GPDA_RAT
ID GPDA_RAT Reviewed; 349 AA.
AC O35077; Q5I0F4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 161.
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|RGD:621381};
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].
RC STRAIN=Wistar; TISSUE=White adipose tissue;
RX PubMed=9237667; DOI=10.1016/s0014-5793(97)00619-4;
RA Daikoku T., Shinohara Y., Shima A., Yamazaki N., Terada H.;
RT "Dramatic enhancement of the specific expression of the heart-type fatty
RT acid binding protein in rat brown adipose tissue by cold exposure.";
RL FEBS Lett. 410:383-386(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP PROTEIN SEQUENCE OF 6-48; 21-35; 70-101; 188-224 AND 241-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21695}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AB002558; BAA21763.1; -; mRNA.
DR EMBL; BC088396; AAH88396.1; -; mRNA.
DR RefSeq; NP_071551.2; NM_022215.2.
DR RefSeq; XP_006257438.1; XM_006257376.2.
DR AlphaFoldDB; O35077; -.
DR SMR; O35077; -.
DR BioGRID; 248887; 2.
DR STRING; 10116.ENSRNOP00000026200; -.
DR ChEMBL; CHEMBL3971; -.
DR iPTMnet; O35077; -.
DR PhosphoSitePlus; O35077; -.
DR jPOST; O35077; -.
DR PaxDb; O35077; -.
DR PRIDE; O35077; -.
DR Ensembl; ENSRNOT00000087662; ENSRNOP00000074647; ENSRNOG00000056457.
DR GeneID; 60666; -.
DR KEGG; rno:60666; -.
DR UCSC; RGD:621381; rat.
DR CTD; 2819; -.
DR RGD; 621381; Gpd1.
DR eggNOG; KOG2711; Eukaryota.
DR GeneTree; ENSGT00390000003114; -.
DR HOGENOM; CLU_033449_2_2_1; -.
DR InParanoid; O35077; -.
DR OMA; NRMFGNM; -.
DR OrthoDB; 476066at2759; -.
DR PhylomeDB; O35077; -.
DR TreeFam; TF300836; -.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR PRO; PR:O35077; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000056457; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; O35077; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:RGD.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IDA:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IDA:RGD.
DR GO; GO:0046486; P:glycerolipid metabolic process; IDA:RGD.
DR GO; GO:0006127; P:glycerophosphate shuttle; ISO:RGD.
DR GO; GO:0006734; P:NADH metabolic process; IDA:RGD.
DR GO; GO:0006116; P:NADH oxidation; IDA:RGD.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:RGD.
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_0000138082"
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:0000250|UniProtKB:P13707"
FT MOD_RES 326
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 179
FT /note="E -> D (in Ref. 1; BAA21763)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="F -> S (in Ref. 1; BAA21763)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="F -> I (in Ref. 1; BAA21763)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="C -> R (in Ref. 1; BAA21763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37453 MW; 26208A55DC033A9A CRC64;
MAGKKVCIVG SGNWGSAIAK IVGSNASQLA HFDPRVTMWV FEEDIGGRKL TEIINTQHEN
VKYLPGHKLP PNVVAVPDVV QAATGADILV FVVPHQFIGK ICDQLKGHLK ANTIGISLIK
GIDEGPNGLK LISEVIGESL GIPMSVLMGA NIASEVAEEK FCETTIGCKD PAQGQLLKEL
MQTPNFRITV VQEVDTVEIC GALKNIVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK
LFCSGSVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP
QTARELHSIL QHKGLVDKFP LFTAVYKVCY EGQPVGEFIC CLQNHPEHM
