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Protein

Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

Gene

Gapdhs

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity).By similarity

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (Gapdh-ps2), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (RGD1562758)
  2. Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Alpha-enolase (Eno1), Beta-enolase (Eno3), Gamma-enolase (Eno2)
  5. Pyruvate kinase PKLR (Pklr), Pyruvate kinase PKM (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (LOC100362738), Pyruvate kinase (Pkm), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301NADBy similarity
Binding sitei175 – 1751NAD; via carbonyl oxygenBy similarity
Binding sitei197 – 1971NADBy similarity
Binding sitei217 – 2171NADBy similarity
Active sitei248 – 2481NucleophilePROSITE-ProRule annotation
Sitei275 – 2751Activates thiol group during catalysisBy similarity
Binding sitei278 – 2781Glyceraldehyde 3-phosphateBy similarity
Binding sitei330 – 3301Glyceraldehyde 3-phosphateBy similarity
Binding sitei412 – 4121NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi109 – 1102NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • glucose metabolic process Source: InterPro
  • glycolytic process Source: RGD
  • spermatid development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.12. 5301.
ReactomeiR-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (EC:1.2.1.12)
Alternative name(s):
Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
Short name:
GAPDH-2
Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
Gene namesi
Name:Gapdhs
Synonyms:Gapd-s, Gapds
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620150. Gapdhs.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • cytoplasm Source: RGD
  • motile cilium Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glyceraldehyde-3-phosphate dehydrogenase, testis-specificPRO_0000380245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei350 – 3501PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9ESV6.
PRIDEiQ9ESV6.

PTM databases

iPTMnetiQ9ESV6.
PhosphoSiteiQ9ESV6.
SwissPalmiQ9ESV6.

Expressioni

Tissue specificityi

Expressed in both head and flagellum of epididymal sperm.1 Publication

Gene expression databases

ExpressionAtlasiQ9ESV6. baseline.
GenevisibleiQ9ESV6. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028518.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi102 – 1054Combined sources
Helixi109 – 12113Combined sources
Beta strandi124 – 1296Combined sources
Helixi135 – 1439Combined sources
Turni146 – 1483Combined sources
Beta strandi155 – 1584Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi167 – 1726Combined sources
Helixi177 – 1793Combined sources
Helixi182 – 1854Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi194 – 1963Combined sources
Helixi200 – 2034Combined sources
Helixi205 – 2084Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi221 – 2233Combined sources
Turni228 – 2303Combined sources
Helixi232 – 2343Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2444Combined sources
Helixi248 – 26417Combined sources
Beta strandi266 – 27611Combined sources
Beta strandi281 – 2855Combined sources
Helixi293 – 2953Combined sources
Turni298 – 3003Combined sources
Beta strandi303 – 3053Combined sources
Helixi309 – 3168Combined sources
Helixi318 – 3203Combined sources
Beta strandi323 – 33210Combined sources
Beta strandi337 – 34711Combined sources
Helixi351 – 36313Combined sources
Turni364 – 3696Combined sources
Beta strandi370 – 3734Combined sources
Helixi379 – 3824Combined sources
Beta strandi388 – 3925Combined sources
Turni393 – 3953Combined sources
Beta strandi397 – 4004Combined sources
Beta strandi403 – 4108Combined sources
Helixi414 – 42916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VYNX-ray2.20D102-432[»]
2VYVX-ray2.38D102-432[»]
ProteinModelPortaliQ9ESV6.
SMRiQ9ESV6. Positions 100-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ESV6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9797Testis-specific N-terminal extensionBy similarityAdd
BLAST
Regioni247 – 2493Glyceraldehyde 3-phosphate bindingBy similarity
Regioni307 – 3082Glyceraldehyde 3-phosphate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 3415Cys/Pro-richAdd
BLAST
Compositional biasi55 – 6511Poly-ProAdd
BLAST
Compositional biasi76 – 9621Poly-ProAdd
BLAST

Domaini

The testis-specific N-terminal extension mediates tight association with the cytoskeletal fibrous sheath of the spermatozoa flagellum, possibly via interchain disulfide-bonding of Cys-33 with sheath components.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiQ9ESV6.
KOiK10705.
OrthoDBiEOG7Q5HDF.
PhylomeDBiQ9ESV6.
TreeFamiTF300533.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ESV6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRDVVLTN VTVVQLRRDP CPCPCPCPCP CPCPVIRPPP PPPKVEEPPP
60 70 80 90 100
PKEEPPPPPP PPPPPQIEPE EPKEAPPPPP PPPPPPPPPP PPPPKPAKEL
110 120 130 140 150
TVGINGFGRI GRLVLRVCME KGVRVVAVND PFIDPEYMVY MFKYDSTHGR
160 170 180 190 200
YKGTVEHKNG RLVVDNLEIN VFQCKEPKEI PWSSVGNPYV VEATGVYLSI
210 220 230 240 250
EAASGHISSG ARRVIVTAPS PDAPMLVMGV NEKDYNPGSM TVVSNASCTT
260 270 280 290 300
NCLAPLAKVI HERFGIVEGL MTTVHAYTAT QKTVDGPSKK DWRGGRGAHQ
310 320 330 340 350
NIIPSSTGAA KAVGKVIPEL NGKLTGMAFR VPTPNVSVVD LTCRLAQPAS
360 370 380 390 400
YTAIKEAVKA AAKGPMAGIL AYTEDQVVST DFNGDSHSSI FDAKAGIALN
410 420 430
DNFVKLVSWY DNEYGYSHRV VDLLRYMFSR EK
Length:432
Mass (Da):46,708
Last modified:March 1, 2001 - v1
Checksum:iEC5F08F31DC8D35C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297631 mRNA. Translation: CAC05399.1.
RefSeqiNP_076454.1. NM_023964.1.
UniGeneiRn.64496.

Genome annotation databases

EnsembliENSRNOT00000028518; ENSRNOP00000028518; ENSRNOG00000021009.
GeneIDi66020.
KEGGirno:66020.
UCSCiRGD:620150. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297631 mRNA. Translation: CAC05399.1.
RefSeqiNP_076454.1. NM_023964.1.
UniGeneiRn.64496.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VYNX-ray2.20D102-432[»]
2VYVX-ray2.38D102-432[»]
ProteinModelPortaliQ9ESV6.
SMRiQ9ESV6. Positions 100-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028518.

PTM databases

iPTMnetiQ9ESV6.
PhosphoSiteiQ9ESV6.
SwissPalmiQ9ESV6.

Proteomic databases

PaxDbiQ9ESV6.
PRIDEiQ9ESV6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028518; ENSRNOP00000028518; ENSRNOG00000021009.
GeneIDi66020.
KEGGirno:66020.
UCSCiRGD:620150. rat.

Organism-specific databases

CTDi26330.
RGDi620150. Gapdhs.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
InParanoidiQ9ESV6.
KOiK10705.
OrthoDBiEOG7Q5HDF.
PhylomeDBiQ9ESV6.
TreeFamiTF300533.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BRENDAi1.2.1.12. 5301.
ReactomeiR-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.

Miscellaneous databases

EvolutionaryTraceiQ9ESV6.
NextBioi614310.
PROiQ9ESV6.

Gene expression databases

ExpressionAtlasiQ9ESV6. baseline.
GenevisibleiQ9ESV6. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of rat testis-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDH-2) cDNA."
    McLaughlin E.A., Hall L.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Testis.
  2. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
    Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
    Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals target for contraceptive design."
    Frayne J., Taylor A., Cameron G., Hadfield A.T.
    J. Biol. Chem. 284:22703-22712(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 102-432 IN TETRAMER WITH E.COLI GAPDH.

Entry informationi

Entry nameiG3PT_RAT
AccessioniPrimary (citable) accession number: Q9ESV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2001
Last modified: February 17, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.