Glutathione peroxidase 3 precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P22352 (GPX3_HUMAN)

Last modified November 25, 2008. Version 96. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glutathione peroxidase 3
    EC=1.11.1.9
Alternative name(s):
    GSHPx-3
      Short name=GPx-3
    Extracellular glutathione peroxidase
    Plasma glutathione peroxidase
    GSHPx-P
      Short name=GPx-P

Gene names

Name:	GPX3
Synonyms:	GPXP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 + H(2)O(2) = glutathione disulfide + 2 H(2)O.
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.

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Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism Selenocysteine
Domain	Signal
Ligand	Selenium
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein homotetramerization Inferred from direct assay. Source: UniProtKB response to lipid hydroperoxide Traceable author statement. Source: UniProtKB
Cellular component	extracellular space Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	glutathione peroxidase activity Ref.7 Inferred from direct assay. Source: UniProtKB selenium binding Inferred from direct assay. Source: UniProtKB transcription factor binding Ref.3 Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Chain

21 – 226

206

Glutathione peroxidase 3

PRO_0000013062

Sites

Active site

Amino acid modifications

Non-standard residue

Selenocysteine

Natural variations

Natural variant

128

F → L

VAR_020943

Secondary structure

226

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P22352-1 [UniParc].

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

226

25,552

        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

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References

	« Hide 'large scale' referencesShow '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: 2229017] [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: 1339300] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"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: 8056346] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lymphocyte.
[4]	"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: 10970826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-128.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Duodenum, Lung and Pancreas.
[7]	"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: 1897960] [Abstract] Cited for: PROTEIN SEQUENCE OF 107-138 AND 148-175, CHARACTERIZATION.
+	Additional computationally mapped references.

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Web resources

Wikipedia

Glutathione peroxidase entry

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Cross-references

Sequence databases

D00632 mRNA. Translation: BAA00525.1.
X58295 mRNA. Translation: CAA41228.1.
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.
BC013601 mRNA. Translation: AAH13601.1.
BC035841 mRNA. Translation: AAH35841.1.
BC050378 mRNA. Translation: AAH50378.2.

PIR

JQ0476. I53822.

RefSeq

NP_002075.2.

UniGene

Hs.386793
Hs.663430

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2R37	X-ray	1.85	A/B	25-223	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

3602. HsGPx03.

Polymorphism databases

NIEHS-SNPs

Search...

2-D gel databases

SWISS-2DPAGE

P22352.

REPRODUCTION-2DPAGE

IPI00026199.

Genome annotation databases

Ensembl

ENSG00000211445. Homo sapiens. [Contig view]

GeneID

2878.

KEGG

hsa:2878.

Organism-specific databases

HGNC

HGNC:4555. GPX3.

MIM

138321. gene.

PharmGKB

PA28951.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P22352.

HOVERGEN

P22352.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-9873.

Gene expression databases

CleanEx

HS_GPX3.

GermOnline

ENSG00000211445. Homo sapiens.

Family and domain databases

InterPro

IPR000889. Glut_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR11592. Glut_peroxidase. 1 hit.

Pfam

PF00255. GSHPx. 1 hit.
[Graphical view]

PIRSF

PIRSF000303. Glutathion_perox. 1 hit.

PRINTS

PR01011. GLUTPROXDASE.

PROSITE

PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

11363.

SOURCE

Search...

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Entry information

Entry name

GPX3_HUMAN

Accession

Primary (citable) accession number: P22352
Secondary accession number(s): O43787

Q9UEL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 26, 2008
Last modified:	November 25, 2008
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 5

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Polymorphism databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents