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Protein

Glutathione peroxidase 3

Gene

Gpx3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

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

GO - Molecular functioni

  • glutathione binding Source: RGD
  • glutathione peroxidase activity Source: UniProtKB
  • selenium binding Source: UniProtKB

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • female pregnancy Source: RGD
  • glutathione metabolic process Source: RGD
  • hydrogen peroxide catabolic process Source: RGD
  • protein homotetramerization Source: UniProtKB
  • response to corticosterone Source: RGD
  • response to drug Source: RGD
  • response to molecule of fungal origin Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to oxidative stress Source: InterPro
  • response to selenium ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Protein family/group databases

PeroxiBasei3732. RnoGPx03.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 3 (EC:1.11.1.9)
Short name:
GPx-3
Short name:
GSHPx-3
Alternative name(s):
Plasma glutathione peroxidase
Short name:
GPx-P
Short name:
GSHPx-P
Gene namesi
Name:Gpx3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69224. Gpx3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 226202Glutathione peroxidase 3PRO_0000013064Add
BLAST

Proteomic databases

PRIDEiP23764.

PTM databases

iPTMnetiP23764.

Expressioni

Tissue specificityi

Secreted in plasma.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP23764.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP23764.
KOiK00432.
PhylomeDBiP23764.

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.

P23764-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARILRASCL LSLLLAGFVP PGRGQEKSKT DCHGGMSGTI YEYGALTIDG
60 70 80 90 100
EEYIPFKQYA GKYILFVNVA SYUGLTDQYL ELNALQEELG PFGLVILGFP
110 120 130 140 150
CNQFGKQEPG ENSEILPSLK YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT
160 170 180 190 200
FLKNSCPPTA ELLGSPGRLF WEPMKIHDIR WNFEKFLVGP DGIPIMRWYH
210 220
RTTVSNVKMD ILSYMRRQAA LGARGK
Length:226
Mass (Da):25,424
Last modified:February 26, 2008 - v2
Checksum:i414BF56F8F553F88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → S in BAA00587 (PubMed:1939013).Curated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei73 – 731Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00680 mRNA. Translation: BAA00587.2.
BC062227 mRNA. Translation: AAH62227.1.
PIRiJX0176.
RefSeqiNP_071970.2. NM_022525.3.
UniGeneiRn.108074.

Genome annotation databases

GeneIDi64317.
KEGGirno:64317.
UCSCiRGD:69224. rat.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00680 mRNA. Translation: BAA00587.2.
BC062227 mRNA. Translation: AAH62227.1.
PIRiJX0176.
RefSeqiNP_071970.2. NM_022525.3.
UniGeneiRn.108074.

3D structure databases

ProteinModelPortaliP23764.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei3732. RnoGPx03.

PTM databases

iPTMnetiP23764.

Proteomic databases

PRIDEiP23764.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64317.
KEGGirno:64317.
UCSCiRGD:69224. rat.

Organism-specific databases

CTDi2878.
RGDi69224. Gpx3.

Phylogenomic databases

HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP23764.
KOiK00432.
PhylomeDBiP23764.

Miscellaneous databases

PROiP23764.

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. "Tissue specific expression of the plasma glutathione peroxidase gene in rat kidney."
    Yoshimura S., Watanabe K., Suemizu H., Onozawa T., Mizoguchi J., Tsuda K., Hatta H., Moriuchi T.
    J. Biochem. 109:918-923(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "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].
    Tissue: Pituitary.

Entry informationi

Entry nameiGPX3_RAT
AccessioniPrimary (citable) accession number: P23764
Secondary accession number(s): Q6P6H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 120 of the entry and version 2 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.