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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731

GO - Molecular functioni

  1. glutathione peroxidase activity Source: UniProtKB
  2. selenium binding Source: UniProtKB
  3. transcription factor binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciMetaCyc:HS08224-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiREACT_264249. 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
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:4555. GPX3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28951.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX3.
DMDMi172046796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 226206Glutathione peroxidase 3PRO_0000013062Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiP22352.
PaxDbiP22352.
PRIDEiP22352.

2D gel databases

REPRODUCTION-2DPAGEIPI00026199.
SWISS-2DPAGEP22352.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

BgeeiP22352.
CleanExiHS_GPX3.
ExpressionAtlasiP22352. baseline and differential.
GenevestigatoriP22352.

Organism-specific databases

HPAiCAB069456.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109136. 2 interactions.
IntActiP22352. 7 interactions.
STRINGi9606.ENSP00000373477.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 423Combined sources
Beta strandi44 – 474Combined sources
Beta strandi53 – 553Combined sources
Helixi56 – 594Combined sources
Beta strandi62 – 698Combined sources
Beta strandi71 – 733Combined sources
Turni74 – 774Combined sources
Helixi78 – 8912Combined sources
Helixi90 – 923Combined sources
Beta strandi94 – 1007Combined sources
Helixi112 – 1143Combined sources
Helixi115 – 1217Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi140 – 1423Combined sources
Helixi147 – 1559Combined sources
Helixi166 – 1683Combined sources
Beta strandi185 – 1884Combined sources
Beta strandi194 – 1985Combined sources
Helixi204 – 22320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R37X-ray1.85A/B25-223[»]
ProteinModelPortaliP22352.
SMRiP22352. Positions 36-223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22352.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP22352.
KOiK00432.
OMAiIMRWHHR.
OrthoDBiEOG7KQ23C.
PhylomeDBiP22352.
TreeFamiTF105318.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281F → L.1 Publication
Corresponds to variant rs8177445 [ dbSNP | Ensembl ].
VAR_020943

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei73 – 731Selenocysteine1 Publication

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_002075.2. NM_002084.3.
UniGeneiHs.386793.

Genome annotation databases

EnsembliENST00000388825; ENSP00000373477; ENSG00000211445.
GeneIDi2878.
KEGGihsa:2878.
UCSCiuc021yga.1. human.

Polymorphism and mutation databases

BioMutaiGPX3.

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_002075.2. NM_002084.3.
UniGeneiHs.386793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R37X-ray1.85A/B25-223[»]
ProteinModelPortaliP22352.
SMRiP22352. Positions 36-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109136. 2 interactions.
IntActiP22352. 7 interactions.
STRINGi9606.ENSP00000373477.

Chemistry

DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3602. HsGPx03.

Polymorphism and mutation databases

BioMutaiGPX3.
DMDMi172046796.

2D gel databases

REPRODUCTION-2DPAGEIPI00026199.
SWISS-2DPAGEP22352.

Proteomic databases

MaxQBiP22352.
PaxDbiP22352.
PRIDEiP22352.

Protocols and materials databases

DNASUi2878.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388825; ENSP00000373477; ENSG00000211445.
GeneIDi2878.
KEGGihsa:2878.
UCSCiuc021yga.1. human.

Organism-specific databases

CTDi2878.
GeneCardsiGC05P150381.
H-InvDBHIX0024803.
HGNCiHGNC:4555. GPX3.
HPAiCAB069456.
MIMi138321. gene.
neXtProtiNX_P22352.
PharmGKBiPA28951.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP22352.
KOiK00432.
OMAiIMRWHHR.
OrthoDBiEOG7KQ23C.
PhylomeDBiP22352.
TreeFamiTF105318.

Enzyme and pathway databases

BioCyciMetaCyc:HS08224-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiREACT_264249. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiGPX3. human.
EvolutionaryTraceiP22352.
GeneWikiiGPX3.
GenomeRNAii2878.
NextBioi11363.
PROiP22352.
SOURCEiSearch...

Gene expression databases

BgeeiP22352.
CleanExiHS_GPX3.
ExpressionAtlasiP22352. baseline and differential.
GenevestigatoriP22352.

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. "Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences."
    Takahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J., Koyama J.
    J. Biochem. 108:145-148(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Fetal liver and Placenta.
  2. "Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents."
    Chu F.-F., Esworthy R.S., Doroshow J.H., Doan K., Liu X.F.
    Blood 79:3233-3238(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. Chu F.-F.
    Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 73.
  4. "The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32."
    Yoshimura S., Suemizu H., Taniguchi Y., Arimori K., Kawabe N., Moriuchi T.
    Gene 145:293-297(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lymphocyte.
  5. "Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke."
    Comhair S.A.A., Thomassen M.J., Erzurum S.C.
    Am. J. Respir. Cell Mol. Biol. 23:350-354(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. NIEHS SNPs program
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-128.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Duodenum, Lung and Pancreas.
  9. "Characterization and partial amino acid sequence of human plasma glutathione peroxidase."
    Esworthy R.S., Chu F.-F., Paxton R.J., Akman S., Doroshow J.H.
    Arch. Biochem. Biophys. 286:330-336(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 107-138 AND 148-175, CHARACTERIZATION.
  10. "Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)."
    Structural genomics consortium (SGC)
    Submitted (SEP-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 25-223.

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: April 29, 2015
This is version 161 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

External Data

Dasty 3

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 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.