GPDM_MOUSE
ID GPDM_MOUSE Reviewed; 727 AA.
AC Q64521; Q3TK51; Q3UDY8; Q61507; Q8CBX6; Q8K4U5; Q8VDT0; Q9ERP0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
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 AltName: Full=Protein TISP38;
DE Flags: Precursor;
GN Name=Gpd2 {ECO:0000312|MGI:MGI:99778}; Synonyms=Gdm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipocyte;
RX PubMed=8951039; DOI=10.1006/abbi.1996.0536;
RA Koza R.A., Kozak U.C., Brown L.J., Leiter E.H., Macdonald M.J., Kozak L.P.;
RT "Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-
RT 3-phosphate dehydrogenase.";
RL Arch. Biochem. Biophys. 336:97-104(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=8772729; DOI=10.2337/diab.45.9.1238;
RA Ishihara H., Nakazaki M., Kanegae Y., Inukai K., Asano T., Katagiri H.,
RA Yazaki Y., Kikuchi M., Miyazaki J., Saito I., Oka Y.;
RT "Effect of mitochondrial and/or cytosolic glycerol 3-phosphate
RT dehydrogenase overexpression on glucose-stimulated insulin secretion from
RT MIN6 and HIT cells.";
RL Diabetes 45:1238-1244(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Diencephalon, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [5]
RP PROTEIN SEQUENCE OF 58-91; 95-110; 125-135; 167-178; 200-209; 212-254;
RP 285-298; 340-348; 381-390; 392-409; 442-453; 464-473; 483-499; 519-538;
RP 558-579; 598-606; 609-627 AND 635-693.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-686.
RC STRAIN=129/Sv; TISSUE=Liver;
RA Weitzel J.M.;
RT "Genomic sequence of mouse mitochondrial glycerol-3-phosphate dehydrogenase
RT (mGPDH).";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 611-727.
RC TISSUE=Testis;
RA Tamura K., Nishimune Y., Nojima H.;
RT "Mus musculus TISP38 mRNA.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 inner membrane.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; U60987; AAB50545.1; -; mRNA.
DR EMBL; D50430; BAA08926.1; -; mRNA.
DR EMBL; AK034353; BAC28685.1; -; mRNA.
DR EMBL; AK144716; BAE26028.1; -; mRNA.
DR EMBL; AK149851; BAE29123.1; -; mRNA.
DR EMBL; AK167152; BAE39294.1; -; mRNA.
DR EMBL; BC021359; AAH21359.1; -; mRNA.
DR EMBL; AH009802; AAG12342.1; -; Genomic_DNA.
DR EMBL; AB045714; BAB97201.1; -; mRNA.
DR CCDS; CCDS16045.1; -.
DR RefSeq; NP_001139292.1; NM_001145820.1.
DR RefSeq; NP_034404.3; NM_010274.3.
DR AlphaFoldDB; Q64521; -.
DR SMR; Q64521; -.
DR BioGRID; 199894; 21.
DR IntAct; Q64521; 2.
DR STRING; 10090.ENSMUSP00000108237; -.
DR iPTMnet; Q64521; -.
DR PhosphoSitePlus; Q64521; -.
DR SwissPalm; Q64521; -.
DR REPRODUCTION-2DPAGE; Q64521; -.
DR EPD; Q64521; -.
DR jPOST; Q64521; -.
DR MaxQB; Q64521; -.
DR PaxDb; Q64521; -.
DR PeptideAtlas; Q64521; -.
DR PRIDE; Q64521; -.
DR ProteomicsDB; 271263; -.
DR Antibodypedia; 2370; 282 antibodies from 30 providers.
DR DNASU; 14571; -.
DR Ensembl; ENSMUST00000028167; ENSMUSP00000028167; ENSMUSG00000026827.
DR Ensembl; ENSMUST00000169687; ENSMUSP00000130992; ENSMUSG00000026827.
DR GeneID; 14571; -.
DR KEGG; mmu:14571; -.
DR UCSC; uc008jsc.2; mouse.
DR CTD; 2820; -.
DR MGI; MGI:99778; Gpd2.
DR VEuPathDB; HostDB:ENSMUSG00000026827; -.
DR eggNOG; KOG0042; Eukaryota.
DR GeneTree; ENSGT00390000001718; -.
DR InParanoid; Q64521; -.
DR OMA; CIVNAAG; -.
DR OrthoDB; 669193at2759; -.
DR BRENDA; 1.1.5.3; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR UniPathway; UPA00618; UER00673.
DR BioGRID-ORCS; 14571; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gpd2; mouse.
DR PRO; PR:Q64521; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64521; protein.
DR Bgee; ENSMUSG00000026827; Expressed in seminiferous tubule of testis and 269 other tissues.
DR ExpressionAtlas; Q64521; baseline and differential.
DR Genevisible; Q64521; MM.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; TAS:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; ISO:MGI.
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; IGI:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IMP:MGI.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
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; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; 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_0000010430"
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:0007744|PubMed:18034455"
FT CONFLICT 26
FT /note="P -> Q (in Ref. 1; AAB50545 and 4; AAH21359)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="Missing (in Ref. 3; BAC28685)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="L -> V (in Ref. 1; AAB50545)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="D -> E (in Ref. 2; BAA08926)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="D -> N (in Ref. 4; AAH21359)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="A -> P (in Ref. 2; BAA08926)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="N -> D (in Ref. 1; AAB50545)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> G (in Ref. 1; AAB50545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 80954 MW; 319F52E31CFDFC44 CRC64;
MAFQKAVKGT ILVGGGALAT VLGLSPFAHY RRKQVSLAYV EAAGYLTEPV NREPPSREAQ
LMTLKNTPEF DILVIGGGAT GCGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
YLQKAIMNLD VEQYRMVKEA LHERANLLEI APHLSAPLPI MLPLYKWWQL PYYWVGIKMY
DLVAGSQCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
AATANYMEVV SLLKKTDPET GKERVSGARC KDVLTGQEFD VRAKCVINAS GPFTDSVRKM
DDKNVVPICQ PSAGVHIVMP GYYSPENMGL LDPATSDGRV IFFLPWEKMT IAGTTDTPTD
VTHHPIPSEE DINFILNEVR NYLSSDVEVR RGDVLAAWSG IRPLVTDPKS ADTQSISRNH
VVDISDSGLI TIAGGKWTTY RSMAEDTVDA AVKFHNLNAG PSRTVGLFLQ GGKDWSPTLY
IRLVQDYGLE SEVAQHLAKT YGDKAFEVAK MASVTGKRWP VVGVRLVSEF PYIEAEVKYG
IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWSELRKQE ELETATRFLY
YEMGYKSRTE QLTDSTEISL LPSDIDRYKK RFHKFDEDEK GFITIVDVQR VLESINVQMD
ENTLHEILCE VDLNKNGQVE LHEFLQLMSA VQKGRVSGSR LAILMKTAEE NLDRRVPIPV
DRSCGGL
