ID Q0P3X1_DANRE Unreviewed; 536 AA.
AC Q0P3X1;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN Name=gpd2 {ECO:0000313|EMBL:AAI22403.1,
GN ECO:0000313|RefSeq:NP_001038813.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-4869};
GN Synonyms=cb853 {ECO:0000313|RefSeq:NP_001038813.1}, wu:fe02f02
GN {ECO:0000313|RefSeq:NP_001038813.1}, zgc:153729
GN {ECO:0000313|RefSeq:NP_001038813.1};
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 {ECO:0000313|EMBL:AAI22403.1};
RN [1] {ECO:0000313|EMBL:AAI22403.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium {ECO:0000313|EMBL:AAI22403.1}, and PCR
RC rescue {ECO:0000313|EMBL:AAI65374.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_001038813.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21743250; DOI=10.1086/660162;
RA Robinson J.L., Hall J.R., Charman M., Ewart K.V., Driedzic W.R.;
RT "Molecular analysis, tissue profiles, and seasonal patterns of cytosolic
RT and mitochondrial GPDH in freeze-resistant rainbow smelt (Osmerus
RT mordax).";
RL Physiol. Biochem. Zool. 84:363-376(2011).
RN [3] {ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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 [4] {ECO:0000313|RefSeq:NP_001038813.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [5] {ECO:0000313|RefSeq:NP_001038813.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [6] {ECO:0000313|RefSeq:NP_001038813.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR EMBL; BC122402; AAI22403.1; -; mRNA.
DR EMBL; BC165374; AAI65374.1; -; mRNA.
DR RefSeq; NP_001038813.1; NM_001045348.1.
DR GeneID; 751628; -.
DR KEGG; dre:751628; -.
DR AGR; ZFIN:ZDB-GENE-030131-4869; -.
DR CTD; 2820; -.
DR ZFIN; ZDB-GENE-030131-4869; gpd2.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000000437; Chromosome 6.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 1: Evidence at protein level;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q0P3X1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 70..440
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 461..517
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 536 AA; 58951 MW; AA6955F8F7036873 CRC64;
MAFRKALKGT LIGGGAVATA VGLSQFFEYR KNQARLAYVE AQGELKVPFK DALPTREEQL
STLRNTEEFD VLVVGGGATG SGCALDAVTR NLKTALVERS DFSSGTSSRS TKLIHGGVRY
LQKAIMKLDY EQYMMVKEAL HERANLLEIA PHLSAPLPIM LPVYKWWQLP YYWAGIKMYD
LVAGSQCLKS SYVLSKSKAL EFFPMLKKDK LVGAIVYYDG QHNDARMNLA IALTAARHGA
AIANYTEVVH LLKKPDPKTG QEKVCGARCR DVVTGQEFDI RAKCVINATG PFTDSLRKMD
NQKTANICQP SAGVHIVIPG YYSPDNMGLL DPATSDGRVI FFLPWEKMTI AGTTDTPTEV
TAHPIPMEDD INFILSEVRN YLSPDVEVRR GDVLAAWSGI RPLVTDPSSK DTQSICRNHI
VNVSDSGLIT IAGGKWTTYR SMAEETLDAA IKAHNLSAGP SRTVGLTLEG GKDWTPTLYI
RLVQDYGLEN EVAQHLAATY GGRSFEVAKM AQVTGKRWPI VGKRLVSVVL IFQLVR
//
