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Reviewed, UniProtKB/Swiss-Prot O75715 (GPX5_HUMAN)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Epididymal secretory glutathione peroxidase
    EC=1.11.1.9
Alternative name(s):
    Epididymis-specific glutathione peroxidase-like protein
      Short name=EGLP
Gene names
Name: GPX5
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Subcellular location

Secreted.

Tissue specificity

Epididymis.

Sequence similarities

Belongs to the glutathione peroxidase family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionOxidoreductase
Peroxidase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processlipid metabolic process Ref.1

Non-traceable author statement. Source: ProtInc

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglutathione peroxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 221200Epididymal secretory glutathione peroxidase
PRO_0000013076

Sites

Active site731 By similarity

Natural variations

Natural variant851L → V: dbSNP rs769188. Ref.2
VAR_012040

Secondary structure

....................................... 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75715-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: CE3E7BFD53CE979F

FASTA22125,202
        10         20         30         40         50         60 
MTTQLRVVHL LPLLLACFVQ TSPKQEKMKM DCHKDEKGTI YDYEAIALNK NEYVSFKQYV 

        70         80         90        100        110        120 
GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP CNQFGKQEPG DNKEILPGLK 

       130        140        150        160        170        180 
YVRPGGGFVP SFQLFEKGDV NGEKEQKVFS FLKHSCPHPS EILGTFKSIS WDPVKVHDIR 

       190        200        210        220 
WNFEKFLVGP DGIPVMRWSH RATVSSVKTD ILAYLKQFKT K 

« Hide

References

« Hide 'large scale' references
[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: 9639555] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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. expand/collapse author list , 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: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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.

Web resources

Cross-references

Sequence databases

AJ005277 mRNA. Translation: CAA06463.1.
AY882013 Genomic DNA. Translation: AAW56939.1.
AL049543 Genomic DNA. Translation: CAB71121.1.
IPIIPI00026802.
RefSeqNP_001500.1.
UniGeneHs.248129

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2I3YX-ray2.00A28-220[»]
ModBaseSearch...

Protein family/group databases

PeroxiBase3604. HsGPx05-a.
3629. HsGPx05-b.

Proteomic databases

PRIDEO75715.

Genome annotation databases

EnsemblENSG00000079782. Homo sapiens. [Contig view]
GeneID2880.
KEGGhsa:2880.

Organism-specific databases

GeneCardsGC06P028604.
H-InvDBHIX0005673.
HGNCHGNC:4557. GPX5.
MIM603435. gene.
PharmGKBPA28953.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO75715.
HOVERGENO75715.
OMAO75715. TIYDYEA.

Enzyme and pathway databases

BRENDA1.11.1.9. 247.

Gene expression databases

ArrayExpressO75715.
CleanExHS_GPX5.
GermOnlineENSG00000079782. Homo sapiens.

Family and domain databases

InterProIPR000889. Glutathione_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR11592. Glut_peroxidase. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00143. Glutathione.
NextBio11375.
SOURCESearch...

Entry information

Entry nameGPX5_HUMAN
AccessionPrimary (citable) accession number: O75715
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents