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Protein

Glutathione peroxidase 3

Gene

GPX3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Active sitei731

GO - Molecular functioni

  • glutathione peroxidase activity Source: UniProtKB
  • selenium binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • hydrogen peroxide catabolic process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • response to lipid hydroperoxide Source: UniProtKB
  • response to reactive oxygen species Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciMetaCyc:HS08224-MONOMER.
ZFISH:HS08224-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei3602. HsGPx03.

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):
Extracellular glutathione peroxidase
Plasma glutathione peroxidase
Short name:
GPx-P
Short name:
GSHPx-P
Gene namesi
Name:GPX3
Synonyms:GPXP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:4555. GPX3.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi2878.
OpenTargetsiENSG00000211445.
PharmGKBiPA28951.

Chemistry databases

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX3.
DMDMi172046796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001306221 – 226Glutathione peroxidase 3Add BLAST206

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

EPDiP22352.
MaxQBiP22352.
PaxDbiP22352.
PeptideAtlasiP22352.
PRIDEiP22352.

2D gel databases

REPRODUCTION-2DPAGEIPI00026199.
SWISS-2DPAGEP22352.

PTM databases

iPTMnetiP22352.
PhosphoSitePlusiP22352.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

BgeeiENSG00000211445.
CleanExiHS_GPX3.
ExpressionAtlasiP22352. baseline and differential.
GenevisibleiP22352. HS.

Organism-specific databases

HPAiCAB069456.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
UBQLN1Q9UMX0-23EBI-2832946,EBI-10173939

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109136. 2 interactors.
IntActiP22352. 7 interactors.
STRINGi9606.ENSP00000373477.

Structurei

Secondary structure

1226
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 42Combined sources3
Beta strandi44 – 47Combined sources4
Beta strandi53 – 55Combined sources3
Helixi56 – 59Combined sources4
Beta strandi62 – 69Combined sources8
Beta strandi71 – 73Combined sources3
Turni74 – 77Combined sources4
Helixi78 – 89Combined sources12
Helixi90 – 92Combined sources3
Beta strandi94 – 100Combined sources7
Helixi112 – 114Combined sources3
Helixi115 – 121Combined sources7
Beta strandi131 – 135Combined sources5
Beta strandi140 – 142Combined sources3
Helixi147 – 155Combined sources9
Helixi166 – 168Combined sources3
Beta strandi185 – 188Combined sources4
Beta strandi194 – 198Combined sources5
Helixi204 – 223Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R37X-ray1.85A/B25-223[»]
ProteinModelPortaliP22352.
SMRiP22352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22352.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP22352.
KOiK00432.
OMAiIMRWHHR.
OrthoDBiEOG091G10LN.
PhylomeDBiP22352.
TreeFamiTF105318.

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.

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

P22352-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLLQASCL LSLLLAGFVS QSRGQEKSKM DCHGGISGTI YEYGALTIDG
60 70 80 90 100
EEYIPFKQYA GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP
110 120 130 140 150
CNQFGKQEPG ENSEILPTLK YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT
160 170 180 190 200
FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR WNFEKFLVGP DGIPIMRWHH
210 220
RTTVSNVKMD ILSYMRRQAA LGVKRK
Length:226
Mass (Da):25,552
Last modified:February 26, 2008 - v2
Checksum:iA839E87A5CDB51A9
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020943128F → L.1 PublicationCorresponds to variant rs8177445dbSNPEnsembl.1

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei73Selenocysteine1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00632 mRNA. Translation: BAA00525.1.
X58295 mRNA. Translation: CAA41228.2.
D16360 Genomic DNA. Translation: BAA03862.1.
D16361 Genomic DNA. Translation: BAA03863.2.
D16362 Genomic DNA. Translation: BAA03864.1.
AF217787 mRNA. Translation: AAF43005.1.
AY310878 Genomic DNA. Translation: AAP50261.1.
AC008641 Genomic DNA. No translation available.
BC013601 mRNA. Translation: AAH13601.1.
BC035841 mRNA. Translation: AAH35841.1.
BC050378 mRNA. Translation: AAH50378.2.
CCDSiCCDS43389.1.
PIRiI53822. JQ0476.
RefSeqiNP_001316719.1. NM_001329790.1.
NP_002075.2. NM_002084.4.
UniGeneiHs.386793.

Genome annotation databases

EnsembliENST00000388825; ENSP00000373477; ENSG00000211445.
GeneIDi2878.
KEGGihsa:2878.
UCSCiuc021yga.2. human.

Keywords - Coding sequence diversityi

Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glutathione peroxidase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00632 mRNA. Translation: BAA00525.1.
X58295 mRNA. Translation: CAA41228.2.
D16360 Genomic DNA. Translation: BAA03862.1.
D16361 Genomic DNA. Translation: BAA03863.2.
D16362 Genomic DNA. Translation: BAA03864.1.
AF217787 mRNA. Translation: AAF43005.1.
AY310878 Genomic DNA. Translation: AAP50261.1.
AC008641 Genomic DNA. No translation available.
BC013601 mRNA. Translation: AAH13601.1.
BC035841 mRNA. Translation: AAH35841.1.
BC050378 mRNA. Translation: AAH50378.2.
CCDSiCCDS43389.1.
PIRiI53822. JQ0476.
RefSeqiNP_001316719.1. NM_001329790.1.
NP_002075.2. NM_002084.4.
UniGeneiHs.386793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R37X-ray1.85A/B25-223[»]
ProteinModelPortaliP22352.
SMRiP22352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109136. 2 interactors.
IntActiP22352. 7 interactors.
STRINGi9606.ENSP00000373477.

Chemistry databases

DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3602. HsGPx03.

PTM databases

iPTMnetiP22352.
PhosphoSitePlusiP22352.

Polymorphism and mutation databases

BioMutaiGPX3.
DMDMi172046796.

2D gel databases

REPRODUCTION-2DPAGEIPI00026199.
SWISS-2DPAGEP22352.

Proteomic databases

EPDiP22352.
MaxQBiP22352.
PaxDbiP22352.
PeptideAtlasiP22352.
PRIDEiP22352.

Protocols and materials databases

DNASUi2878.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388825; ENSP00000373477; ENSG00000211445.
GeneIDi2878.
KEGGihsa:2878.
UCSCiuc021yga.2. human.

Organism-specific databases

CTDi2878.
DisGeNETi2878.
GeneCardsiGPX3.
H-InvDBHIX0024803.
HGNCiHGNC:4555. GPX3.
HPAiCAB069456.
MIMi138321. gene.
neXtProtiNX_P22352.
OpenTargetsiENSG00000211445.
PharmGKBiPA28951.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP22352.
KOiK00432.
OMAiIMRWHHR.
OrthoDBiEOG091G10LN.
PhylomeDBiP22352.
TreeFamiTF105318.

Enzyme and pathway databases

BioCyciMetaCyc:HS08224-MONOMER.
ZFISH:HS08224-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiGPX3. human.
EvolutionaryTraceiP22352.
GeneWikiiGPX3.
GenomeRNAii2878.
PROiP22352.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000211445.
CleanExiHS_GPX3.
ExpressionAtlasiP22352. baseline and differential.
GenevisibleiP22352. HS.

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 nameiGPX3_HUMAN
AccessioniPrimary (citable) accession number: P22352
Secondary accession number(s): O43787
, Q86W78, Q9NZ74, Q9UEL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 26, 2008
Last modified: November 30, 2016
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.