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UniProtKB/Swiss-Prot entry O22850


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

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Entry information
Entry name GPX3_ARATH
Primary accession number O22850
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 2004
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 56)
Name and origin of the protein
Protein name Probable glutathione peroxidase 3, mitochondrial [Precursor]
Synonym EC 1.11.1.9
Gene name
Name: GPX3
OrderedLocusNames: At2g43350
ORFNames: T1O24.9
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1046/j.1365-313X.2003.01901.x; PubMed=14617062 [NCBI, ExPASy, EBI, Israel, Japan]
Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.;
"Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways.";
Plant J. 36:602-615(2003).
[5]
FUNCTION, ENZYME REGULATION, INDUCTION, AND INTERACTION WITH ABI1 AND ABI2.
DOI=10.1105/tpc.106.044230; PubMed=16998070 [NCBI, ExPASy, EBI, Israel, Japan]
Miao Y., Lv D., Wang P., Wang X.-C., Chen J., Miao C., Song C.-P.;
"An Arabidopsis glutathione peroxidase functions as both a redox transducer and a scavenger in abscisic acid and drought stress responses.";
Plant Cell 18:2749-2766(2006).
Comments
  • FUNCTION: May constitute a glutathionine peroxidase-like protective system against oxidative stresses. Involved positively in abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, seed germination and inhibition of vegetative growth. Oxidizes and represses target proteins (e.g. the phosphatase activity of ABI1 and ABI2) when oxidized by H(2)O(2), probably after ABA signaling. Modulates the calcium channel activity in guard cells in response to ABA or H(2)O(2). Confers tolerance to drought stress, by enhancing the ABA-dependent stomatal closure.
  • CATALYTIC ACTIVITY: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
  • ENZYME REGULATION: The redox states are modulated by H(2)O(2).
  • SUBUNIT: Interacts with ABI1 and ABI2.
  • SUBCELLULAR LOCATION: Mitochondrion (Potential).
  • TISSUE SPECIFICITY: Ubiquitous.
  • INDUCTION: By osmotic stress, H(2)O(2), drought stress, and metals. Regulated by abscisic acid (ABA); down-regulated by 1mM ABA (PubMed:14617062), whereas induced by 60uM ABA (PubMed:16998070).
  • MISCELLANEOUS: Leaves of plants lacking GPX3 are 1 degree Celsius lower than normal plants, whereas leaves from plants over-expressing GPX3 are 1.2 degrees Celsius higher, probably because of the impaired evapotranspiration.
  • MISCELLANEOUS: The reduced form of ABI2 is converted to the oxidized form by the addition of oxidized GPX3.
  • 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
AC002335; AAB64335.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY065372; AAL38813.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY096479; AAM20119.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087030; AAM64591.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A84865; A84865.
RefSeq NP_181863.1; -.
UniGene At.28611
3D structure databases
HSSP P00435; 1GP1. [HSSP ENTRY / PDB]
ModBase O22850.
Protein family/group databases
PeroxiBase 2501; AtGPx03.
Organism-specific databases
GeneFarm 2051; 163.
TAIR At2g43350; -.
Gene expression databases
ArrayExpress O22850; -.
GermOnline AT2G43350; Arabidopsis thaliana.
Ontologies
GO
GO:0009738; Biological process: abscisic acid mediated signaling (inferred from mutant phenotype from TAIR).
GO:0042631; Biological process: cellular response to water deprivation (inferred from mutant phenotype from TAIR).
GO:0042542; Biological process: response to hydrogen peroxide (inferred from mutant phenotype from TAIR).
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 O22850.
Genome annotation databases
GeneID 818936; -.
GenomeReviews CT485783_GR; AT2G43350.
KEGG ath:AT2G43350; -.
NMPDR fig|3702.1.peg.11491; -.
Other
ProtoNet O22850.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Abscisic acid signaling pathway; Complete proteome; Mitochondrion; Oxidoreductase; Peroxidase; Stress response; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
TRANSIT   1    12  12     Mitochondrion (Potential). 
CHAIN   13   206  194     Probable glutathione peroxidase 3, mitochondrial. PRO_0000045458
ACT_SITE   80    80        By similarity. 
Sequence information
Length: 206 AA [This is the length of the unprocessed precursor] Molecular weight: 23258 Da [This is the MW of the unprocessed precursor] CRC64: C060AE62F079BD7F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPRSSRWVNQ RATSKIKKFI LFLGVAFVFY LYRYPSSPST VEQSSTSIYN ISVKDIEGKD 

        70         80         90        100        110        120 
VSLSKFTGKV LLIVNVASKC GLTHGNYKEM NILYAKYKTQ GFEILAFPCN QFGSQEPGSN 

       130        140        150        160        170        180 
MEIKETVCNI FKAEFPIFDK IEVNGKNTCP LYNFLKEQKG GLFGDAIKWN FAKFLVDRQG 

       190        200 
NVVDRYAPTT SPLEIEKDIV KLLASA 

O22850 in FASTA format

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