ID F1Q555_DANRE Unreviewed; 726 AA.
AC F1Q555; A0A8M2BD42;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00020025};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN Name=gpd2 {ECO:0000313|Ensembl:ENSDARP00000119186,
GN ECO:0000313|RefSeq:XP_005165900.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-4869};
GN Synonyms=cb853 {ECO:0000313|RefSeq:XP_005165900.1}, im:7147983
GN {ECO:0000313|RefSeq:XP_005165900.1}, wu:fe02f02
GN {ECO:0000313|RefSeq:XP_005165900.1}, zgc:153729
GN {ECO:0000313|RefSeq:XP_005165900.1};
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|Ensembl:ENSDARP00000119186};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000119186}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000119186};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000119186, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000119186};
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 [3] {ECO:0000313|RefSeq:XP_005165900.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005165900.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Calcium-responsive mitochondrial glycerol-3-phosphate
CC dehydrogenase which seems to be a key component of the pancreatic beta-
CC cell glucose-sensing device. {ECO:0000256|ARBA:ARBA00003074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18978;
CC Evidence={ECO:0000256|ARBA:ARBA00001590};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation.
CC {ECO:0000256|ARBA:ARBA00004745}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR376780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005165900.1; XM_005165843.4.
DR STRING; 7955.ENSDARP00000119186; -.
DR PaxDb; 7955-ENSDARP00000108297; -.
DR Ensembl; ENSDART00000144028; ENSDARP00000119186; ENSDARG00000062430.
DR Ensembl; ENSDART00000144028.2; ENSDARP00000119186.1; ENSDARG00000062430.7.
DR GeneID; 751628; -.
DR AGR; ZFIN:ZDB-GENE-030131-4869; -.
DR CTD; 2820; -.
DR ZFIN; ZDB-GENE-030131-4869; gpd2.
DR eggNOG; KOG0042; Eukaryota.
DR HOGENOM; CLU_015740_3_1_1; -.
DR OMA; PHIVKPM; -.
DR OrthoDB; 989271at2759; -.
DR Reactome; R-DRE-1483166; Synthesis of PA.
DR Reactome; R-DRE-163560; Triglyceride catabolism.
DR Proteomes; UP000000437; Chromosome 6.
DR Bgee; ENSDARG00000062430; Expressed in zone of skin and 34 other cell types or tissues.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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 Pfam; PF13499; EF-hand_7; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1Q555};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 622..657
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 658..693
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 726 AA; 80595 MW; FA62F3BEA4DD0372 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 VGKRLVSEFP YIESEVQYAI
KEYACTAIDV ISRRTRLGFL NVQAADEALP RIVEIMGKEL QWTEQKKKEE LEAAKNFLYL
EMGYKARSEQ LSKTTEISLT PQEVARYKKR FYKFDKESKG FITTVDVQQV LERLSIHIDE
NALHEILNEV DLNKNGQVEL DEFLQLMSAV QRGQISDSRL AILLKTAEEG LDLRGPVSVD
RSGGGV
//
