GPX6_ARATH
ID GPX6_ARATH Reviewed; 232 AA.
AC O48646; Q94BV3;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial;
DE Short=AtGPX1;
DE Short=PHGPx;
DE EC=1.11.1.12;
DE Flags: Precursor;
GN Name=GPX6; Synonyms=GPX1; OrderedLocusNames=At4g11600; ORFNames=T5C23.30;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RA Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M.;
RT "Cloning of a cDNA encoding a putative glutathione peroxidase protein from
RT Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR98-047(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-232.
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-232, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9511228; DOI=10.1266/ggs.72.311;
RA Sugimoto M., Sakamoto W.;
RT "Putative phospholipid hydroperoxide glutathione peroxidase gene from
RT Arabidopsis thaliana induced by oxidative stress.";
RL Genes Genet. Syst. 72:311-316(1997).
RN [7]
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: Mitochondrion {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at a low but detectable level in leaves,
CC stems, and flowers, but at a higher level in siliques and even higher
CC in roots. Predominantly expressed in seeds.
CC {ECO:0000269|PubMed:14617062, ECO:0000269|Ref.1}.
CC -!- INDUCTION: By salt stress, osmotic stress, cold treatment, and metals.
CC Up-regulated by salicylic acid (SA), jasmonic acid (JA), abscisic acid
CC (ABA) and auxin. {ECO:0000269|PubMed:14617062,
CC ECO:0000269|PubMed:9511228, ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC09173.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM66969.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA24226.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB39931.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB78203.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF030132; AAC09173.1; ALT_INIT; mRNA.
DR EMBL; AL049500; CAB39931.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161532; CAB78203.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE83029.1; -; Genomic_DNA.
DR EMBL; AY039863; AAK63967.1; -; mRNA.
DR EMBL; AY077655; AAL76133.1; -; mRNA.
DR EMBL; AY088647; AAM66969.1; ALT_INIT; mRNA.
DR EMBL; AB001568; BAA24226.1; ALT_INIT; mRNA.
DR PIR; T04207; T04207.
DR RefSeq; NP_192897.2; NM_117229.4.
DR AlphaFoldDB; O48646; -.
DR SMR; O48646; -.
DR BioGRID; 12064; 3.
DR IntAct; O48646; 2.
DR MINT; O48646; -.
DR STRING; 3702.AT4G11600.1; -.
DR PeroxiBase; 2502; AtGPx06.
DR iPTMnet; O48646; -.
DR PaxDb; O48646; -.
DR PRIDE; O48646; -.
DR ProteomicsDB; 220582; -.
DR EnsemblPlants; AT4G11600.1; AT4G11600.1; AT4G11600.
DR GeneID; 826765; -.
DR Gramene; AT4G11600.1; AT4G11600.1; AT4G11600.
DR KEGG; ath:AT4G11600; -.
DR Araport; AT4G11600; -.
DR TAIR; locus:2139712; AT4G11600.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_0_1_1; -.
DR InParanoid; O48646; -.
DR OMA; LAPFKGQ; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; O48646; -.
DR PRO; PR:O48646; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O48646; baseline and differential.
DR Genevisible; O48646; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISS:TAIR.
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 Mitochondrion; Oxidoreductase; Peroxidase; Reference proteome;
KW Stress response; Transit peptide.
FT TRANSIT 1..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 55..232
FT /note="Probable phospholipid hydroperoxide glutathione
FT peroxidase 6, mitochondrial"
FT /id="PRO_0000013088"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P36968"
FT CONFLICT 30
FT /note="S -> SSSS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="S -> Y (in Ref. 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 25584 MW; 93F3084A8A331494 CRC64;
MLRSSIRLLY IRRTSPLLRS LSSSSSSSSS KRFDSAKPLF NSHRIISLPI STTGAKLSRS
EHSMAASSEP KSLYDFTVKD AKGNDVDLSI YKGKVLLIVN VASQCGLTNS NYTELAQLYE
KYKGHGFEIL AFPCNQFGNQ EPGTNEEIVQ FACTRFKAEY PIFDKVDVNG DKAAPVYKFL
KSSKGGLFGD GIKWNFAKFL VDKDGNVVDR FAPTTSPLSI EKDVKKLLGV TA
