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   03-AUG-2022, entry version 143.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   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., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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   [5]
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 regulated
RT   by abiotic stresses through diverse signaling pathways.";
RL   Plant J. 36:602-615(2003).
RN   [6]
RP   FUNCTION, ACTIVITY REGULATION, INDUCTION, INTERACTION WITH ABI1 AND ABI2,
RP   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 transducer
RT   and a scavenger in abscisic acid and drought stress responses.";
RL   Plant Cell 18:2749-2766(2006).
CC   -!- FUNCTION: May constitute a glutathione peroxidase-like protective
CC       system against oxidative stresses. Involved positively in abscisic acid
CC       (ABA) signaling pathway that regulates numerous ABA responses, such as
CC       stomatal closure, seed germination and inhibition of vegetative growth.
CC       Oxidizes and represses target proteins (e.g. the phosphatase activity
CC       of ABI1 and ABI2) when oxidized by H(2)O(2), probably after ABA
CC       signaling. Modulates the calcium channel activity in guard cells in
CC       response to ABA or H(2)O(2). Confers tolerance to drought stress, by
CC       enhancing the ABA-dependent stomatal closure.
CC       {ECO:0000269|PubMed:16998070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC   -!- ACTIVITY REGULATION: The redox states are modulated by H(2)O(2).
CC       {ECO:0000269|PubMed:16998070}.
CC   -!- SUBUNIT: Interacts with ABI1 and ABI2. {ECO:0000269|PubMed:16998070}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14617062}.
CC   -!- INDUCTION: By osmotic stress, H(2)O(2), drought stress, and metals.
CC       Regulated by abscisic acid (ABA); down-regulated by 1 mM ABA
CC       (PubMed:14617062), whereas induced by 60 uM ABA (PubMed:16998070).
CC       {ECO:0000269|PubMed:14617062, ECO:0000269|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 of the
CC       impaired evapotranspiration. {ECO:0000269|PubMed:16998070}.
CC   -!- MISCELLANEOUS: The reduced form of ABI2 is converted to the oxidized
CC       form by the addition of oxidized GPX3.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC002335; AAB64335.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10254.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10255.1; -; Genomic_DNA.
DR   EMBL; AY065372; AAL38813.1; -; mRNA.
DR   EMBL; AY096479; AAM20119.1; -; mRNA.
DR   EMBL; AY087030; AAM64591.1; -; mRNA.
DR   PIR; A84865; A84865.
DR   RefSeq; NP_001189742.1; NM_001202813.1.
DR   RefSeq; NP_181863.1; NM_129896.4.
DR   AlphaFoldDB; O22850; -.
DR   SMR; O22850; -.
DR   BioGRID; 4273; 3.
DR   STRING; 3702.AT2G43350.2; -.
DR   PeroxiBase; 2501; AtGPx03.
DR   SwissPalm; O22850; -.
DR   PaxDb; O22850; -.
DR   PRIDE; O22850; -.
DR   ProteomicsDB; 220706; -.
DR   EnsemblPlants; AT2G43350.1; AT2G43350.1; AT2G43350.
DR   EnsemblPlants; AT2G43350.2; AT2G43350.2; AT2G43350.
DR   GeneID; 818936; -.
DR   Gramene; AT2G43350.1; AT2G43350.1; AT2G43350.
DR   Gramene; AT2G43350.2; AT2G43350.2; AT2G43350.
DR   KEGG; ath:AT2G43350; -.
DR   Araport; AT2G43350; -.
DR   TAIR; locus:2058233; AT2G43350.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_0_1_1; -.
DR   InParanoid; O22850; -.
DR   OMA; EMNILYA; -.
DR   OrthoDB; 1483113at2759; -.
DR   PhylomeDB; O22850; -.
DR   BioCyc; ARA:AT2G43350-MON; -.
DR   BRENDA; 1.11.1.9; 399.
DR   PRO; PR:O22850; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22850; baseline and differential.
DR   Genevisible; O22850; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; ISS:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0042631; P:cellular response to water deprivation; IMP:TAIR.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:TAIR.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 1.
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; Mitochondrion; Oxidoreductase; Peroxidase;
KW   Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..12
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           13..206
FT                   /note="Probable glutathione peroxidase 3, mitochondrial"
FT                   /id="PRO_0000045458"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000250"
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