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   03-AUG-2022, entry version 103.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPD-M;
DE            Short=GPDH-M;
DE            EC=1.1.5.3 {ECO:0000250|UniProtKB:P43304};
DE   Flags: Precursor;
GN   Name=GPD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   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   -!- 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:0000250|UniProtKB:P43304}.
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:0000250|UniProtKB:P43304};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18978;
CC         Evidence={ECO:0000250|UniProtKB:P43304};
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|UniProtKB:P43304}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       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}.
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DR   EMBL; BC148085; AAI48086.1; -; mRNA.
DR   RefSeq; NP_001093766.1; NM_001100296.1.
DR   RefSeq; XP_005202471.1; XM_005202414.3.
DR   AlphaFoldDB; A6QLU1; -.
DR   SMR; A6QLU1; -.
DR   STRING; 9913.ENSBTAP00000012886; -.
DR   PaxDb; A6QLU1; -.
DR   PRIDE; A6QLU1; -.
DR   Ensembl; ENSBTAT00000012886; ENSBTAP00000012886; ENSBTAG00000009770.
DR   Ensembl; ENSBTAT00000067743; ENSBTAP00000064800; ENSBTAG00000009770.
DR   GeneID; 504948; -.
DR   KEGG; bta:504948; -.
DR   CTD; 2820; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009770; -.
DR   VGNC; VGNC:29531; GPD2.
DR   eggNOG; KOG0042; Eukaryota.
DR   GeneTree; ENSGT00390000001718; -.
DR   HOGENOM; CLU_015740_3_1_1; -.
DR   InParanoid; A6QLU1; -.
DR   OMA; CIVNAAG; -.
DR   OrthoDB; 669193at2759; -.
DR   TreeFam; TF300359; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000009770; Expressed in conceptus and 109 other tissues.
DR   ExpressionAtlas; A6QLU1; baseline and differential.
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: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:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Calcium; FAD; Flavoprotein; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           43..727
FT                   /note="Glycerol-3-phosphate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000355966"
FT   DOMAIN          623..658
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          659..694
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         71..99
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         672
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         674
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         676
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         678
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         683
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         601
FT                   /note="Phosphotyrosine"
FT                   /evidence="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