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P22352 (GPX3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione peroxidase 3

Short name=GPx-3
Short name=GSHPx-3
EC=1.11.1.9
Alternative name(s):
Extracellular glutathione peroxidase
Plasma glutathione peroxidase
Short name=GPx-P
Short name=GSHPx-P
Gene names
Name:GPX3
Synonyms:GPXP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.

Catalytic activity

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Subunit structure

Homotetramer.

Subcellular location

Secreted.

Tissue specificity

Secreted in plasma.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the glutathione peroxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 226206Glutathione peroxidase 3
PRO_0000013062

Sites

Active site731

Amino acid modifications

Non-standard residue731Selenocysteine Ref.1

Natural variations

Natural variant1281F → L. Ref.6
Corresponds to variant rs8177445 [ dbSNP | Ensembl ].
VAR_020943

Secondary structure

.................................. 226
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22352 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: A839E87A5CDB51A9

FASTA22625,552
        10         20         30         40         50         60 
MARLLQASCL LSLLLAGFVS QSRGQEKSKM DCHGGISGTI YEYGALTIDG EEYIPFKQYA 

        70         80         90        100        110        120 
GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP CNQFGKQEPG ENSEILPTLK 

       130        140        150        160        170        180 
YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR 

       190        200        210        220 
WNFEKFLVGP DGIPIMRWHH RTTVSNVKMD ILSYMRRQAA LGVKRK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Glutathione peroxidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS43389.1.
PIRJQ0476. I53822.
RefSeqNP_002075.2. NM_002084.3.
UniGeneHs.386793.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R37X-ray1.85A/B25-223[»]
ProteinModelPortalP22352.
SMRP22352. Positions 36-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109136. 1 interaction.
IntActP22352. 6 interactions.
STRING9606.ENSP00000373477.

Chemistry

DrugBankDB00143. Glutathione.

Protein family/group databases

PeroxiBase3602. HsGPx03.

Polymorphism databases

DMDM172046796.

2D gel databases

REPRODUCTION-2DPAGEIPI00026199.
SWISS-2DPAGEP22352.

Proteomic databases

MaxQBP22352.
PaxDbP22352.
PRIDEP22352.

Protocols and materials databases

DNASU2878.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000388825; ENSP00000373477; ENSG00000211445.
GeneID2878.
KEGGhsa:2878.
UCSCuc021yga.1. human.

Organism-specific databases

CTD2878.
GeneCardsGC05P150381.
H-InvDBHIX0024803.
HGNCHGNC:4555. GPX3.
MIM138321. gene.
neXtProtNX_P22352.
PharmGKBPA28951.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0386.
HOGENOMHOG000277055.
HOVERGENHBG004333.
InParanoidP22352.
KOK00432.
OMAWYHRTTV.
OrthoDBEOG7KQ23C.
PhylomeDBP22352.
TreeFamTF105318.

Enzyme and pathway databases

BioCycMetaCyc:HS08224-MONOMER.
ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP22352.
BgeeP22352.
CleanExHS_GPX3.
GenevestigatorP22352.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11592. PTHR11592. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPX3. human.
EvolutionaryTraceP22352.
GeneWikiGPX3.
GenomeRNAi2878.
NextBio11363.
PROP22352.
SOURCESearch...

Entry information

Entry nameGPX3_HUMAN
AccessionPrimary (citable) accession number: P22352
Secondary accession number(s): O43787 expand/collapse secondary AC list , Q86W78, Q9NZ74, Q9UEL1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 26, 2008
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM