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Protein

Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

Gene

Gapdhs

Organism
Mus musculus (Mouse)
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.1 Publication

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 (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (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 sitei138NADBy similarity1
Binding sitei183NAD; via carbonyl oxygenBy similarity1
Binding sitei205NADBy similarity1
Binding sitei225NADBy similarity1
Active sitei256NucleophilePROSITE-ProRule annotation1
Sitei283Activates thiol group during catalysisBy similarity1
Binding sitei286Glyceraldehyde 3-phosphateBy similarity1
Binding sitei338Glyceraldehyde 3-phosphateBy similarity1
Binding sitei420NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi117 – 118NADBy similarity2

GO - Molecular functioni

GO - Biological processi

  • flagellated sperm motility Source: UniProtKB
  • glucose metabolic process Source: InterPro
  • glycolytic process Source: MGI
  • positive regulation of glycolytic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95653. Gapdhs.

Subcellular locationi

GO - Cellular componenti

  • cilium Source: MGI
  • cytoplasm Source: UniProtKB-SubCell
  • motile cilium Source: MGI
  • nucleus Source: MGI
  • sperm fibrous sheath Source: MGI
  • sperm principal piece Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice display greatly reduced ATP levels in sperm, severely impaired sperm motility and are infertile.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001455041 – 440Glyceraldehyde-3-phosphate dehydrogenase, testis-specificAdd BLAST440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei358PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ64467.
MaxQBiQ64467.
PaxDbiQ64467.
PeptideAtlasiQ64467.
PRIDEiQ64467.

PTM databases

iPTMnetiQ64467.
PhosphoSitePlusiQ64467.
SwissPalmiQ64467.

Expressioni

Tissue specificityi

Testis specific.

Developmental stagei

First expressed at day 20 in post-meiotic germ cells. Levels increase until day 24 and then remain constant during maturity.

Gene expression databases

BgeeiENSMUSG00000061099.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ64467. 3 interactors.
MINTiMINT-4095460.
STRINGi10090.ENSMUSP00000074317.

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi109 – 113Combined sources5
Helixi117 – 129Combined sources13
Beta strandi132 – 137Combined sources6
Helixi143 – 151Combined sources9
Turni154 – 156Combined sources3
Beta strandi163 – 166Combined sources4
Beta strandi169 – 172Combined sources4
Beta strandi175 – 180Combined sources6
Helixi185 – 187Combined sources3
Helixi190 – 193Combined sources4
Beta strandi197 – 200Combined sources4
Beta strandi202 – 204Combined sources3
Helixi208 – 216Combined sources9
Beta strandi220 – 226Combined sources7
Beta strandi229 – 231Combined sources3
Turni236 – 238Combined sources3
Helixi240 – 242Combined sources3
Turni245 – 247Combined sources3
Beta strandi249 – 252Combined sources4
Helixi256 – 271Combined sources16
Beta strandi274 – 284Combined sources11
Beta strandi289 – 293Combined sources5
Helixi301 – 303Combined sources3
Turni306 – 308Combined sources3
Beta strandi311 – 314Combined sources4
Turni317 – 320Combined sources4
Helixi321 – 324Combined sources4
Helixi326 – 328Combined sources3
Turni329 – 331Combined sources3
Beta strandi332 – 340Combined sources9
Beta strandi345 – 355Combined sources11
Helixi359 – 371Combined sources13
Turni372 – 377Combined sources6
Beta strandi378 – 381Combined sources4
Helixi387 – 390Combined sources4
Beta strandi396 – 400Combined sources5
Turni401 – 403Combined sources3
Beta strandi405 – 408Combined sources4
Beta strandi411 – 418Combined sources8
Helixi422 – 437Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5C7IX-ray2.01O/R107-439[»]
ProteinModelPortaliQ64467.
SMRiQ64467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 105Testis-specific N-terminal extensionBy similarityAdd BLAST105
Regioni255 – 257Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni315 – 316Glyceraldehyde 3-phosphate bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi21 – 41Cys/Pro-richAdd BLAST21
Compositional biasi54 – 73Poly-ProAdd BLAST20
Compositional biasi84 – 100Poly-ProAdd BLAST17

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.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiQ64467.
KOiK10705.
PhylomeDBiQ64467.
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.

Q64467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRDVVLTN VTVVQLRRDR CPCPCPCPCP CPCPVIRPPP PKLEDPPPTV
60 70 80 90 100
EEQPPPPPPP PPPPPPPPPP PPPQIEPDKF EEAPPPPPPP PPPPPPPPPP
110 120 130 140 150
LQKPARELTV GINGFGRIGR LVLRVCMEKG IRVVAVNDPF IDPEYMVYMF
160 170 180 190 200
KYDSTHGRYK GNVEHKNGQL VVDNLEINTY QCKDPKEIPW SSIGNPYVVE
210 220 230 240 250
CTGVYLSIEA ASAHISSGAR RVVVTAPSPD APMFVMGVNE KDYNPGSMTI
260 270 280 290 300
VSNASCTTNC LAPLAKVIHE NFGIVEGLMT TVHSYTATQK TVDGPSKKDW
310 320 330 340 350
RGGRGAHQNI IPSSTGAAKA VGKVIPELKG KLTGMAFRVP TPNVSVVDLT
360 370 380 390 400
CRLAKPASYS AITEAVKAAA KGPLAGILAY TEDQVVSTDF NGNPHSSIFD
410 420 430 440
AKAGIALNDN FVKLVAWYDN EYGYSNRVVD LLRYMFSREK
Length:440
Mass (Da):47,657
Last modified:November 1, 1996 - v1
Checksum:i05FF0A093D1ABD9C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti33 – 34Missing in AAA80276 (PubMed:7736666).Curated2
Sequence conflicti43L → V in AAA80276 (PubMed:7736666).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60978 mRNA. Translation: AAA53033.1.
U09964 Genomic DNA. Translation: AAA80276.1.
CCDSiCCDS71933.1.
PIRiI49681.
RefSeqiNP_032111.1. NM_008085.2.
UniGeneiMm.436562.

Genome annotation databases

GeneIDi14447.
KEGGimmu:14447.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60978 mRNA. Translation: AAA53033.1.
U09964 Genomic DNA. Translation: AAA80276.1.
CCDSiCCDS71933.1.
PIRiI49681.
RefSeqiNP_032111.1. NM_008085.2.
UniGeneiMm.436562.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5C7IX-ray2.01O/R107-439[»]
ProteinModelPortaliQ64467.
SMRiQ64467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ64467. 3 interactors.
MINTiMINT-4095460.
STRINGi10090.ENSMUSP00000074317.

PTM databases

iPTMnetiQ64467.
PhosphoSitePlusiQ64467.
SwissPalmiQ64467.

Proteomic databases

EPDiQ64467.
MaxQBiQ64467.
PaxDbiQ64467.
PeptideAtlasiQ64467.
PRIDEiQ64467.

Protocols and materials databases

DNASUi14447.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14447.
KEGGimmu:14447.

Organism-specific databases

CTDi26330.
MGIiMGI:95653. Gapdhs.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiQ64467.
KOiK10705.
PhylomeDBiQ64467.
TreeFamiTF300533.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.

Miscellaneous databases

ChiTaRSiGapdhs. mouse.
PROiQ64467.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000061099.

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_MOUSE
AccessioniPrimary (citable) accession number: Q64467
Secondary accession number(s): Q60650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 153 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.