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Protein

Epididymal secretory glutathione peroxidase

Gene

GPX5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731By similarity

GO - Molecular functioni

GO - Biological processi

  • lipid metabolic process Source: ProtInc
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.9. 2681.

Protein family/group databases

PeroxiBasei3604. HsGPx05-A.
3629. HsGPx05-B.

Names & Taxonomyi

Protein namesi
Recommended name:
Epididymal secretory glutathione peroxidase (EC:1.11.1.9)
Alternative name(s):
Epididymis-specific glutathione peroxidase-like protein
Short name:
EGLP
Glutathione peroxidase 5
Short name:
GPx-5
Short name:
GSHPx-5
Gene namesi
Name:GPX5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 6, Unplaced

Organism-specific databases

HGNCiHGNC:4557. GPX5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28953.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 221200Epididymal secretory glutathione peroxidasePRO_0000013076Add
BLAST

Proteomic databases

PaxDbiO75715.
PRIDEiO75715.

Expressioni

Tissue specificityi

Epididymis.

Gene expression databases

BgeeiO75715.
CleanExiHS_GPX5.
ExpressionAtlasiO75715. baseline and differential.
GenevisibleiO75715. HS.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 423Combined sources
Beta strandi44 – 518Combined sources
Beta strandi53 – 553Combined sources
Helixi56 – 594Combined sources
Beta strandi62 – 698Combined sources
Beta strandi71 – 733Combined sources
Helixi74 – 785Combined sources
Helixi79 – 8911Combined sources
Helixi90 – 923Combined sources
Beta strandi94 – 1007Combined sources
Helixi112 – 1143Combined sources
Helixi115 – 1217Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi140 – 1423Combined sources
Helixi147 – 1559Combined sources
Turni166 – 1683Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi185 – 1884Combined sources
Beta strandi194 – 1985Combined sources
Helixi204 – 21411Combined sources
Helixi215 – 2173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I3YX-ray2.00A28-220[»]
ProteinModelPortaliO75715.
SMRiO75715. Positions 31-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75715.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000115921.
HOVERGENiHBG004333.
InParanoidiO75715.
KOiK00432.
OMAiMSTEIYA.
OrthoDBiEOG7KQ23C.
PhylomeDBiO75715.
TreeFamiTF105318.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75715-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTTQLRVVHL LPLLLACFVQ TSPKQEKMKM DCHKDEKGTI YDYEAIALNK
60 70 80 90 100
NEYVSFKQYV GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP
110 120 130 140 150
CNQFGKQEPG DNKEILPGLK YVRPGGGFVP SFQLFEKGDV NGEKEQKVFS
160 170 180 190 200
FLKHSCPHPS EILGTFKSIS WDPVKVHDIR WNFEKFLVGP DGIPVMRWSH
210 220
RATVSSVKTD ILAYLKQFKT K
Length:221
Mass (Da):25,202
Last modified:November 1, 1998 - v1
Checksum:iCE3E7BFD53CE979F
GO
Isoform 2 (identifier: O75715-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-221: ELNALQEELK...LAYLKQFKTK → GMSVQGEDLYLVSSFLRKGM

Note: No experimental confirmation available.
Show »
Length:100
Mass (Da):11,429
Checksum:i04BFE67B6E77684F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851L → P.
Corresponds to variant rs58554303 [ dbSNP | Ensembl ].
VAR_061206
Natural varianti85 – 851L → V.1 Publication
Corresponds to variant rs769188 [ dbSNP | Ensembl ].
VAR_012040

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei81 – 221141ELNAL…QFKTK → GMSVQGEDLYLVSSFLRKGM in isoform 2. 1 PublicationVSP_043046Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005277 mRNA. Translation: CAA06463.1.
AY882013 Genomic DNA. Translation: AAW56939.1.
AL049543 Genomic DNA. Translation: CAB71121.1.
CH471081 Genomic DNA. Translation: EAX03168.1.
BC128159 mRNA. Translation: AAI28160.1.
BC128160 mRNA. Translation: AAI28161.1.
CCDSiCCDS4652.1. [O75715-1]
CCDS4653.1. [O75715-2]
RefSeqiNP_001500.1. NM_001509.2. [O75715-1]
NP_003987.2. NM_003996.3. [O75715-2]
UniGeneiHs.248129.

Genome annotation databases

EnsembliENST00000412168; ENSP00000392398; ENSG00000224586. [O75715-1]
ENST00000469384; ENSP00000419935; ENSG00000224586. [O75715-2]
ENST00000550775; ENSP00000450365; ENSG00000257770. [O75715-1]
ENST00000551639; ENSP00000449271; ENSG00000257770. [O75715-2]
GeneIDi2880.
KEGGihsa:2880.
UCSCiuc003nll.2. human. [O75715-1]
uc003nlm.2. human. [O75715-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005277 mRNA. Translation: CAA06463.1.
AY882013 Genomic DNA. Translation: AAW56939.1.
AL049543 Genomic DNA. Translation: CAB71121.1.
CH471081 Genomic DNA. Translation: EAX03168.1.
BC128159 mRNA. Translation: AAI28160.1.
BC128160 mRNA. Translation: AAI28161.1.
CCDSiCCDS4652.1. [O75715-1]
CCDS4653.1. [O75715-2]
RefSeqiNP_001500.1. NM_001509.2. [O75715-1]
NP_003987.2. NM_003996.3. [O75715-2]
UniGeneiHs.248129.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I3YX-ray2.00A28-220[»]
ProteinModelPortaliO75715.
SMRiO75715. Positions 31-218.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3604. HsGPx05-A.
3629. HsGPx05-B.

Polymorphism and mutation databases

BioMutaiGPX5.

Proteomic databases

PaxDbiO75715.
PRIDEiO75715.

Protocols and materials databases

DNASUi2880.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000412168; ENSP00000392398; ENSG00000224586. [O75715-1]
ENST00000469384; ENSP00000419935; ENSG00000224586. [O75715-2]
ENST00000550775; ENSP00000450365; ENSG00000257770. [O75715-1]
ENST00000551639; ENSP00000449271; ENSG00000257770. [O75715-2]
GeneIDi2880.
KEGGihsa:2880.
UCSCiuc003nll.2. human. [O75715-1]
uc003nlm.2. human. [O75715-2]

Organism-specific databases

CTDi2880.
GeneCardsiGC06P028493.
HGNCiHGNC:4557. GPX5.
MIMi603435. gene.
neXtProtiNX_O75715.
PharmGKBiPA28953.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000115921.
HOVERGENiHBG004333.
InParanoidiO75715.
KOiK00432.
OMAiMSTEIYA.
OrthoDBiEOG7KQ23C.
PhylomeDBiO75715.
TreeFamiTF105318.

Enzyme and pathway databases

BRENDAi1.11.1.9. 2681.

Miscellaneous databases

EvolutionaryTraceiO75715.
GeneWikiiGPX5.
GenomeRNAii2880.
NextBioi11375.
PROiO75715.
SOURCEiSearch...

Gene expression databases

BgeeiO75715.
CleanExiHS_GPX5.
ExpressionAtlasiO75715. baseline and differential.
GenevisibleiO75715. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract."
    Hall L., Williams K., Perry A.C.F., Frayne J., Jury J.A.
    Biochem. J. 333:5-9(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Epididymis.
  2. NIEHS SNPs program
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-85.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "Crystal structure of human glutathione peroxidase 5."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-220.

Entry informationi

Entry nameiGPX5_HUMAN
AccessioniPrimary (citable) accession number: O75715
Secondary accession number(s): A1A4Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 24, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.