Reviewed, UniProtKB/Swiss-Prot P13706 (GPDA_DROME)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
      Short name=GPDH-C
      Short name=GPD-C
    EC=1.1.1.8

Gene names

Name:	Gpdh
ORF Names:	CG9042

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.
Pathway	Phospholipid metabolism; alpha-glycerophosphate cycle.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Isoform GPDH-1 is predominant in thorax and isoform GPDH-3 in abdomen.
Developmental stage	Isoform GPDH-2 and isoform GPDH-3 are expressed in both larvae and adults. Isoform GPDH-1 is expressed only in adults. Ref.1 Ref.10
Polymorphism	There are two common alleles; fast and slow. The sequence of fast is shown here.
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	flight behavior Inferred from mutant phenotype. Source: FlyBase glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW triglyceride metabolic process Inferred from mutant phenotype. Source: FlyBase
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform GPDH-4 (identifier: P13706-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform GPDH-1 (identifier: P13706-2)

Also known as: GPDH-411; C;

The sequence of this isoform differs from the canonical sequence as follows:
     351-360: Missing.

Isoform GPDH-2 (identifier: P13706-3)

Also known as: GPDH-37; B;

The sequence of this isoform differs from the canonical sequence as follows:
     361-363: Missing.

Isoform GPDH-3 (identifier: P13706-4)

Also known as: GPDH-1A; A;

The sequence of this isoform differs from the canonical sequence as follows:
     351-363: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic		PRO_0000138075
Regions
	Nucleotide binding	11 – 16	6	NAD By similarity
	Region	270 – 271	2	Substrate binding By similarity
Sites
	Active site	206	1	Proton acceptor By similarity
	Binding site	98	1	NAD By similarity
	Binding site	121	1	NAD; via amide nitrogen By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	155	1	NAD; via amide nitrogen By similarity
	Binding site	270	1	NAD By similarity
	Binding site	299	1	NAD By similarity
Natural variations
	Alternative sequence	351 – 363	13	Missing in isoform GPDH-3.		VSP_001590
	Alternative sequence	351 – 360	10	Missing in isoform GPDH-1.		VSP_001589
	Alternative sequence	361 – 363	3	Missing in isoform GPDH-2.		VSP_001591
	Natural variant	14	1	N → Y in allele GPDH-ACYG22.
	Natural variant	266	1	C → G in allele GPDH-ACB62.
	Natural variant	273	1	R → C in allele GPDH-ACYG22.
	Natural variant	337	1	N → K in allele GPDH-AT198, allele GPDH-ACB62 and allele GPDH-S.
Experimental info
	Sequence conflict	351 – 363	13	DTSIM…KLQNL → GYVHHAVAKTCKICKSPKEA ETFLTFLCTTENKCIFSAQR QLDESLDSIF in CAA47892. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform GPDH-4 [UniParc]. Last modified June 1, 2001. Version 3. Checksum: 49FA09CE7FB6FDF4	FASTA	363	39,684
	10 20 30 40 50 60 MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE 70 80 90 100 110 120 NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI 130 140 150 160 170 180 KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR 190 200 210 220 230 240 DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF 250 260 270 280 290 300 VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG 310 320 330 340 350 360 PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM DTSIMPSPKL QNL
	Isoform GPDH-1 (GPDH-411) (C). Checksum: 629616247F906ACF	FASTA	353	38,614
	10 20 30 40 50 60 MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE 70 80 90 100 110 120 NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI 130 140 150 160 170 180 KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR 190 200 210 220 230 240 DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF 250 260 270 280 290 300 VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG 310 320 330 340 350 PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM QNL
	Isoform GPDH-2 (GPDH-37) (B). Checksum: 7E7FB6FDF432CDD0	FASTA	360	39,329
	10 20 30 40 50 60 MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE 70 80 90 100 110 120 NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI 130 140 150 160 170 180 KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR 190 200 210 220 230 240 DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF 250 260 270 280 290 300 VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG 310 320 330 340 350 360 PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM DTSIMPSPKL
	Isoform GPDH-3 (GPDH-1A) (A). Checksum: B47F906ACF061F8E	FASTA	350	38,259
	10 20 30 40 50 60 MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE 70 80 90 100 110 120 NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI 130 140 150 160 170 180 KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR 190 200 210 220 230 240 DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF 250 260 270 280 290 300 VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG 310 320 330 340 350 PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural characterization of the alpha-glycerol-3-phosphate dehydrogenase-encoding gene of Drosophila melanogaster." von Kalm L., Weaver J., Demarco J., Macintyre R.J., Sullivan D.T. Proc. Natl. Acad. Sci. U.S.A. 86:5020-5024(1989) [PubMed: 2500660] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE. Strain: Canton-S.
[2]	"Sequence, structure and evolution of the gene coding for sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster." Bewley G.C., Cook J.L., Kusakabe S., Mukai T., Rigby D.L., Chambers G.K. Nucleic Acids Res. 17:8553-8567(1989) [PubMed: 2511555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-133; 139-141 AND 148-350, ALTERNATIVE SPLICING, DEFINITION OF ALLELES FAST AND SLOW. Strain: Canton-S, Ogasawara and Oregon-R.
[3]	"Defective P element insertions affect the expression of sn-glycerol-3-phosphate dehydrogenase alleles in natural populations of Drosophila melanogaster." Reed D.S., Gibson J.B. Proc. R. Soc. B 251:39-45(1993) [PubMed: 8094564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS. Strain: Tasmania.
[4]	"Molecular analysis of a Drosophila melanogaster sn-glycerol-3-phosphate dehydrogenase allozyme variant that has cold labile activity." Symonds J.E., Gibson J.B., Wilks A.V., Wilanowski T.M. Insect Biochem. Mol. Biol. 25:789-798(1995) [PubMed: 7633467] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALLELE GPDH-ACB62. Strain: Cardwell.
[5]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[6]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[7]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GPDH-2). Strain: Berkeley. Tissue: Ovary.
[8]	"Molecular heterogeneity of naturally occurring sn-glycerol-3-phosphate dehydrogenase low-activity variants in Drosophila melanogaster." Reed D.S., Gibson J.B. Biochem. Genet. 32:161-179(1994) [PubMed: 7993372] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-363, VARIANTS ALLELES GPDH-MB5 AND GPDH-ACYG22. Strain: Cygnet and Mission beach.
[9]	"Isolation of a genomic clone for Drosophila sn-glycerol-3-phosphate dehydrogenase using synthetic oligonucleotides." Cook J.L., Shaffer J.B., Bewley G.C., MacIntyre R.J., Wright D.A. J. Biol. Chem. 261:11751-11755(1986) [PubMed: 3755720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-245. Strain: Canton-S.
[10]	"Drosophila sn-glycerol-3-phosphate dehydrogenase isozymes are generated by alternate pathways of RNA processing resulting in different carboxyl-terminal amino acid sequences." Cook J.L., Bewley G.C., Shaffer J.B. J. Biol. Chem. 263:10858-10864(1988) [PubMed: 2839508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-350, ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE. Strain: Canton-S.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04567 Genomic DNA. Translation: AAA28591.1. J04567 Genomic DNA. Translation: AAA28592.1. J04567 Genomic DNA. Translation: AAA28593.1. X14179 Genomic DNA. Translation: CAA32379.1. X14179 Genomic DNA. Translation: CAA32380.1. X14179 Genomic DNA. Translation: CAA32381.1. X67650 Genomic DNA. Translation: CAA47892.1. X61223 Genomic DNA. No translation available. X61224 Genomic DNA. Translation: CAA43536.1. AE014134 Genomic DNA. Translation: AAF52304.1. AE014134 Genomic DNA. Translation: AAN10562.1. AE014134 Genomic DNA. Translation: AAN10563.1. AY058492 mRNA. Translation: AAL13721.1. X80204 Genomic DNA. Translation: CAA56497.1. M13786 Genomic DNA. Translation: AAA28590.1. J03927 Genomic DNA. Translation: AAA28553.1. J03927 Genomic DNA. Translation: AAA28554.1. J03927 Genomic DNA. Translation: AAA28555.1.
PIR	S06758. S06759. S06760. S21963.
RefSeq	NP_476565.1. NP_476566.1. NP_476567.1.
UniGene	Dm.4843
3D structure databases
SMR	P13706. Positions 1-350.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-21689N.
IntAct	P13706. 7 interactions.
STRING	P13706.
Genome annotation databases
Ensembl	FBtr0079146; FBpp0078777; FBgn0001128; Drosophila melanogaster. [Genome view] FBtr0079147; FBpp0078778; FBgn0001128; Drosophila melanogaster. [Genome view] FBtr0079148; FBpp0078779; FBgn0001128; Drosophila melanogaster. [Genome view]
GeneID	33824.
KEGG	dme:Dmel_CG9042.
Organism-specific databases
CTD	33824.
FlyBase	FBgn0001128. Gpdh.
Phylogenomic databases
eggNOG	inNOG07819.
InParanoid	P13706.
OMA	THENVKY.
PhylomeDB	P13706.
Enzyme and pathway databases
BRENDA	1.1.1.8. 48.
Gene expression databases
Bgee	P13706.
GermOnline	CG9042. Drosophila melanogaster.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. IPR006168. NAD-dep_Gly3P_DH. IPR017751. NAD-dep_Gly3P_DH_euk. IPR011128. NAD-dep_Gly3P_DH_N. IPR006109. NAD_Gly3P_DH_C. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR11728. NAD_Gly3P_DH. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
TIGRFAMs	TIGR03376. glycerol3P_DH. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	785441.

Entry information

Entry name

GPDA_DROME

Accession

Primary (citable) accession number: P13706
Secondary accession number(s): Q27590 , Q27925, Q95077, Q95TV4, Q9VML0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project