P18283 (GPX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione peroxidase 2
Short name=GPx-2
Short name=GSHPx-2
EC=1.11.1.9

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

Gene names

Name:

GPX2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism Selenocysteine
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	interaction with symbiont Inferred from electronic annotation. Source: Compara negative regulation of inflammatory response to antigenic stimulus Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: InterPro response to symbiotic bacterium Inferred from electronic annotation. Source: Compara temperature homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	electron carrier activity Traceable author statement Ref.2. Source: UniProtKB glutathione peroxidase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

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. Ref.4
Corresponds to variant rs17881652 [ dbSNP | Ensembl ].

VAR_020916

Natural variant

146

1

R → C. Ref.4
Corresponds to variant rs17880492 [ dbSNP | Ensembl ].

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

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190

Helix Strand Turn

Details...

Helix

8 – 10

3

Beta strand

12 – 15

4

Beta strand

20 – 22

3

Helix

23 – 26

4

Beta strand

29 – 36

8

Helix

43 – 56

14

Turn

58 – 60

3

Beta strand

61 – 68

8

Helix

79 – 81

3

Helix

82 – 88

7

Beta strand

98 – 102

5

Beta strand

105 – 109

5

Helix

114 – 122

9

Helix

137 – 139

3

Beta strand

156 – 159

4

Beta strand

165 – 169

5

Helix

175 – 178

4

Helix

179 – 186

8

Sequences

	Sequence		Length	Mass (Da)
	P18283 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: FC8C4E69C4DE83A0	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Prostate and Urinary bladder.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Crystal structure of the selenocysteine to cysteine mutant of human glutathione 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.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_002083.3.

UniGene

Hs.2704.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P18283.

ModBase

Search...

Protein-protein interaction databases

IntAct

P18283. 3 interactions.

STRING

9606.ENSP00000374265.

Protein family/group databases

PeroxiBase

3601. HsGPx02.

PTM databases

PhosphoSite

P18283.

Polymorphism databases

DMDM

172046064.

Proteomic databases

PaxDb

P18283.

PRIDE

P18283.

Protocols and materials databases

DNASU

2877.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389614; ENSP00000374265; ENSG00000176153.

GeneID

2877.

KEGG

hsa:2877.

UCSC

uc021ruq.1. human.

Organism-specific databases

CTD

2877.

GeneCards

GC14M065405.

H-InvDB

HIX0037716.

HGNC

HGNC:4554. GPX2.

HPA

HPA003545.

MIM

138319. gene.

neXtProt

NX_P18283.

PharmGKB

PA28950.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0386.

HOGENOM

HOG000277055.

HOVERGEN

HBG004333.

InParanoid

P18283.

KO

K00432.

OMA

IYDIAVE.

OrthoDB

EOG4SBF08.

PhylomeDB

P18283.

Enzyme and pathway databases

BioCyc

MetaCyc:HS11006-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P18283.

Gene expression databases

ArrayExpress

P18283.

Bgee

P18283.

CleanEx

HS_GPX2.

Genevestigator

P18283.

GermOnline

ENSG00000176153. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PANTHER

PTHR11592. PTHR11592. 1 hit.

Pfam

PF00255. GSHPx. 1 hit.
[Graphical view]

PIRSF

PIRSF000303. Glutathion_perox. 1 hit.

PRINTS

PR01011. GLUTPROXDASE.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

P18283.

GenomeRNAi

2877.

NextBio

11359.

SOURCE

Search...

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:	May 1, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.