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 04-NOV-2026, entry version 122. 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 = dihydroxyacetone CC phosphate + a quinol; 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}. 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; BC148085; AAI48086.1; -; mRNA. DR RefSeq; NP_001093766.1; NM_001100296.1. DR RefSeq; XP_005202471.1; XM_005202414.5. DR RefSeq; XP_024855441.1; XM_024999673.2. DR RefSeq; XP_059748128.1; XM_059892145.1. DR RefSeq; XP_059748134.1; XM_059892151.1. DR RefSeq; XP_059748137.1; XM_059892154.1. DR AlphaFoldDB; A6QLU1; -. DR SMR; A6QLU1; -. DR FunCoup; A6QLU1; 1750. DR STRING; 9913.ENSBTAP00000064800; -. DR PaxDb; 9913-ENSBTAP00000064800; -. DR Ensembl; ENSBTAT00000012886.6; ENSBTAP00000012886.5; ENSBTAG00000009770.7. DR Ensembl; ENSBTAT00085023910; ENSBTAP00085050874; ENSBTAG00085015062. DR Ensembl; ENSBTAT00090010887; ENSBTAP00090004963; ENSBTAG00090006151. 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 OrthoDB; 264015at2759; -. 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 conceptus and 109 other cell types or tissues. DR ExpressionAtlas; A6QLU1; baseline. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-ARBA. 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; ISS:UniProtKB. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006127; P:glycerol-3-phosphate shuttle; IBA:GO_Central. DR CDD; cd00051; EFh; 1. DR FunFam; 1.10.238.10:FF:000155; Glycerol-3-phosphate dehydrogenase; 1. DR FunFam; 1.10.8.870:FF:000001; Glycerol-3-phosphate dehydrogenase; 1. DR FunFam; 3.30.9.10:FF:000037; Glycerol-3-phosphate dehydrogenase; 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; 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 //