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UniProtKB/Swiss-Prot entry Q9JHC0


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

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Entry information
Entry name GPX2_MOUSE
Primary accession number Q9JHC0
Secondary accession number Q3V2B2
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on February 26, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 60)
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
Gene name
Name: Gpx2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
DOI=10.1006/geno.1996.0227; PubMed=8661011 [NCBI, ExPASy, EBI, Israel, Japan]
Chu F.-F., Esworthy R.S., Burmeister M.;
"The mouse glutathione peroxidase Gpx2 gene maps to chromosome 12; its pseudogene Gpx2-ps maps to chromosome 7.";
Genomics 33:516-518(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
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
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
U62658; AAD41533.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK131940; BAE20886.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010823; AAH10823.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034335; AAH34335.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039658; AAH39658.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054848; AAH54848.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_109602.2; -.
UniGene Mm.441856
3D structure databases
HSSP P00435; 1GP1. [HSSP ENTRY / PDB]
SMR Q9JHC0; 4-187.
ModBase Q9JHC0.
Protein family/group databases
PeroxiBase 3710; MmGPx02.
PTM databases
PhosphoSite Q9JHC0; -.
Organism-specific databases
MGI MGI:106609; Gpx2.
Gene expression databases
ArrayExpress Q9JHC0; -.
CleanEx MM_GPX2; -.
GermOnline ENSMUSG00000042808; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from MGI).
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from mutant phenotype from MGI).
GO:0008430; Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051702; Biological process: interaction with symbiont (inferred from genetic interaction from MGI).
GO:0002862; Biological process: negative regulation of inflammatory response to antigenic stimulus (inferred from genetic interaction from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979; Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
GO:0009609; Biological process: response to symbiotic bacterium (inferred from genetic interaction from MGI).
GO:0001659; Biological process: temperature homeostasis (inferred from genetic interaction from MGI).
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).
ProtoNet Q9JHC0.
Genome annotation databases
Ensembl ENSMUSG00000042808; Mus musculus. [Contig view]
GeneID 14776; -.
KEGG mmu:14776; -.
Phylogenomic databases
HOGENOM Q9JHC0; -.
HOVERGEN Q9JHC0; -.
Other
NextBio 286881; -.
SOURCE Gpx2; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Oxidoreductase; Peroxidase; Selenium; Selenocysteine.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   190  190     Glutathione peroxidase 2. PRO_0000066622
ACT_SITE   40    40         
NON_STD   40    40        Selenocysteine. 
CONFLICT   14    14        I -> V (in Ref. 2; BAE20886). 
Sequence information
Length: 190 AA [This is the length of the unprocessed precursor] Molecular weight: 21990 Da [This is the MW of the unprocessed precursor] CRC64: F66BDD7A431E1A6D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAYIAKSFYD LSAIGLDGEK IDFNTFRGRA VLIENVASLU GTTTRDYNQL NELQCRFPRR 

        70         80         90        100        110        120 
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFS LTQKCDVNGQ NEHPVFAYLK 

       130        140        150        160        170        180 
DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV SWNFEKFLIG PEGEPFRRYS RSFQTINIEP 

       190 
DIKRLLKVAI 

Q9JHC0 in FASTA format

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