GPDA_DROME
ID GPDA_DROME Reviewed; 363 AA.
AC P13706; Q27590; Q27925; Q95077; Q95TV4; Q9VML0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic;
DE Short=GPD-C;
DE Short=GPDH-C;
DE EC=1.1.1.8;
GN Name=Gpdh1 {ECO:0000312|FlyBase:FBgn0001128};
GN Synonyms=Gpdh {ECO:0000303|PubMed:2500660};
GN ORFNames=CG9042 {ECO:0000312|FlyBase:FBgn0001128};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S;
RX PubMed=2500660; DOI=10.1073/pnas.86.13.5020;
RA von Kalm L., Weaver J., Demarco J., Macintyre R.J., Sullivan D.T.;
RT "Structural characterization of the alpha-glycerol-3-phosphate
RT dehydrogenase-encoding gene of Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5020-5024(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-133; 139-141 AND
RP 148-350, ALTERNATIVE SPLICING, AND DEFINITION OF ALLELES FAST AND SLOW.
RC STRAIN=Canton-S, Ogasawara, and Oregon-R;
RX PubMed=2511555; DOI=10.1093/nar/17.21.8553;
RA Bewley G.C., Cook J.L., Kusakabe S., Mukai T., Rigby D.L., Chambers G.K.;
RT "Sequence, structure and evolution of the gene coding for sn-glycerol-3-
RT phosphate dehydrogenase in Drosophila melanogaster.";
RL Nucleic Acids Res. 17:8553-8567(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS.
RC STRAIN=Tasmania;
RX PubMed=8094564; DOI=10.1098/rspb.1993.0006;
RA Reed D.S., Gibson J.B.;
RT "Defective P element insertions affect the expression of sn-glycerol-3-
RT phosphate dehydrogenase alleles in natural populations of Drosophila
RT melanogaster.";
RL Proc. R. Soc. B 251:39-45(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE GPDH-ACB62).
RC STRAIN=Cardwell;
RX PubMed=7633467; DOI=10.1016/0965-1748(95)00002-d;
RA Symonds J.E., Gibson J.B., Wilks A.V., Wilanowski T.M.;
RT "Molecular analysis of a Drosophila melanogaster sn-glycerol-3-phosphate
RT dehydrogenase allozyme variant that has cold labile activity.";
RL Insect Biochem. Mol. Biol. 25:789-798(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GPDH-2).
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-363 (ALLELES GPDH-MB5 AND
RP GPDH-ACYG22).
RC STRAIN=Cygnet, and Mission beach;
RX PubMed=7993372; DOI=10.1007/bf00554620;
RA Reed D.S., Gibson J.B.;
RT "Molecular heterogeneity of naturally occurring sn-glycerol-3-phosphate
RT dehydrogenase low-activity variants in Drosophila melanogaster.";
RL Biochem. Genet. 32:161-179(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-245.
RC STRAIN=Canton-S;
RX PubMed=3755720; DOI=10.1016/s0021-9258(18)67307-7;
RA Cook J.L., Shaffer J.B., Bewley G.C., MacIntyre R.J., Wright D.A.;
RT "Isolation of a genomic clone for Drosophila sn-glycerol-3-phosphate
RT dehydrogenase using synthetic oligonucleotides.";
RL J. Biol. Chem. 261:11751-11755(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-350, ALTERNATIVE SPLICING, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=2839508; DOI=10.1016/s0021-9258(18)38049-9;
RA Cook J.L., Bewley G.C., Shaffer J.B.;
RT "Drosophila sn-glycerol-3-phosphate dehydrogenase isozymes are generated by
RT alternate pathways of RNA processing resulting in different carboxyl-
RT terminal amino acid sequences.";
RL J. Biol. Chem. 263:10858-10864(1988).
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 -!- PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=GPDH-4;
CC IsoId=P13706-1; Sequence=Displayed;
CC Name=GPDH-1; Synonyms=GPDH-411, C;
CC IsoId=P13706-2; Sequence=VSP_001589;
CC Name=GPDH-2; Synonyms=GPDH-37, B;
CC IsoId=P13706-3; Sequence=VSP_001591;
CC Name=GPDH-3; Synonyms=GPDH-1A, A;
CC IsoId=P13706-4; Sequence=VSP_001590;
CC -!- TISSUE SPECIFICITY: Isoform GPDH-1 is predominant in thorax and isoform
CC GPDH-3 in abdomen.
CC -!- DEVELOPMENTAL STAGE: Isoform GPDH-2 and isoform GPDH-3 are expressed in
CC both larvae and adults. Isoform GPDH-1 is expressed only in adults.
CC {ECO:0000269|PubMed:2500660, ECO:0000269|PubMed:2839508}.
CC -!- POLYMORPHISM: There are two common alleles; fast and slow. The sequence
CC of fast is shown here.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; J04567; AAA28591.1; -; Genomic_DNA.
DR EMBL; J04567; AAA28592.1; -; Genomic_DNA.
DR EMBL; J04567; AAA28593.1; -; Genomic_DNA.
DR EMBL; X14179; CAA32379.1; -; Genomic_DNA.
DR EMBL; X14179; CAA32380.1; -; Genomic_DNA.
DR EMBL; X14179; CAA32381.1; -; Genomic_DNA.
DR EMBL; X67650; CAA47892.1; -; Genomic_DNA.
DR EMBL; X61223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X61224; CAA43536.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52304.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10562.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10563.1; -; Genomic_DNA.
DR EMBL; AY058492; AAL13721.1; -; mRNA.
DR EMBL; X80204; CAA56497.1; -; Genomic_DNA.
DR EMBL; M13786; AAA28590.1; -; Genomic_DNA.
DR EMBL; J03927; AAA28553.1; -; Genomic_DNA.
DR EMBL; J03927; AAA28554.1; -; Genomic_DNA.
DR EMBL; J03927; AAA28555.1; -; Genomic_DNA.
DR PIR; S06758; S06758.
DR PIR; S06759; S06759.
DR PIR; S06760; S06760.
DR PIR; S21963; S21963.
DR RefSeq; NP_001260111.1; NM_001273182.1. [P13706-4]
DR RefSeq; NP_001260112.1; NM_001273183.2. [P13706-3]
DR RefSeq; NP_001260113.1; NM_001273184.2. [P13706-2]
DR RefSeq; NP_476565.1; NM_057217.4. [P13706-3]
DR RefSeq; NP_476566.1; NM_057218.4. [P13706-2]
DR RefSeq; NP_476567.1; NM_057219.4. [P13706-4]
DR AlphaFoldDB; P13706; -.
DR SMR; P13706; -.
DR BioGRID; 59989; 73.
DR DIP; DIP-21689N; -.
DR IntAct; P13706; 1.
DR STRING; 7227.FBpp0305431; -.
DR PaxDb; P13706; -.
DR DNASU; 33824; -.
DR EnsemblMetazoa; FBtr0079146; FBpp0078777; FBgn0001128. [P13706-3]
DR EnsemblMetazoa; FBtr0079147; FBpp0078778; FBgn0001128. [P13706-2]
DR EnsemblMetazoa; FBtr0079148; FBpp0078779; FBgn0001128. [P13706-4]
DR EnsemblMetazoa; FBtr0333228; FBpp0305430; FBgn0001128. [P13706-4]
DR EnsemblMetazoa; FBtr0333229; FBpp0305431; FBgn0001128. [P13706-3]
DR EnsemblMetazoa; FBtr0333230; FBpp0305432; FBgn0001128. [P13706-2]
DR GeneID; 33824; -.
DR KEGG; dme:Dmel_CG9042; -.
DR CTD; 33824; -.
DR FlyBase; FBgn0001128; Gpdh1.
DR VEuPathDB; VectorBase:FBgn0001128; -.
DR eggNOG; KOG2711; Eukaryota.
DR GeneTree; ENSGT00390000003114; -.
DR InParanoid; P13706; -.
DR OMA; NRMFGNM; -.
DR PhylomeDB; P13706; -.
DR BRENDA; 1.1.1.8; 1994.
DR Reactome; R-DME-1483166; Synthesis of PA.
DR SignaLink; P13706; -.
DR UniPathway; UPA00086; -.
DR BioGRID-ORCS; 33824; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Gpdh; fly.
DR GenomeRNAi; 33824; -.
DR PRO; PR:P13706; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001128; Expressed in capitellum (Drosophila) and 24 other tissues.
DR ExpressionAtlas; P13706; baseline and differential.
DR Genevisible; P13706; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0031430; C:M band; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IDA:FlyBase.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006067; P:ethanol metabolic process; IMP:CACAO.
DR GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006734; P:NADH metabolic process; IDA:FlyBase.
DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central.
DR GO; GO:0055093; P:response to hyperoxia; IMP:FlyBase.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:FlyBase.
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 Alternative splicing; Cytoplasm; Direct protein sequencing; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..363
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT cytoplasmic"
FT /id="PRO_0000138075"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270..271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT VAR_SEQ 351..363
FT /note="Missing (in isoform GPDH-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001590"
FT VAR_SEQ 351..360
FT /note="Missing (in isoform GPDH-1)"
FT /evidence="ECO:0000305"
FT /id="VSP_001589"
FT VAR_SEQ 361..363
FT /note="Missing (in isoform GPDH-2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_001591"
FT VARIANT 14
FT /note="N -> Y (in allele GPDH-ACYG22)"
FT VARIANT 266
FT /note="C -> G (in allele GPDH-ACB62)"
FT VARIANT 273
FT /note="R -> C (in allele GPDH-ACYG22)"
FT VARIANT 337
FT /note="N -> K (in allele GPDH-AT198, allele GPDH-ACB62 and
FT allele GPDH-S)"
FT CONFLICT 351..363
FT /note="DTSIMPSPKLQNL -> GYVHHAVAKTCKICKSPKEAETFLTFLCTTENKCI
FT FSAQRQLDESLDSIF (in Ref. 3; CAA47892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39684 MW; 49FA09CE7FB6FDF4 CRC64;
MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE
NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI
KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR
DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF
VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG
PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM DTSIMPSPKL
QNL
