; GO:0090382; P:phagosome maturation; ISS:UniProtKB.
DR InterPro; IPR031638; Melanoregulin.
DR PANTHER; PTHR34340; PTHR34340; 1.
DR Pfam; PF15812; MREG; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Lipid-binding; Lipoprotein; Lysosome;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1..234
FT /note="Melanoregulin"
FT /id="PRO_0000292177"
FT REGION 215..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 27149 MW; 9A0DAE3845731F17 CRC64;
MGTAFKKFCI KFCCCCCCED EDEEEKAPLI GHDTLDYFDR EAKKRRDQET NLWSEPGDPS
HSERDDDRVL YKLLQCRQQT QPGSRGYRRL SIDIEAMRDV RREVRDKWKM ILENLGFMAE
AESLLNVSAS ASYDRMRNAA SARSLLQTLH TETSLFNSKE PPPERYLFIL DRLIYLDAAE
DFVAKARRFY PPKDDDEEEE SNPLGINLPL LLSRMNQNIS GGEDEDEDES EPDD