ID   GPX3_ARATH              Reviewed;         206 AA.
AC   O22850;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Probable glutathione peroxidase 3, mitochondrial;
DE            EC=1.11.1.9;
DE   Flags: Precursor;
GN   Name=GPX3; OrderedLocusNames=At2g43350; ORFNames=T1O24.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14617062; DOI=10.1046/j.1365-313X.2003.01901.x;
RA   Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.;
RT   "Glutathione peroxidase genes in Arabidopsis are ubiquitous and
RT   regulated by abiotic stresses through diverse signaling pathways.";
RL   Plant J. 36:602-615(2003).
RN   [5]
RP   FUNCTION, ENZYME REGULATION, INDUCTION, INTERACTION WITH ABI1 AND
RP   ABI2, AND DISRUPTION PHENOTYPE.
RX   PubMed=16998070; DOI=10.1105/tpc.106.044230;
RA   Miao Y., Lv D., Wang P., Wang X.-C., Chen J., Miao C., Song C.-P.;
RT   "An Arabidopsis glutathione peroxidase functions as both a redox
RT   transducer and a scavenger in abscisic acid and drought stress
RT   responses.";
RL   Plant Cell 18:2749-2766(2006).
CC   -!- FUNCTION: May constitute a glutathionine peroxidase-like
CC       protective system against oxidative stresses. Involved positively
CC       in abscisic acid (ABA) signaling pathway that regulates numerous
CC       ABA responses, such as stomatal closure, seed germination and
CC       inhibition of vegetative growth. Oxidizes and represses target
CC       proteins (e.g. the phosphatase activity of ABI1 and ABI2) when
CC       oxidized by H(2)O(2), probably after ABA signaling. Modulates the
CC       calcium channel activity in guard cells in response to ABA or
CC       H(2)O(2). Confers tolerance to drought stress, by enhancing the
CC       ABA-dependent stomatal closure.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- ENZYME REGULATION: The redox states are modulated by H(2)O(2).
CC   -!- SUBUNIT: Interacts with ABI1 and ABI2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: By osmotic stress, H(2)O(2), drought stress, and
CC       metals. Regulated by abscisic acid (ABA); down-regulated by 1mM
CC       ABA (PubMed:14617062), whereas induced by 60uM ABA
CC       (PubMed:16998070).
CC   -!- DISRUPTION PHENOTYPE: Leaves of plants lacking GPX3 are 1 degree
CC       Celsius lower than normal plants, whereas leaves from plants over-
CC       expressing GPX3 are 1.2 degrees Celsius higher, probably because
CC       of the impaired evapotranspiration.
CC   -!- MISCELLANEOUS: The reduced form of ABI2 is converted to the
CC       oxidized form by the addition of oxidized GPX3.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; AC002335; AAB64335.1; -; Genomic_DNA.
DR   EMBL; AY065372; AAL38813.1; -; mRNA.
DR   EMBL; AY096479; AAM20119.1; -; mRNA.
DR   EMBL; AY087030; AAM64591.1; -; mRNA.
DR   IPI; IPI00546051; -.
DR   PIR; A84865; A84865.
DR   RefSeq; NP_181863.1; -.
DR   UniGene; At.28611; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 2501; AtGPx03.
DR   PRIDE; O22850; -.
DR   GeneID; 818936; -.
DR   GenomeReviews; CT485783_GR; AT2G43350.
DR   KEGG; ath:AT2G43350; -.
DR   NMPDR; fig|3702.1.peg.11491; -.
DR   GeneFarm; 2051; 163.
DR   TAIR; At2g43350; -.
DR   OMA; O22850; AQNGNDL.
DR   BRENDA; 1.11.1.9; 302.
DR   ArrayExpress; O22850; -.
DR   GermOnline; AT2G43350; Arabidopsis thaliana.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EC.
DR   GO; GO:0009738; P:abscisic acid mediated signaling; IMP:TAIR.
DR   GO; GO:0042631; P:cellular response to water deprivation; IMP:TAIR.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:TAIR.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Complete proteome; Mitochondrion;
KW   Oxidoreductase; Peroxidase; Stress response; Transit peptide.
FT   TRANSIT       1     12       Mitochondrion (Potential).
FT   CHAIN        13    206       Probable glutathione peroxidase 3,
FT                                mitochondrial.
FT                                /FTId=PRO_0000045458.
FT   ACT_SITE     80     80       By similarity.
SQ   SEQUENCE   206 AA;  23258 MW;  C060AE62F079BD7F CRC64;
     MPRSSRWVNQ RATSKIKKFI LFLGVAFVFY LYRYPSSPST VEQSSTSIYN ISVKDIEGKD
     VSLSKFTGKV LLIVNVASKC GLTHGNYKEM NILYAKYKTQ GFEILAFPCN QFGSQEPGSN
     MEIKETVCNI FKAEFPIFDK IEVNGKNTCP LYNFLKEQKG GLFGDAIKWN FAKFLVDRQG
     NVVDRYAPTT SPLEIEKDIV KLLASA
//