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Protein

Phospholipid hydroperoxide glutathione peroxidase, mitochondrial

Gene

Gpx4

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

Functioni

Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage.1 Publication

Catalytic activityi

2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O.1 Publication

Sites

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

GO - Molecular functioni

  • glutathione binding Source: RGD
  • glutathione peroxidase activity Source: RGD
  • phospholipid-hydroperoxide glutathione peroxidase activity Source: RGD
  • selenium binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cellular oxidant detoxification Source: GOC
  • glutathione metabolic process Source: RGD
  • hydrogen peroxide catabolic process Source: RGD
  • multicellular organism development Source: UniProtKB-KW
  • regulation of inflammatory response Source: RGD
  • response to estradiol Source: RGD
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.12. 5301.

Protein family/group databases

PeroxiBasei3733. RnoGPx04-A.
3812. RnoGPx04-B.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid hydroperoxide glutathione peroxidase, mitochondrial (EC:1.11.1.121 Publication)
Short name:
PHGPx
Alternative name(s):
Glutathione peroxidase 4
Short name:
GPx-4
Short name:
GSHPx-4
Gene namesi
Name:Gpx4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69226. Gpx4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 197Phospholipid hydroperoxide glutathione peroxidase, mitochondrialPRO_0000013073
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP36970.
PRIDEiP36970.

PTM databases

SwissPalmiP36970.

Expressioni

Tissue specificityi

Present primarily in testis. Expressed in flagella of epididymal sperm.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018691.

Structurei

3D structure databases

ProteinModelPortaliP36970.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
HOGENOMiHOG000277054.
HOVERGENiHBG004333.
KOiK05361.
PhylomeDBiP36970.

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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform Mitochondrial (identifier: P36970-1) [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

        10         20         30         40         50
MSWGRLSRLL KPALLCGALA VPGLAGTMCA SRDDWRCARS MHEFAAKDID
60 70 80 90 100
GHMVCLDKYR GCVCIVTNVA SQUGKTDVNY TQLVDLHARY AECGLRILAF
110 120 130 140 150
PCNQFGRQEP GSNQEIKEFA AGYNVRFDMY SKICVNGDDA HPLWKWMKVQ
160 170 180 190
PKGRGMLGNA IKWNFTKFLI DKNGCVVKRY GPMEEPQVIE KDLPCYL
Length:197
Mass (Da):22,225
Last modified:February 26, 2008 - v3
Checksum:i83FF001A5A42F814
GO
Isoform Nuclear (identifier: Q91XR8-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry Q91XR8.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:253
Mass (Da):29,335
GO
Isoform Cytoplasmic (identifier: P36970-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.

Note: Produced by alternative initiation at Met-28 of isoform Mitochondrial.
Show »
Length:170
Mass (Da):19,490
Checksum:iA882EE0827902EA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451A → S in AAC52503 (PubMed:7592947).Curated
Sequence conflicti45 – 451A → S in CAD61276 (Ref. 2) Curated
Sequence conflicti45 – 451A → S in CAD61277 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2727Missing in isoform Cytoplasmic. CuratedVSP_018746Add
BLAST

Non-standard residue

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37427 mRNA. Translation: AAC52503.2.
AJ537598 Genomic DNA. Translation: CAD61276.1.
AJ537598 Genomic DNA. Translation: CAD61277.1.
X82679 mRNA. Translation: CAA57996.1.
L24896 mRNA. Translation: AAA41842.2.
PIRiJC4332.
RefSeqiNP_001034938.1. NM_001039849.2.
NP_058861.3. NM_017165.2. [P36970-1]
UniGeneiRn.3647.

Genome annotation databases

GeneIDi29328.
KEGGirno:29328.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37427 mRNA. Translation: AAC52503.2.
AJ537598 Genomic DNA. Translation: CAD61276.1.
AJ537598 Genomic DNA. Translation: CAD61277.1.
X82679 mRNA. Translation: CAA57996.1.
L24896 mRNA. Translation: AAA41842.2.
PIRiJC4332.
RefSeqiNP_001034938.1. NM_001039849.2.
NP_058861.3. NM_017165.2. [P36970-1]
UniGeneiRn.3647.

3D structure databases

ProteinModelPortaliP36970.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018691.

Protein family/group databases

PeroxiBasei3733. RnoGPx04-A.
3812. RnoGPx04-B.

PTM databases

SwissPalmiP36970.

Proteomic databases

PaxDbiP36970.
PRIDEiP36970.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29328.
KEGGirno:29328.

Organism-specific databases

CTDi2879.
RGDi69226. Gpx4.

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
HOGENOMiHOG000277054.
HOVERGENiHBG004333.
KOiK05361.
PhylomeDBiP36970.

Enzyme and pathway databases

BRENDAi1.11.1.12. 5301.

Miscellaneous databases

NextBioi608793.

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. "Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites."
    Pushpa-Rekha T.R., Burdsall A.L., Oleksa L.M., Chisolm G.M., Driscoll D.M.
    J. Biol. Chem. 270:26993-26999(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "Distinct promoters determine alternative transcription of gpx-4 into PHGPx variants."
    Maiorino M., Scapin M., Ursini F., Biasolo M., Bosello V., Flohe L.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
  3. "Molecular cloning and functional expression of a cDNA for rat phospholipid hydroperoxide glutathione peroxidase: 3'-untranslated region of the gene is necessary for functional expression."
    Imai H., Sumi D., Hanamoto A., Arai M., Sugiyama A., Chiba N., Kuchino Y., Nakagawa Y.
    J. Biochem. 118:1061-1067(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-197.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Rat liver phospholipid hydroperoxide glutathione peroxidase."
    Sunde R.A., Dyer J.A., Moran T.V., Evenson J.K.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-197.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "Phospholipid hydroperoxide glutathione peroxidase of rat testis. Gonadotropin dependence and immunocytochemical identification."
    Roveri A., Casasco A., Maiorino M., Dalan P., Calligaro A., Ursini F.
    J. Biol. Chem. 267:6142-6146(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION.
    Tissue: Testis.
  6. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
    Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
    Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPX41_RAT
AccessioniPrimary (citable) accession number: P36970
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 26, 2008
Last modified: May 11, 2016
This is version 130 of the entry and version 3 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.