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   10-JUN-2026, entry version 168.
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 {ECO:0000312|RGD:2726};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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; DOI=10.1016/s0021-9258(17)36629-2;
RA   Brown L.J., McDonald M.J., Lehn D.A., Moran S.M.;
RT   "Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA.
RT   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 dehydrogenase
RT   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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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;
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 (anaerobic
CC       route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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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_012736.2.
DR   RefSeq; XP_038960257.1; XM_039104329.2.
DR   RefSeq; XP_038960258.1; XM_039104330.2.
DR   RefSeq; XP_038960259.1; XM_039104331.2.
DR   RefSeq; XP_063139207.1; XM_063283137.1.
DR   AlphaFoldDB; P35571; -.
DR   SMR; P35571; -.
DR   BioGRID; 247139; 2.
DR   FunCoup; P35571; 2113.
DR   IntAct; P35571; 2.
DR   MINT; P35571; -.
DR   STRING; 10116.ENSRNOP00000043749; -.
DR   iPTMnet; P35571; -.
DR   PhosphoSitePlus; P35571; -.
DR   SwissPalm; P35571; -.
DR   jPOST; P35571; -.
DR   PaxDb; 10116-ENSRNOP00000043749; -.
DR   Ensembl; ENSRNOT00000090323.3; ENSRNOP00000071643.3; ENSRNOG00000033824.6.
DR   GeneID; 25062; -.
DR   KEGG; rno:25062; -.
DR   UCSC; RGD:2726; rat.
DR   AGR; RGD:2726; -.
DR   CTD; 2820; -.
DR   RGD; 2726; Gpd2.
DR   eggNOG; KOG0042; Eukaryota.
DR   GeneTree; ENSGT00390000001718; -.
DR   InParanoid; P35571; -.
DR   PhylomeDB; P35571; -.
DR   BRENDA; 1.1.5.3; 5301.
DR   Reactome; R-RNO-1483166; Synthesis of PA.
DR   Reactome; R-RNO-163560; Triglyceride catabolism.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:P35571; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   ExpressionAtlas; P35571; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
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:0043010; P:camera-type eye development; ISO:RGD.
DR   GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; ISO:RGD.
DR   GO; GO:0006127; P:glycerol-3-phosphate shuttle; ISO:RGD.
DR   GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR   CDD; cd00051; EFh; 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   FunFam; 1.10.238.10:FF:000539; Glycerol-3-phosphate dehydrogenase, mitochondrial; 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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; FAD; Flavoprotein; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW   Transit peptide.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:8182039"
FT   CHAIN           43..727
FT                   /note="Glycerol-3-phosphate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000010431"
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;  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
//