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Glutathione peroxidase 2 (GPx-2) (GSHPx-2) (EC 1.11.1.9) (Gastrointestinal glutathione peroxidase) (Glutathione peroxidase-gastrointestinal) (GPx-GI) (GSHPx-GI) (Glutathione peroxidase-related protein 2) (GPRP-2)

 GPX2_HUMAN              Reviewed;         190 AA.
P18283; Q6PJ52; Q8WWI7; Q9NRP9;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 3.
23-MAY-2018, entry version 174.
RecName: Full=Glutathione peroxidase 2;
Short=GPx-2;
Short=GSHPx-2;
EC=1.11.1.9;
AltName: Full=Gastrointestinal glutathione peroxidase;
AltName: Full=Glutathione peroxidase-gastrointestinal;
Short=GPx-GI;
Short=GSHPx-GI;
AltName: Full=Glutathione peroxidase-related protein 2;
Short=GPRP-2;
Name=GPX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2388849; DOI=10.1093/nar/18.15.4619;
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;
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.
PubMed=10806356; DOI=10.1016/S0378-1119(00)00137-2;
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.
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
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.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Prostate, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4-188.
Structural genomics consortium (SGC);
"Crystal structure of the selenocysteine to cysteine mutant of human
glutathione peroxidase 2 (GPX2).";
Submitted (FEB-2009) to the PDB data bank.
-!- 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 + H(2)O(2) = glutathione
disulfide + 2 H(2)O.
-!- 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.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/gpx2/";
-----------------------------------------------------------------------
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EMBL; X53463; CAB43534.1; -; mRNA.
EMBL; X68314; CAA48394.1; -; mRNA.
EMBL; AF199441; AAF74026.1; -; Genomic_DNA.
EMBL; AY785560; AAV31780.1; -; Genomic_DNA.
EMBL; AL139022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005277; AAH05277.1; -; mRNA.
EMBL; BC016756; AAH16756.1; -; mRNA.
EMBL; BC022820; AAH22820.2; -; mRNA.
EMBL; BC067221; AAH67221.1; -; mRNA.
CCDS; CCDS41964.1; -.
PIR; A45207; A45207.
RefSeq; NP_002074.2; NM_002083.3.
UniGene; Hs.2704; -.
PDB; 2HE3; X-ray; 2.10 A; A=4-188.
PDBsum; 2HE3; -.
ProteinModelPortal; P18283; -.
SMR; P18283; -.
BioGrid; 109135; 3.
IntAct; P18283; 3.
STRING; 9606.ENSP00000374265; -.
DrugBank; DB00143; Glutathione.
PeroxiBase; 3601; HsGPx02.
iPTMnet; P18283; -.
PhosphoSitePlus; P18283; -.
BioMuta; GPX2; -.
DMDM; 172046064; -.
MaxQB; P18283; -.
PaxDb; P18283; -.
PeptideAtlas; P18283; -.
PRIDE; P18283; -.
DNASU; 2877; -.
Ensembl; ENST00000389614; ENSP00000374265; ENSG00000176153.
GeneID; 2877; -.
KEGG; hsa:2877; -.
UCSC; uc021ruq.3; human.
CTD; 2877; -.
DisGeNET; 2877; -.
EuPathDB; HostDB:ENSG00000176153.11; -.
GeneCards; GPX2; -.
H-InvDB; HIX0037716; -.
HGNC; HGNC:4554; GPX2.
HPA; HPA003545; -.
MIM; 138319; gene.
neXtProt; NX_P18283; -.
OpenTargets; ENSG00000176153; -.
PharmGKB; PA28950; -.
eggNOG; KOG1651; Eukaryota.
eggNOG; COG0386; LUCA.
GeneTree; ENSGT00760000119230; -.
HOGENOM; HOG000277055; -.
HOVERGEN; HBG004333; -.
InParanoid; P18283; -.
KO; K00432; -.
OMA; PFKRYSK; -.
OrthoDB; EOG091G10LN; -.
PhylomeDB; P18283; -.
TreeFam; TF105318; -.
BioCyc; MetaCyc:HS11006-MONOMER; -.
BRENDA; 1.11.1.9; 2681.
Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids.
Reactome; R-HSA-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
SABIO-RK; P18283; -.
EvolutionaryTrace; P18283; -.
GeneWiki; GPX2_(gene); -.
GenomeRNAi; 2877; -.
PRO; PR:P18283; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000176153; -.
CleanEx; HS_GPX2; -.
ExpressionAtlas; P18283; baseline and differential.
Genevisible; P18283; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
GO; GO:0004602; F:glutathione peroxidase activity; TAS:Reactome.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
CDD; cd00340; GSH_Peroxidase; 1.
InterPro; IPR000889; Glutathione_peroxidase.
InterPro; IPR029759; GPX_AS.
InterPro; IPR029760; GPX_CS.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR11592; PTHR11592; 1.
Pfam; PF00255; GSHPx; 1.
PIRSF; PIRSF000303; Glutathion_perox; 1.
PRINTS; PR01011; GLUTPROXDASE.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Oxidoreductase;
Peroxidase; Polymorphism; Reference proteome; Selenocysteine.
CHAIN 1 190 Glutathione peroxidase 2.
/FTId=PRO_0000066619.
ACT_SITE 40 40
NON_STD 40 40 Selenocysteine.
VARIANT 37 37 A -> L (requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:10806356}.
/FTId=VAR_003615.
VARIANT 126 126 P -> L (in dbSNP:rs17881652).
{ECO:0000269|Ref.4}.
/FTId=VAR_020916.
VARIANT 146 146 R -> C (in dbSNP:rs17880492).
{ECO:0000269|Ref.4}.
/FTId=VAR_020917.
VARIANT 176 176 I -> M.
/FTId=VAR_003616.
CONFLICT 37 37 A -> R (in Ref. 1; CAB43534).
{ECO:0000305}.
CONFLICT 77 77 C -> S (in Ref. 1; CAB43534).
{ECO:0000305}.
HELIX 8 10 {ECO:0000244|PDB:2HE3}.
STRAND 12 15 {ECO:0000244|PDB:2HE3}.
STRAND 20 22 {ECO:0000244|PDB:2HE3}.
HELIX 23 26 {ECO:0000244|PDB:2HE3}.
STRAND 29 36 {ECO:0000244|PDB:2HE3}.
HELIX 43 56 {ECO:0000244|PDB:2HE3}.
TURN 58 60 {ECO:0000244|PDB:2HE3}.
STRAND 61 68 {ECO:0000244|PDB:2HE3}.
HELIX 79 81 {ECO:0000244|PDB:2HE3}.
HELIX 82 88 {ECO:0000244|PDB:2HE3}.
STRAND 98 102 {ECO:0000244|PDB:2HE3}.
STRAND 105 109 {ECO:0000244|PDB:2HE3}.
HELIX 114 122 {ECO:0000244|PDB:2HE3}.
HELIX 137 139 {ECO:0000244|PDB:2HE3}.
STRAND 156 159 {ECO:0000244|PDB:2HE3}.
STRAND 165 169 {ECO:0000244|PDB:2HE3}.
HELIX 175 178 {ECO:0000244|PDB:2HE3}.
HELIX 179 186 {ECO:0000244|PDB:2HE3}.
SEQUENCE 190 AA; 21954 MW; FC8C4E69C4DE83A0 CRC64;
MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL NELQCRFPRR
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK
DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP
DIKRLLKVAI


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