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UniProtKB/Swiss-Prot entry P22352


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

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Entry information
Entry name GPX3_HUMAN
Primary accession number P22352
Secondary accession numbers O43787 Q86W78 Q9NZ74 Q9UEL1
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on February 26, 2008 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 93)
Name and origin of the protein
Protein name Glutathione peroxidase 3 [Precursor]
Synonyms EC 1.11.1.9
GSHPx-3
GPx-3
Extracellular glutathione peroxidase
Plasma glutathione peroxidase
GSHPx-P
GPx-P
Gene name
Name: GPX3
Synonyms: GPXP
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], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fetal liver, and Placenta;
PubMed=2229017 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J., Koyama J.;
"Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences.";
J. Biochem. 108:145-148(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=1339300 [NCBI, ExPASy, EBI, Israel, Japan]
Chu F.-F., Esworthy R.S., Doroshow J.H., Doan K., Liu X.F.;
"Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents.";
Blood 79:3233-3238(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymphocyte;
DOI=10.1016/0378-1119(94)90023-X; PubMed=8056346 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshimura S., Suemizu H., Taniguchi Y., Arimori K., Kawabe N., Moriuchi T.;
"The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32.";
Gene 145:293-297(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10970826 [NCBI, ExPASy, EBI, Israel, Japan]
Comhair S.A.A., Thomassen M.J., Erzurum S.C.;
"Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke.";
Am. J. Respir. Cell Mol. Biol. 23:350-354(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-128.
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.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Duodenum, Lung, and Pancreas;
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).
[7]
PROTEIN SEQUENCE OF 107-138 AND 148-175, AND CHARACTERIZATION.
DOI=10.1016/0003-9861(91)90048-N; PubMed=1897960 [NCBI, ExPASy, EBI, Israel, Japan]
Esworthy R.S., Chu F.-F., Paxton R.J., Akman S., Doroshow J.H.;
"Characterization and partial amino acid sequence of human plasma glutathione peroxidase.";
Arch. Biochem. Biophys. 286:330-336(1991).
Comments
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
D00632; BAA00525.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X58295; CAA41228.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D16360; BAA03862.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D16361; BAA03863.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D16362; BAA03864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF217787; AAF43005.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY310878; AAP50261.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013601; AAH13601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC035841; AAH35841.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050378; AAH50378.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I53822; JQ0476.
RefSeq NP_002075.2; -.
UniGene Hs.386793
3D structure databases
PDB
2R37; X-ray; 1.85 A; A/B=25-223.[ExPASy / RCSB / EBI]
PDBsum 2R37; -.
ModBase P22352.
Protein family/group databases
PeroxiBase 3602; HsGPx03.
Enzyme and pathway databases
BioCyc MetaCyc:MON-9873; -.
Polymorphism databases
NIEHS-SNPs GPX3.
2D gel databases
SWISS-2DPAGE P22352; -.
REPRODUCTION-2DPAGE IPI00026199; -.
Organism-specific databases
HGNC HGNC:4555; GPX3.
GenAtlas GPX3.
MIM 138321; gene. [NCBI / EBI]
PharmGKB PA28951; -.
GeneCards P22352.
Gene expression databases
CleanEx HS_GPX3; -.
GermOnline ENSG00000211445; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from direct assay from UniProtKB).
GO:0008430; Molecular function: selenium binding (inferred from direct assay from UniProtKB).
GO:0008134; Molecular function: transcription factor binding (traceable author statement from UniProtKB).
GO:0042744; Biological process: hydrogen peroxide catabolic process (traceable author statement from UniProtKB).
GO:0051289; Biological process: protein homotetramerization (inferred from direct assay from UniProtKB).
GO:0006982; Biological process: response to lipid hydroperoxide (traceable author statement from UniProtKB).
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 P22352.
Genome annotation databases
Ensembl ENSG00000211445; Homo sapiens. [Contig view]
GeneID 2878; -.
KEGG hsa:2878; -.
Phylogenomic databases
HOGENOM P22352; -.
HOVERGEN P22352; -.
Other
DrugBank DB00143; Glutathione.
SOURCE GPX3; Homo sapiens.
ProtoNet P22352.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Oxidoreductase; Peroxidase; Polymorphism; Secreted; Selenium; Selenocysteine; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Potential. 
CHAIN   21   226  206     Glutathione peroxidase 3. PRO_0000013062
ACT_SITE   73    73         
NON_STD   73    73        Selenocysteine. 
VARIANT   128   128  1     F -> L. VAR_020943 
Sequence information
Length: 226 AA [This is the length of the unprocessed precursor] Molecular weight: 25552 Da [This is the MW of the unprocessed precursor] CRC64: A839E87A5CDB51A9 [This is a checksum on the sequence]
        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 

P22352 in FASTA format

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View entry in raw text format (no links)
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