GenomeNet

Database: UniProt/SWISS-PROT
Entry: GPDM_MOUSE
LinkDB: GPDM_MOUSE
Original site: 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   20-JUN-2018, entry version 161.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPD-M;
DE            Short=GPDH-M;
DE            EC=1.1.5.3;
DE   AltName: Full=Protein TISP38;
DE   Flags: Precursor;
GN   Name=Gpd2; Synonyms=Gdm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Kozak L.P.;
RT   "Sequence and tissue-dependent RNA expression of mouse FAD-linked
RT   glycerol-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.,
RA   Katagiri H., 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
RT   from 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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;
RP   519-538; 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
RT   dehydrogenase (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
RP   BY 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,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- ENZYME REGULATION: Calcium-binding enhance the activity of the
CC       enzyme.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic 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}.
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   UniGene; Mm.3711; -.
DR   ProteinModelPortal; Q64521; -.
DR   SMR; Q64521; -.
DR   BioGrid; 199894; 1.
DR   IntAct; Q64521; 5.
DR   MINT; Q64521; -.
DR   STRING; 10090.ENSMUSP00000028167; -.
DR   iPTMnet; Q64521; -.
DR   PhosphoSitePlus; Q64521; -.
DR   SwissPalm; Q64521; -.
DR   REPRODUCTION-2DPAGE; Q64521; -.
DR   EPD; Q64521; -.
DR   MaxQB; Q64521; -.
DR   PaxDb; Q64521; -.
DR   PeptideAtlas; Q64521; -.
DR   PRIDE; Q64521; -.
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   eggNOG; KOG0042; Eukaryota.
DR   eggNOG; COG0578; LUCA.
DR   GeneTree; ENSGT00390000001718; -.
DR   HOVERGEN; HBG005897; -.
DR   InParanoid; Q64521; -.
DR   KO; K00111; -.
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   ChiTaRS; Gpd2; mouse.
DR   PRO; PR:Q64521; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000026827; -.
DR   CleanEx; MM_GPD2; -.
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; -; 3.
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; 2.
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; Complete proteome; Direct protein sequencing; FAD;
KW   Flavoprotein; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT       1     42       Mitochondrion. {ECO:0000250}.
FT   CHAIN        43    727       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000010430.
FT   DOMAIN      623    658       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      659    694       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND      71     99       FAD. {ECO:0000255}.
FT   CA_BIND     672    683       {ECO:0000255|PROSITE-ProRule:PRU00448}.
FT   MOD_RES     601    601       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18034455}.
FT   CONFLICT     26     26       P -> Q (in Ref. 1; AAB50545 and 4;
FT                                AAH21359). {ECO:0000305}.
FT   CONFLICT     42     42       Missing (in Ref. 3; BAC28685).
FT                                {ECO:0000305}.
FT   CONFLICT    158    158       L -> V (in Ref. 1; AAB50545).
FT                                {ECO:0000305}.
FT   CONFLICT    295    295       D -> E (in Ref. 2; BAA08926).
FT                                {ECO:0000305}.
FT   CONFLICT    449    449       D -> N (in Ref. 4; AAH21359).
FT                                {ECO:0000305}.
FT   CONFLICT    498    498       A -> P (in Ref. 2; BAA08926).
FT                                {ECO:0000305}.
FT   CONFLICT    582    582       N -> D (in Ref. 1; AAB50545).
FT                                {ECO:0000305}.
FT   CONFLICT    593    593       E -> G (in Ref. 1; AAB50545).
FT                                {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
//
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