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UniProtKB/Swiss-Prot entry P18283


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPX2_HUMAN
Primary accession number P18283
Secondary accession numbers Q6PJ52 Q8WWI7 Q9NRP9
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on February 26, 2008 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Glutathione peroxidase 2
Synonyms EC 1.11.1.9
GSHPx-2
GPx-2
Glutathione peroxidase-gastrointestinal
GSHPx-GI
Glutathione peroxidase-related protein 2
Gastrointestinal glutathione peroxidase
GPRP
Gene name
Name: GPX2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2388849 [NCBI, ExPASy, EBI, Israel, Japan]
Akasaka M., Mizoguchi J., Takahashi K.;
"A human cDNA sequence of a novel glutathione peroxidase-related protein.";
Nucleic Acids Res. 18:4619-4619(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Liver;
PubMed=8428933 [NCBI, ExPASy, EBI, Israel, Japan]
Chu F.-F., Doroshow J.H., Esworthy R.S.;
"Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI.";
J. Biol. Chem. 268:2571-2576(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-37.
DOI=10.1016/S0378-1119(00)00137-2; PubMed=10806356 [NCBI, ExPASy, EBI, Israel, Japan]
Kelner M.J., Bagnell R.D., Montoya M.A., Lanham K.A.;
"Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents.";
Gene 248:109-116(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-126 AND CYS-146.
Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Prostate, and Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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: Homotetramer.
  • SUBCELLULAR LOCATION: Cytoplasm. Note=Mainly cytoplasmic.
  • TISSUE SPECIFICITY: Mostly in liver and gastrointestinal tract, not found in heart or kidney.
  • SIMILARITY: Belongs to the glutathione peroxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X53463; CAB43534.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68314; CAA48394.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF199441; AAF74026.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY785560; AAV31780.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005277; AAH05277.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016756; AAH16756.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022820; AAH22820.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067221; AAH67221.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45207; A45207.
RefSeq NP_002074.2; -.
UniGene Hs.2704
3D structure databases
PDB
2HE3; X-ray; 2.10 A; A=2-188.[ExPASy / RCSB / EBI]
PDBsum 2HE3; -.
ModBase P18283.
Protein family/group databases
PeroxiBase 3601; HsGPx02.
Enzyme and pathway databases
BioCyc MetaCyc:MON-9901; -.
Polymorphism databases
NIEHS-SNPs GPX2.
Organism-specific databases
H-InvDB HIX0037716; -.
HGNC HGNC:4554; GPX2.
GenAtlas GPX2.
MIM 138319; gene. [NCBI / EBI]
PharmGKB PA28950; -.
GeneCards P18283.
Gene expression databases
ArrayExpress P18283; -.
CleanEx HS_GPX2; -.
GermOnline ENSG00000176153; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0004602; Molecular function: glutathione peroxidase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PANTHER PTHR11592; Glut_peroxidase; 1.
Pfam PF00255; GSHPx; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000303; Glutathion_perox; 1.
PRINTS PR01011; GLUTPROXDASE.
PROSITE PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P18283.
Genome annotation databases
Ensembl ENSG00000176153; Homo sapiens. [Contig view]
GeneID 2877; -.
KEGG hsa:2877; -.
Phylogenomic databases
HOGENOM P18283; -.
HOVERGEN P18283; -.
Other
DrugBank DB00143; Glutathione.
LinkHub P18283; -.
SOURCE GPX2; Homo sapiens.
ProtoNet P18283.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Oxidoreductase; Peroxidase; Polymorphism; Selenium; Selenocysteine.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   190  190     Glutathione peroxidase 2. PRO_0000066619
ACT_SITE   40    40         
NON_STD   40    40        Selenocysteine. 
VARIANT   37    37  1     A -> L (requires 2 nucleotide substitutions). VAR_003615 
VARIANT   126   126  1     P -> L (in dbSNP:rs17881652 [NCBI]). VAR_020916 
VARIANT   146   146  1     R -> C (in dbSNP:rs17880492 [NCBI]). VAR_020917 
VARIANT   176   176  1     I -> M. VAR_003616 
CONFLICT   37    37        A -> R (in Ref. 1; CAB43534). 
CONFLICT   77    77        C -> S (in Ref. 1; CAB43534). 
Sequence information
Length: 190 AA [This is the length of the unprocessed precursor] Molecular weight: 21954 Da [This is the MW of the unprocessed precursor] CRC64: FC8C4E69C4DE83A0 [This is a checksum on the sequence]
        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 

P18283 in FASTA format

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