GPX1_ARATH
ID GPX1_ARATH Reviewed; 236 AA.
AC P52032; O19985; O81717;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic;
DE Short=PHGPx;
DE EC=1.11.1.12;
DE Flags: Precursor;
GN Name=GPX1; OrderedLocusNames=At2g25080; ORFNames=F13D4.40;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Gachotte D., Benveniste P.;
RT "Cloning and sequencing of a glutathione peroxidase homologue from
RT Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR95-133(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9680987; DOI=10.1046/j.1365-313x.1998.00052.x;
RA Mullineaux P.M., Karpinski S., Jimenez A., Cleary S.P., Robinson C.,
RA Creissen G.P.;
RT "Identification of cDNAS encoding plastid-targeted glutathione
RT peroxidase.";
RL Plant J. 13:375-379(1998).
RN [3]
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 [4]
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 [5]
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 [6]
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).
CC -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC organic hydroperoxide, by glutathione. {ECO:0000250|UniProtKB:O70325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a
CC hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O;
CC Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019;
CC EC=1.11.1.12; Evidence={ECO:0000250|UniProtKB:P36968};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, green siliques
CC and seeds. {ECO:0000269|PubMed:14617062}.
CC -!- INDUCTION: By salt stress, osmotic stress, metals and heat treatment.
CC Up-regulated by abscisic acid (ABA) and auxin.
CC {ECO:0000269|PubMed:14617062}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; X89866; CAA61965.1; -; mRNA.
DR EMBL; AJ000469; CAA04112.1; -; mRNA.
DR EMBL; CP002685; AEC07655.1; -; Genomic_DNA.
DR EMBL; AY035153; AAK59657.1; -; mRNA.
DR EMBL; AY063024; AAL34198.1; -; mRNA.
DR PIR; A84644; A84644.
DR PIR; S71250; S71250.
DR RefSeq; NP_180080.1; NM_128065.5.
DR AlphaFoldDB; P52032; -.
DR SMR; P52032; -.
DR BioGRID; 2398; 1.
DR STRING; 3702.AT2G25080.1; -.
DR PeroxiBase; 2499; AtGPx01.
DR iPTMnet; P52032; -.
DR PaxDb; P52032; -.
DR PRIDE; P52032; -.
DR ProteomicsDB; 220702; -.
DR EnsemblPlants; AT2G25080.1; AT2G25080.1; AT2G25080.
DR GeneID; 817046; -.
DR Gramene; AT2G25080.1; AT2G25080.1; AT2G25080.
DR KEGG; ath:AT2G25080; -.
DR Araport; AT2G25080; -.
DR TAIR; locus:2040179; AT2G25080.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_0_0_1; -.
DR InParanoid; P52032; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; P52032; -.
DR BioCyc; ARA:AT2G25080-MON; -.
DR PRO; PR:P52032; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P52032; baseline and differential.
DR Genevisible; P52032; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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 2: Evidence at transcript level;
KW Chloroplast; Oxidoreductase; Peroxidase; Plastid; Reference proteome;
KW Stress response; Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..236
FT /note="Phospholipid hydroperoxide glutathione peroxidase 1,
FT chloroplastic"
FT /id="PRO_0000013086"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /evidence="ECO:0000250|UniProtKB:P36968"
FT CONFLICT 18
FT /note="V -> F (in Ref. 1; CAA61965)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="A -> ELKNF (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26016 MW; D676C0381526C37A CRC64;
MVSMTTSSSS YGTFSTVVNS SRPNSSATFL VPSLKFSTGI SNFANLSNGF SLKSPINPGF
LFKSRPFTVQ ARAAAEKTVH DFTVKDIDGK DVALNKFKGK VMLIVNVASR CGLTSSNYSE
LSHLYEKYKT QGFEILAFPC NQFGFQEPGS NSEIKQFACT RFKAEFPIFD KVDVNGPSTA
PIYEFLKSNA GGFLGGLIKW NFEKFLIDKK GKVVERYPPT TSPFQIEKDI QKLLAA
