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Protein

Epididymal secretory glutathione peroxidase

Gene

Gpx5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Protein family/group databases

PeroxiBasei3735. RnoGPx05.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69227. Gpx5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 221200Epididymal secretory glutathione peroxidasePRO_0000013080Add
BLAST

Proteomic databases

PRIDEiP30710.

Expressioni

Tissue specificityi

Epididymis.

Structurei

3D structure databases

ProteinModelPortaliP30710.
SMRiP30710. Positions 31-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004333.
InParanoidiP30710.
KOiK00432.
PhylomeDBiP30710.

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]

Sequencei

Sequence statusi: Complete.

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

P30710-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIQLRVFYL VPLLLASYVQ TTPRLEKMKM DCYKDVKGTI YNYEALSLNG
60 70 80 90 100
KERIPFKQYA GKHVLFVNVA TYCGLTIQYP ELNALQDDLK QFGLVILGFP
110 120 130 140 150
CNQFGKQEPG DNTEILPGLK YVRPGKGFLP NFQLFAKGDV NGEKEQEIFT
160 170 180 190 200
FLKRSCPHPS ETVVTSKHTF WEPIKVHDIR WNFEKFLVGP NGVPVMRWFH
210 220
QAPVSTVKSD ILAYLNQFKT I
Length:221
Mass (Da):25,385
Last modified:April 1, 1993 - v1
Checksum:i0D9D3FAAC9F12D16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62404 mRNA. Translation: CAA44274.1.
PIRiS24328.
RefSeqiNP_001099208.1. NM_001105738.1.
UniGeneiRn.218434.

Genome annotation databases

GeneIDi113919.
KEGGirno:113919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62404 mRNA. Translation: CAA44274.1.
PIRiS24328.
RefSeqiNP_001099208.1. NM_001105738.1.
UniGeneiRn.218434.

3D structure databases

ProteinModelPortaliP30710.
SMRiP30710. Positions 31-218.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei3735. RnoGPx05.

Proteomic databases

PRIDEiP30710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi113919.
KEGGirno:113919.

Organism-specific databases

CTDi2880.
RGDi69227. Gpx5.

Phylogenomic databases

HOVERGENiHBG004333.
InParanoidiP30710.
KOiK00432.
PhylomeDBiP30710.

Miscellaneous databases

PROiP30710.

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

  1. "Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon."
    Perry A.C.F., Jones R., Niang L.S.P., Jackson R.M., Hall L.
    Biochem. J. 285:863-870(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Epididymis.

Entry informationi

Entry nameiGPX5_RAT
AccessioniPrimary (citable) accession number: P30710
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 8, 2016
This is version 97 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

Complete proteome, Reference proteome

Documents

  1. 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.