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O75715

- GPX5_HUMAN

UniProt

O75715 - GPX5_HUMAN

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Protein

Epididymal secretory glutathione peroxidase

Gene
GPX5
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 731 By similarity

GO - Molecular functioni

  1. glutathione peroxidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

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: Chromosome 6

Organism-specific databases

HGNCiHGNC:4557. GPX5.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28953.

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiO75715.
PRIDEiO75715.

Expressioni

Tissue specificityi

Epididymis.

Gene expression databases

ArrayExpressiO75715.
BgeeiO75715.
CleanExiHS_GPX5.
GenevestigatoriO75715.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000392398.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I3YX-ray2.00A28-220[»]
ProteinModelPortaliO75715.
SMRiO75715. Positions 31-218.

Miscellaneous databases

EvolutionaryTraceiO75715.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0386.
HOGENOMiHOG000115921.
HOVERGENiHBG004333.
InParanoidiO75715.
KOiK00432.
OMAiIAEFCTI.
OrthoDBiEOG7KQ23C.
PhylomeDBiO75715.
TreeFamiTF105318.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
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. Align

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

MTTQLRVVHL LPLLLACFVQ TSPKQEKMKM DCHKDEKGTI YDYEAIALNK    50
NEYVSFKQYV GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP 100
CNQFGKQEPG DNKEILPGLK YVRPGGGFVP SFQLFEKGDV NGEKEQKVFS 150
FLKHSCPHPS EILGTFKSIS WDPVKVHDIR WNFEKFLVGP DGIPVMRWSH 200
RATVSSVKTD ILAYLKQFKT K 221
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. VSP_043046Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4652.1. [O75715-1 ]
CCDS4653.1. [O75715-2 ]
RefSeqi NP_001500.1. NM_001509.2. [O75715-1 ]
NP_003987.2. NM_003996.3. [O75715-2 ]
UniGenei Hs.248129.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I3Y X-ray 2.00 A 28-220 [» ]
ProteinModelPortali O75715.
SMRi O75715. Positions 31-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000392398.

Chemistry

DrugBanki DB00143. Glutathione.

Protein family/group databases

PeroxiBasei 3604. HsGPx05-A.
3629. HsGPx05-B.

Proteomic databases

PaxDbi O75715.
PRIDEi O75715.

Protocols and materials databases

DNASUi 2880.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000412168 ; ENSP00000392398 ; ENSG00000224586 . [O75715-1 ]
ENST00000469384 ; ENSP00000419935 ; ENSG00000224586 . [O75715-2 ]
GeneIDi 2880.
KEGGi hsa:2880.
UCSCi uc003nll.2. human. [O75715-1 ]
uc003nlm.2. human. [O75715-2 ]

Organism-specific databases

CTDi 2880.
GeneCardsi GC06P028493.
HGNCi HGNC:4557. GPX5.
MIMi 603435. gene.
neXtProti NX_O75715.
PharmGKBi PA28953.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0386.
HOGENOMi HOG000115921.
HOVERGENi HBG004333.
InParanoidi O75715.
KOi K00432.
OMAi IAEFCTI.
OrthoDBi EOG7KQ23C.
PhylomeDBi O75715.
TreeFami TF105318.

Miscellaneous databases

EvolutionaryTracei O75715.
GeneWikii GPX5.
GenomeRNAii 2880.
NextBioi 11375.
PROi O75715.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75715.
Bgeei O75715.
CleanExi HS_GPX5.
Genevestigatori O75715.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
PANTHERi PTHR11592. PTHR11592. 1 hit.
Pfami PF00255. GSHPx. 1 hit.
[Graphical view ]
PIRSFi PIRSF000303. Glutathion_perox. 1 hit.
PRINTSi PR01011. GLUTPROXDASE.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 124 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

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