GPDA_MOUSE
ID GPDA_MOUSE Reviewed; 349 AA.
AC P13707; Q3UVM3; Q5DTS5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic;
DE Short=GPD-C;
DE Short=GPDH-C;
DE EC=1.1.1.8 {ECO:0000250|UniProtKB:P21695};
GN Name=Gpd1 {ECO:0000312|MGI:MGI:95679}; Synonyms=Gdc-1, Gdc1, Kiaa4010;
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].
RX PubMed=3027100; DOI=10.1016/s0021-9258(19)75710-x;
RA Dobson D.E., Groves D.L., Spiegelman B.M.;
RT "Nucleotide sequence and hormonal regulation of mouse glycerophosphate
RT dehydrogenase mRNA during adipocyte and muscle cell differentiation.";
RL J. Biol. Chem. 262:1804-1809(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3755721; DOI=10.1016/s0021-9258(18)67311-9;
RA Ireland R.C., Kotarski M.A., Johnston L.A., Stadler U., Birkenmeier E.,
RA Kozak L.P.;
RT "Primary structure of the mouse glycerol-3-phosphate dehydrogenase gene.";
RL J. Biol. Chem. 261:11779-11785(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3015943; DOI=10.1016/s0021-9258(18)67461-7;
RA Phillips M., Djian P., Green H.;
RT "The nucleotide sequence of three genes participating in the adipose
RT differentiation of 3T3 cells.";
RL J. Biol. Chem. 261:10821-10827(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Lung, and Urinary bladder;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [7]
RP PROTEIN SEQUENCE OF 50-62; 111-130; 205-218; 230-240; 297-304 AND 319-340,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
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).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-289, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Has glycerol-3-phosphate dehydrogenase activity.
CC {ECO:0000250|UniProtKB:P21695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8;
CC Evidence={ECO:0000250|UniProtKB:P21695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC Evidence={ECO:0000250|UniProtKB:P21695};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21695}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90479.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J02655; AAA37728.1; -; mRNA.
DR EMBL; M25558; AAA37726.1; -; Genomic_DNA.
DR EMBL; M13366; AAA37727.1; -; Genomic_DNA.
DR EMBL; AK220445; BAD90479.1; ALT_INIT; mRNA.
DR EMBL; AK137134; BAE23246.1; -; mRNA.
DR EMBL; AK004565; BAB23376.1; -; mRNA.
DR EMBL; AK018733; BAB31376.1; -; mRNA.
DR EMBL; BC005756; AAH05756.1; -; mRNA.
DR EMBL; BC019391; AAH19391.1; -; mRNA.
DR CCDS; CCDS27828.1; -.
DR PIR; A25952; A25952.
DR RefSeq; NP_034401.1; NM_010271.2.
DR AlphaFoldDB; P13707; -.
DR SMR; P13707; -.
DR BioGRID; 199883; 2.
DR IntAct; P13707; 3.
DR MINT; P13707; -.
DR STRING; 10090.ENSMUSP00000023760; -.
DR ChEMBL; CHEMBL1075171; -.
DR iPTMnet; P13707; -.
DR PhosphoSitePlus; P13707; -.
DR SwissPalm; P13707; -.
DR REPRODUCTION-2DPAGE; IPI00230185; -.
DR REPRODUCTION-2DPAGE; P13707; -.
DR SWISS-2DPAGE; P13707; -.
DR CPTAC; non-CPTAC-3813; -.
DR jPOST; P13707; -.
DR MaxQB; P13707; -.
DR PaxDb; P13707; -.
DR PeptideAtlas; P13707; -.
DR PRIDE; P13707; -.
DR ProteomicsDB; 271037; -.
DR Antibodypedia; 26155; 345 antibodies from 33 providers.
DR DNASU; 14555; -.
DR Ensembl; ENSMUST00000023760; ENSMUSP00000023760; ENSMUSG00000023019.
DR GeneID; 14555; -.
DR KEGG; mmu:14555; -.
DR UCSC; uc007xqd.1; mouse.
DR CTD; 2819; -.
DR MGI; MGI:95679; Gpd1.
DR VEuPathDB; HostDB:ENSMUSG00000023019; -.
DR eggNOG; KOG2711; Eukaryota.
DR GeneTree; ENSGT00390000003114; -.
DR InParanoid; P13707; -.
DR OMA; NRMFGNM; -.
DR OrthoDB; 476066at2759; -.
DR PhylomeDB; P13707; -.
DR TreeFam; TF300836; -.
DR BRENDA; 1.1.1.8; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR SABIO-RK; P13707; -.
DR BioGRID-ORCS; 14555; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Gpd1; mouse.
DR PRO; PR:P13707; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P13707; protein.
DR Bgee; ENSMUSG00000023019; Expressed in brown adipose tissue and 211 other tissues.
DR ExpressionAtlas; P13707; baseline and differential.
DR Genevisible; P13707; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; TAS:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; ISO:MGI.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IDA:MGI.
DR GO; GO:0051287; F:NAD binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IMP:MGI.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IMP:MGI.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:MGI.
DR GO; GO:0006127; P:glycerophosphate shuttle; IMP:MGI.
DR GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
DR GO; GO:0006116; P:NADH oxidation; IMP:MGI.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:MGI.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..349
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT cytoplasmic"
FT /id="PRO_0000138080"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 269..270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT MOD_RES 289
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 326
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35077"
FT CONFLICT 218
FT /note="G -> R (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="T -> I (in Ref. 2; AAA37726/AAA37727 and 4;
FT BAD90479)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="K -> R (in Ref. 5; BAE23246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37573 MW; F2C572DADFEA1B99 CRC64;
MAGKKVCIVG SGNWGSAIAK IVGSNAGRLA HFDPRVTMWV FEEDIGGRKL TEIINTQHEN
VKYLPGHKLP PNVVAIPDVV QAATGADILV FVVPHQFIGK ICDQLKGHLK ANTIGISLIK
GVDEGPNGLK LISEVIGERL GIPMSVLMGA NIASEVAEEK FCETTIGCKD PAQGQLLKDL
MQTPNFRITV VQEVDTVEIC GALKNIVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK
LFCSGTVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP
QTARELHSIL QHKGLVDKFP LFTAVYKVCY EGQPVGEFIR CLQNHPEHM
