Glutathione peroxidase 2 - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Glutathione peroxidase 2
    EC=1.11.1.9
Alternative name(s):
    GSHPx-2
      Short name=GPx-2
    Glutathione peroxidase-gastrointestinal
    GSHPx-GI
    Glutathione peroxidase-related protein 2
    Gastrointestinal glutathione peroxidase
    GPRP

Gene names

Name:

GPX2

Organism

Homo sapiens (Human) [Complete proteome]

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	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors.
Catalytic activity	2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm. Note: Mainly cytoplasmic.
Tissue specificity	Mostly in liver and gastrointestinal tract, not found in heart or kidney.
Sequence similarities	Belongs to the glutathione peroxidase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism Selenocysteine
Ligand	Selenium
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Ref.2 Traceable author statement. Source: ProtInc
Molecular function	electron carrier activity Ref.2 Traceable author statement. Source: UniProtKB glutathione peroxidase activity Ref.2 Traceable author statement. Source: ProtInc selenium binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 190

190

Glutathione peroxidase 2

PRO_0000066619

Sites

Active site

40

1

Amino acid modifications

Non-standard residue

40

1

Selenocysteine

Natural variations

Natural variant

37

1

A → L Requires 2 nucleotide substitutions. Ref.3

VAR_003615

Natural variant

126

1

P → L: dbSNP rs17881652. Ref.4

VAR_020916

Natural variant

146

1

R → C: dbSNP rs17880492. Ref.4

VAR_020917

Natural variant

176

1

I → M

VAR_003616

Experimental info

Sequence conflict

37

1

A → R in CAB43534. Ref.1

Sequence conflict

77

1

C → S in CAB43534. Ref.1

Secondary structure

1

.

190

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P18283-1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: FC8C4E69C4DE83A0
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FASTA

190

21,954

        10         20         30         40         50         60 
MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL NELQCRFPRR 

        70         80         90        100        110        120 
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK 

       130        140        150        160        170        180 
DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP 

       190 
DIKRLLKVAI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human cDNA sequence of a novel glutathione peroxidase-related protein." Akasaka M., Mizoguchi J., Takahashi K. Nucleic Acids Res. 18:4619-4619(1990) [PubMed: 2388849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI." Chu F.-F., Doroshow J.H., Esworthy R.S. J. Biol. Chem. 268:2571-2576(1993) [PubMed: 8428933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Liver.
[3]	"Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents." Kelner M.J., Bagnell R.D., Montoya M.A., Lanham K.A. Gene 248:109-116(2000) [PubMed: 10806356] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-37.
[4]	NIEHS SNPs program Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-126 AND CYS-146.
[5]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain, Prostate and Urinary bladder.
[7]	"Crystal structure of the selenocysteine to cysteine mutant of human glutathionine peroxidase 2 (GPX2)." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4-188.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

X53463 mRNA. Translation: CAB43534.1.
X68314 mRNA. Translation: CAA48394.1.
AF199441 Genomic DNA. Translation: AAF74026.1.
AY785560 Genomic DNA. Translation: AAV31780.1.
AL139022 Genomic DNA. No translation available.
BC005277 mRNA. Translation: AAH05277.1.
BC016756 mRNA. Translation: AAH16756.1.
BC022820 mRNA. Translation: AAH22820.2.
BC067221 mRNA. Translation: AAH67221.1.

IPI

IPI00298176.

PIR

A45207.

RefSeq

NP_002074.2.

UniGene

Hs.2704

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HE3	X-ray	2.10	A	4-188	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

3601. HsGPx02.

Proteomic databases

PRIDE

P18283.

Genome annotation databases

Ensembl

ENSG00000176153. Homo sapiens. [Contig view]

GeneID

2877.

KEGG

hsa:2877.

Organism-specific databases

GeneCards

GC14M064475.

H-InvDB

HIX0037716.

HGNC

HGNC:4554. GPX2.

MIM

138319. gene.

PharmGKB

PA28950.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P18283.

HOVERGEN

P18283.

OMA

P18283. GEPFRRY.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-9901.

BRENDA

1.11.1.9. 247.

Gene expression databases

ArrayExpress

P18283.

Bgee

P18283.

CleanEx

HS_GPX2.

GermOnline

ENSG00000176153. Homo sapiens.

Family and domain databases

InterPro

IPR000889. Glutathione_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

11359.

SOURCE

Search...

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Entry information

Entry name

GPX2_HUMAN

Accession

Primary (citable) accession number: P18283
Secondary accession number(s): Q6PJ52, Q8WWI7, Q9NRP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	February 26, 2008
Last modified:	July 7, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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