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Database: UniProt
Entry: P35571
LinkDB: P35571
Original site: P35571 
ID   GPDM_RAT                Reviewed;         727 AA.
AC   P35571;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-FEB-2019, entry version 140.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPD-M;
DE            Short=GPDH-M;
DE            EC=1.1.5.3;
DE   Flags: Precursor;
GN   Name=Gpd2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 43-58.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=8182039;
RA   Brown L.J., McDonald M.J., Lehn D.A., Moran S.M.;
RT   "Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase
RT   cDNA. Evidence for EF-hand calcium-binding domains.";
RL   J. Biol. Chem. 269:14363-14366(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=7937996; DOI=10.1073/pnas.91.22.10581;
RA   Mueller S., Seitz H.J.;
RT   "Cloning of a cDNA for the FAD-linked glycerol-3-phosphate
RT   dehydrogenase from rat liver and its regulation by thyroid hormones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10581-10585(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:132124; EC=1.1.5.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- ACTIVITY REGULATION: Calcium-binding enhance the activity of the
CC       enzyme.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; U08027; AAB60443.1; -; mRNA.
DR   EMBL; X78593; CAA55329.1; -; mRNA.
DR   EMBL; BC083565; AAH83565.1; -; mRNA.
DR   PIR; A54051; A54051.
DR   RefSeq; NP_036868.1; NM_012736.1.
DR   UniGene; Rn.89705; -.
DR   ProteinModelPortal; P35571; -.
DR   SMR; P35571; -.
DR   BioGrid; 247139; 2.
DR   STRING; 10116.ENSRNOP00000043749; -.
DR   iPTMnet; P35571; -.
DR   PhosphoSitePlus; P35571; -.
DR   World-2DPAGE; 0004:P35571; -.
DR   jPOST; P35571; -.
DR   PaxDb; P35571; -.
DR   PRIDE; P35571; -.
DR   GeneID; 25062; -.
DR   KEGG; rno:25062; -.
DR   UCSC; RGD:2726; rat.
DR   CTD; 2820; -.
DR   RGD; 2726; Gpd2.
DR   eggNOG; KOG0042; Eukaryota.
DR   eggNOG; COG0578; LUCA.
DR   HOGENOM; HOG000004813; -.
DR   HOVERGEN; HBG005897; -.
DR   InParanoid; P35571; -.
DR   KO; K00111; -.
DR   OrthoDB; 669193at2759; -.
DR   PhylomeDB; P35571; -.
DR   BRENDA; 1.1.5.3; 5301.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:P35571; -.
DR   Proteomes; UP000002494; Unplaced.
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; IBA:GO_Central.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IDA:RGD.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IDA:RGD.
DR   GO; GO:0006734; P:NADH metabolic process; IDA:RGD.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; PTHR11985; 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; SSF47473; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Direct protein sequencing; FAD;
KW   Flavoprotein; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT       1     42       Mitochondrion.
FT                                {ECO:0000269|PubMed:8182039}.
FT   CHAIN        43    727       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000010431.
FT   DOMAIN      623    658       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      659    694       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND      71     99       FAD. {ECO:0000255}.
FT   CA_BIND     672    683       {ECO:0000255|PROSITE-ProRule:PRU00448}.
FT   MOD_RES     601    601       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q64521}.
SQ   SEQUENCE   727 AA;  80973 MW;  B2AAA45E93F5F7CB CRC64;
     MAFQKVVKGT ILMGGGALAT VLGLSQFAHY RRKQVSLAYV EAATCFSEPV NREPPSREAQ
     LMTLQNTSEF DILVIGGGAT GCGCALDAVT RGLKTALVER NDFASGTSSR STKLIHGGVR
     YLQKAITNLD VEQYRMVKEA LHERANLLEI APHLSAPLPI MLPLYKWWQL PYYWVGIKMY
     DLVAGSHCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
     AATANYMEVV SLLKKTDPET GKERVSGARC KDVLTGHEFN VRAKCVINAT GPFTDSVRKM
     DDNDVVPICQ PSAGVHIVMP GYYSPENMGL LDPATSDGRV IFFLPWEKMT IAGTTDSPTD
     VTHHPIPSED DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVTDPKS ANTQSISRNH
     VVEVSDSGLI TIAGGKWTTY RSMAEDTVNK AVKLHNLNAG PSRTVGLFLQ GGKDWSPTLY
     IRLVQDYGLE SEVAQHLAKT YGDKAFDVAK MASVTGKRWP VVGVRLVSEF PYIEAEVKYG
     IKEYACTAVD MISRRTRLAF LNVQAAEEAL PKIVELMGRE LNWSELRKQE ELETATRFLY
     YEMGYKSRTE QLTDSTEISL LPPDIDRYKK RFHMFDEDEK GFITIVDVQR VLESINVQMD
     EDTLHEILCE VDLNKNGQVE LHEFLQLMSA VHTGRVSGSR LAILMKTAEE NLDRRVPIPV
     DRSCGGL
//
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