FXRD2_DANRE
ID FXRD2_DANRE Reviewed; 687 AA.
AC B0UXS1; Q08CE3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=FAD-dependent oxidoreductase domain-containing protein 2;
DE Flags: Precursor;
GN Name=foxred2; ORFNames=si:dkeyp-69e1.5, zgc:153216;
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].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable flavoprotein which may function in endoplasmic
CC reticulum associated degradation (ERAD). May bind non-native proteins
CC in the endoplasmic reticulum and target them to the ubiquitination
CC machinery for subsequent degradation (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FOXRED2 family. {ECO:0000305}.
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DR EMBL; CR383684; CAQ14966.1; -; Genomic_DNA.
DR EMBL; BC124275; AAI24276.1; -; mRNA.
DR RefSeq; NP_001070128.1; NM_001076660.1.
DR RefSeq; XP_005163970.1; XM_005163913.3.
DR RefSeq; XP_009297707.1; XM_009299432.2.
DR AlphaFoldDB; B0UXS1; -.
DR STRING; 7955.ENSDARP00000104384; -.
DR PaxDb; B0UXS1; -.
DR PeptideAtlas; B0UXS1; -.
DR Ensembl; ENSDART00000135389; ENSDARP00000119181; ENSDARG00000061354.
DR Ensembl; ENSDART00000182411; ENSDARP00000150274; ENSDARG00000061354.
DR GeneID; 767722; -.
DR KEGG; dre:767722; -.
DR CTD; 80020; -.
DR ZFIN; ZDB-GENE-060929-1026; foxred2.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00640000091519; -.
DR HOGENOM; CLU_014290_1_0_1; -.
DR InParanoid; B0UXS1; -.
DR OMA; FIHMVSR; -.
DR OrthoDB; 461621at2759; -.
DR PhylomeDB; B0UXS1; -.
DR TreeFam; TF324712; -.
DR PRO; PR:B0UXS1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000061354; Expressed in liver and 21 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..687
FT /note="FAD-dependent oxidoreductase domain-containing
FT protein 2"
FT /id="PRO_0000337694"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 15..17
FT /note="DLL -> VLF (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="D -> N (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="RK -> QE (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="R -> K (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="L -> R (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="I -> T (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="I -> L (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="A -> T (in Ref. 2; AAI24276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 78132 MW; 641ECDEF6400795B CRC64;
MSVIQLVFRL LCVLDLLLAV SASGLHGRNR TLSHEYCVLG AGPAGLQMGY FLSRSQRDYI
ILERNAGPGS FFNIYPRHRK LISINKIYTG RRNKEFNLRH DWNSLLSDRP DLLFQRISRK
LYPSADDFPH YLSLFEKELG LKVKYGTDVG RIKASDFNGH QGYVLTDQNG VNYQCRVLLV
STGLWVPQEV DFRGSDLVEG YESIPTDPEE FKDQAVLILG KGNSAFETAQ SILGRASRIH
LYSPSPVRLA WQTHYVGDLR AVNNELLDTY QLKSLDGLVE GRLEDIAIVR RAKDRGKRRA
AKKRNSTSTK RNEPLYLTLT ELLDDQNDTN ISNVTGQNLP GYHTDNFSLR QPYDRVIRCL
GFRFNFSIFD GSARPPQSSG ARGRLPGVTA WYEGRGTPNM FVLGIAAHSR DYRMSAGGFI
HGFRYTVRAV HKILEQRYHN IAWPTTNIPI SQLQSWILRR VNEASGTYQM FGVLGDIILL
QGSHCEYLEE FPLQALPQLS ALSGRSISDH GLLVLVMQYG LNHTDTLGPG RAESEWTKAW
KSNFLHPVLY YYKTLPTDKD MRQRPVGWPL PRPEAVHHMV EDFLTEWDQP ISHSQPLRRF
LEHCLKTDLR AFYAESCFLL SLTSRNPPLF CRQGYLRKQG IMGNRHLWQH AREAGLMEDA
ALSEDASVPE YLNHAGAAVI STVNFDL
