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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 (LOC108351137), 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 (Pklr), Pyruvate kinase (Pkm)
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)DescriptionActionsGraphical viewLength
Binding sitei130NADBy similarity1
Binding sitei175NAD; via carbonyl oxygenBy similarity1
Binding sitei197NADBy similarity1
Binding sitei217NADBy similarity1
Active sitei248NucleophilePROSITE-ProRule annotation1
Sitei275Activates thiol group during catalysisBy similarity1
Binding sitei278Glyceraldehyde 3-phosphateBy similarity1
Binding sitei330Glyceraldehyde 3-phosphateBy similarity1
Binding sitei412NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi109 – 110NADBy similarity2

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)DescriptionActionsGraphical viewLength
ChainiPRO_00003802451 – 432Glyceraldehyde-3-phosphate dehydrogenase, testis-specificAdd BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei350PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9ESV6.
PRIDEiQ9ESV6.

PTM databases

iPTMnetiQ9ESV6.
PhosphoSitePlusiQ9ESV6.
SwissPalmiQ9ESV6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000021009.
ExpressionAtlasiQ9ESV6. baseline and differential.
GenevisibleiQ9ESV6. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028518.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi102 – 105Combined sources4
Helixi109 – 121Combined sources13
Beta strandi124 – 129Combined sources6
Helixi135 – 143Combined sources9
Turni146 – 148Combined sources3
Beta strandi155 – 158Combined sources4
Beta strandi161 – 164Combined sources4
Beta strandi167 – 172Combined sources6
Helixi177 – 179Combined sources3
Helixi182 – 185Combined sources4
Beta strandi189 – 192Combined sources4
Beta strandi194 – 196Combined sources3
Helixi200 – 203Combined sources4
Helixi205 – 208Combined sources4
Beta strandi214 – 218Combined sources5
Beta strandi221 – 223Combined sources3
Turni228 – 230Combined sources3
Helixi232 – 234Combined sources3
Turni237 – 239Combined sources3
Beta strandi241 – 244Combined sources4
Helixi248 – 264Combined sources17
Beta strandi266 – 276Combined sources11
Beta strandi281 – 285Combined sources5
Helixi293 – 295Combined sources3
Turni298 – 300Combined sources3
Beta strandi303 – 305Combined sources3
Helixi309 – 316Combined sources8
Helixi318 – 320Combined sources3
Beta strandi323 – 332Combined sources10
Beta strandi337 – 347Combined sources11
Helixi351 – 363Combined sources13
Turni364 – 369Combined sources6
Beta strandi370 – 373Combined sources4
Helixi379 – 382Combined sources4
Beta strandi388 – 392Combined sources5
Turni393 – 395Combined sources3
Beta strandi397 – 400Combined sources4
Beta strandi403 – 410Combined sources8
Helixi414 – 429Combined sources16

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9ESV6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 97Testis-specific N-terminal extensionBy similarityAdd BLAST97
Regioni247 – 249Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni307 – 308Glyceraldehyde 3-phosphate bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi20 – 34Cys/Pro-richAdd BLAST15
Compositional biasi55 – 65Poly-ProAdd BLAST11
Compositional biasi76 – 96Poly-ProAdd BLAST21

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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VYNX-ray2.20D102-432[»]
2VYVX-ray2.38D102-432[»]
ProteinModelPortaliQ9ESV6.
SMRiQ9ESV6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028518.

PTM databases

iPTMnetiQ9ESV6.
PhosphoSitePlusiQ9ESV6.
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.
PhylomeDBiQ9ESV6.
TreeFamiTF300533.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9ESV6.
PROiQ9ESV6.

Gene expression databases

BgeeiENSRNOG00000021009.
ExpressionAtlasiQ9ESV6. baseline and differential.
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...

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: November 2, 2016
This is version 107 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.