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Protein

Glutathione peroxidase 1

Gene

GPX1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protects the hemoglobin in erythrocytes from oxidative breakdown.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei521
Sitei52Subject to oxidation and hydroselenide loss to dehydroalanineBy similarity1

GO - Molecular functioni

  • glutathione peroxidase activity Source: ParkinsonsUK-UCL

GO - Biological processi

  • glutathione metabolic process Source: ParkinsonsUK-UCL
  • hydrogen peroxide catabolic process Source: ParkinsonsUK-UCL
  • positive regulation of fibril organization Source: ParkinsonsUK-UCL
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.9. 908.

Protein family/group databases

PeroxiBasei3635. BtGPx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 1 (EC:1.11.1.9)
Short name:
GPx-1
Short name:
GSHPx-1
Alternative name(s):
Cellular glutathione peroxidase
Gene namesi
Name:GPX1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000666081 – 205Glutathione peroxidase 1Add BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37PhosphoserineBy similarity1
Modified residuei91N6-acetyllysine; alternateBy similarity1
Modified residuei91N6-succinyllysine; alternateBy similarity1
Modified residuei117N6-acetyllysine; alternateBy similarity1
Modified residuei117N6-succinyllysine; alternateBy similarity1
Glycosylationi117N-linked (Glc) (glycation); in vitro1
Modified residuei124N6-acetyllysineBy similarity1
Modified residuei151N6-acetyllysine; alternateBy similarity1
Modified residuei151N6-succinyllysine; alternateBy similarity1
Modified residuei200PhosphoserineBy similarity1
Modified residuei204PhosphoserineBy similarity1

Post-translational modificationi

During periods of oxidative stress, Sec-52 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei41Not glycated1
Sitei91Not glycated1
Sitei100Not glycated1
Sitei124Not glycated1
Sitei151Not glycated1
Sitei169Not glycated1

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Phosphoprotein

Proteomic databases

PeptideAtlasiP00435.
PRIDEiP00435.

Interactioni

Subunit structurei

Homotetramer. Interacts with MIEN1.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 21Combined sources3
Helixi35 – 38Combined sources4
Beta strandi41 – 48Combined sources8
Helixi55 – 69Combined sources15
Helixi70 – 72Combined sources3
Beta strandi74 – 80Combined sources7
Turni83 – 86Combined sources4
Helixi92 – 94Combined sources3
Helixi95 – 101Combined sources7
Beta strandi111 – 115Combined sources5
Beta strandi119 – 122Combined sources4
Helixi127 – 135Combined sources9
Helixi150 – 152Combined sources3
Beta strandi155 – 157Combined sources3
Beta strandi169 – 172Combined sources4
Beta strandi178 – 182Combined sources5
Helixi188 – 191Combined sources4
Helixi192 – 199Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GP1X-ray2.00A/B8-205[»]
ProteinModelPortaliP00435.
SMRiP00435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00435.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Phylogenomic databases

HOVERGENiHBG004333.
InParanoidiP00435.
KOiK00432.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
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.

P00435-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCAAQRSAAA LAAAAPRTVY AFSARPLAGG EPFNLSSLRG KVLLIENVAS
60 70 80 90 100
LUGTTVRDYT QMNDLQRRLG PRGLVVLGFP CNQFGHQENA KNEEILNCLK
110 120 130 140 150
YVRPGGGFEP NFMLFEKCEV NGEKAHPLFA FLREVLPTPS DDATALMTDP
160 170 180 190 200
KFITWSPVCR NDVSWNFEKF LVGPDGVPVR RYSRRFLTID IEPDIETLLS

QGASA
Length:205
Mass (Da):22,659
Last modified:February 26, 2008 - v3
Checksum:i7CBDF736CAAA92F6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96L → P in AAI49309 (Ref. 2) Curated1

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei52Selenocysteine1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13684 mRNA. Translation: CAB40806.1.
BC149308 mRNA. Translation: AAI49309.1.
PIRiS04872. OPBOE.
RefSeqiNP_776501.1. NM_174076.3.
UniGeneiBt.4317.

Genome annotation databases

GeneIDi281209.
KEGGibta:281209.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13684 mRNA. Translation: CAB40806.1.
BC149308 mRNA. Translation: AAI49309.1.
PIRiS04872. OPBOE.
RefSeqiNP_776501.1. NM_174076.3.
UniGeneiBt.4317.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GP1X-ray2.00A/B8-205[»]
ProteinModelPortaliP00435.
SMRiP00435.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei3635. BtGPx01.

Proteomic databases

PeptideAtlasiP00435.
PRIDEiP00435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281209.
KEGGibta:281209.

Organism-specific databases

CTDi2876.

Phylogenomic databases

HOVERGENiHBG004333.
InParanoidiP00435.
KOiK00432.

Enzyme and pathway databases

BRENDAi1.11.1.9. 908.

Miscellaneous databases

EvolutionaryTraceiP00435.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
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...

Entry informationi

Entry nameiGPX1_BOVIN
AccessioniPrimary (citable) accession number: P00435
Secondary accession number(s): A6QPG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 133 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.