GPDM_RAT
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 03-AUG-2022, entry version 152.
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 = 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;
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_012736.1.
DR AlphaFoldDB; P35571; -.
DR SMR; P35571; -.
DR BioGRID; 247139; 2.
DR IntAct; P35571; 2.
DR MINT; P35571; -.
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 InParanoid; P35571; -.
DR OrthoDB; 669193at2759; -.
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; 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: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: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; IDA:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO: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; 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
