Reviewed, UniProtKB/Swiss-Prot O75715 (GPX5_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	lipid 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 component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 221

200

Epididymal secretory glutathione peroxidase

PRO_0000013076

Sites

Active site

73

1

By similarity

Natural variations

Natural variant

85

1

L → V: dbSNP rs769188. Ref.2

VAR_012040

Secondary structure

1

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221

Helix Strand Turn

Details...

Helix

40 – 42

3

Beta strand

44 – 51

8

Beta strand

53 – 55

3

Helix

56 – 59

4

Beta strand

62 – 69

8

Beta strand

71 – 73

3

Helix

74 – 78

5

Helix

79 – 89

11

Helix

90 – 92

3

Beta strand

94 – 100

7

Helix

112 – 114

3

Helix

115 – 121

7

Beta strand

131 – 135

5

Beta strand

140 – 142

3

Helix

147 – 155

9

Beta strand

161 – 164

4

Turn

166 – 168

3

Beta strand

171 – 175

5

Beta strand

185 – 188

4

Beta strand

194 – 198

5

Helix

204 – 214

11

Helix

215 – 217

3

Sequences

	Sequence		Length	Mass (Da)
	O75715-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: CE3E7BFD53CE979F	FASTA	221	25,202
	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

References

	« Hide 'large scale' referencesShow '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. , 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

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ005277 mRNA. Translation: CAA06463.1.
AY882013 Genomic DNA. Translation: AAW56939.1.
AL049543 Genomic DNA. Translation: CAB71121.1.

IPI

IPI00026802.

RefSeq

NP_001500.1.

UniGene

Hs.248129

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I3Y	X-ray	2.00	A	28-220	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

3604. HsGPx05-a.
3629. HsGPx05-b.

Proteomic databases

PRIDE

O75715.

Genome annotation databases

Ensembl

ENSG00000079782. Homo sapiens. [Contig view]

GeneID

2880.

KEGG

hsa:2880.

Organism-specific databases

GeneCards

GC06P028604.

H-InvDB

HIX0005673.

HGNC

HGNC:4557. GPX5.

MIM

603435. gene.

PharmGKB

PA28953.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O75715.

HOVERGEN

O75715.

OMA

O75715. TIYDYEA.

Enzyme and pathway databases

BRENDA

1.11.1.9. 247.

Gene expression databases

ArrayExpress

O75715.

CleanEx

HS_GPX5.

GermOnline

ENSG00000079782. Homo sapiens.

Family and domain databases

InterPro

IPR000889. Glutathione_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR11592. Glut_peroxidase. 1 hit.

Pfam

PF00255. GSHPx. 1 hit.
[Graphical view]

PIRSF

PIRSF000303. Glutathion_perox. 1 hit.

PRINTS

PR01011. GLUTPROXDASE.

PROSITE

PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

11375.

SOURCE

Search...

Entry information

Entry name

GPX5_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)