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Database: UniProt/SWISS-PROT
Entry: GPDM_BOVIN
LinkDB: GPDM_BOVIN
Original site: GPDM_BOVIN 
ID   GPDM_BOVIN              Reviewed;         727 AA.
AC   A6QLU1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   12-SEP-2018, entry version 85.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Calcium-binding enhance the activity of the
CC       enzyme. {ECO:0000250}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (aerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; BC148085; AAI48086.1; -; mRNA.
DR   RefSeq; NP_001093766.1; NM_001100296.1.
DR   RefSeq; XP_005202471.1; XM_005202414.3.
DR   UniGene; Bt.48365; -.
DR   ProteinModelPortal; A6QLU1; -.
DR   SMR; A6QLU1; -.
DR   STRING; 9913.ENSBTAP00000012886; -.
DR   PaxDb; A6QLU1; -.
DR   PRIDE; A6QLU1; -.
DR   Ensembl; ENSBTAT00000012886; ENSBTAP00000012886; ENSBTAG00000009770.
DR   GeneID; 504948; -.
DR   KEGG; bta:504948; -.
DR   CTD; 2820; -.
DR   VGNC; VGNC:29531; GPD2.
DR   eggNOG; KOG0042; Eukaryota.
DR   eggNOG; COG0578; LUCA.
DR   GeneTree; ENSGT00390000001718; -.
DR   HOGENOM; HOG000004813; -.
DR   HOVERGEN; HBG005897; -.
DR   InParanoid; A6QLU1; -.
DR   KO; K00111; -.
DR   OMA; VPYYWVG; -.
DR   OrthoDB; EOG091G03ER; -.
DR   TreeFam; TF300359; -.
DR   Reactome; R-BTA-1483166; Synthesis of PA.
DR   Reactome; R-BTA-163560; Triglyceride catabolism.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000009770; Expressed in 10 organ(s), highest expression level in testis.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 3.
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; 2.
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   2: Evidence at transcript level;
KW   Calcium; Complete proteome; FAD; Flavoprotein; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Repeat; Transit peptide.
FT   TRANSIT       1     42       Mitochondrion. {ECO:0000250}.
FT   CHAIN        43    727       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000355966.
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;  80763 MW;  1F02904CEEA3CC71 CRC64;
     MAFQKAVKGT ILVGGGALAT VLGLSHFAHY KRKQVNLAFV EAADCISEPV NREPPSREAQ
     ILTLKNTSEF DVLVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
     YLQKAIMKLD IEQYRMVKEA LHERANLLEI APHLSAPLPI MLPIYKWWQL PYYWVGIKLY
     DLVAGSNCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
     AATANYMEVM SLLKKTDPQT GKERVSGARC KDVLTGEEFD VRAKCVINAT GPFTDTVRKM
     DDKDTTAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWQKMT IAGTTDTPTD
     VTHHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVTDPKS ADTKSISRNH
     VVDISESGLI TIAGGKWTTY RSMAEDTINA AVKAHNLKAG PSRTVGLFLQ GGKDWSPTLY
     IRLVQDYGLE SEVAQHLAAT YGDKAFEVAK MASVTGKRWP IVGVRLVSEF PYIEAEVKYG
     IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWDDSKKEE ELETARKFLY
     YEMGYKSRSE QLTDRSEISL LPSDIDRYKK RFHKFDADQK GFITIVDVQR VLESIGVQMD
     ENTLHEILNE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV
     DRSCGGL
//
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