GPX5_ARATH
ID GPX5_ARATH Reviewed; 173 AA.
AC Q9LYB4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable glutathione peroxidase 5;
DE EC=1.11.1.9;
GN Name=GPX5; OrderedLocusNames=At3g63080; ORFNames=T20O10_180;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [7]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: May constitute a glutathione peroxidase-like protective
CC system against oxidative stresses. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130};
CC Lipid-anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14617062}.
CC -!- INDUCTION: By salt stress, osmotic stress and metals. Down-regulated by
CC abscisic acid (ABA). {ECO:0000269|PubMed:14617062}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; AL163816; CAB87753.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80432.1; -; Genomic_DNA.
DR EMBL; BT003821; AAO41874.1; -; mRNA.
DR EMBL; BT005137; AAO50670.1; -; mRNA.
DR EMBL; AY085116; AAM61670.1; -; mRNA.
DR PIR; T48097; T48097.
DR RefSeq; NP_191867.1; NM_116173.4.
DR AlphaFoldDB; Q9LYB4; -.
DR SMR; Q9LYB4; -.
DR BioGRID; 10797; 6.
DR IntAct; Q9LYB4; 6.
DR STRING; 3702.AT3G63080.1; -.
DR PeroxiBase; 2475; AtGPx05.
DR iPTMnet; Q9LYB4; -.
DR PaxDb; Q9LYB4; -.
DR PRIDE; Q9LYB4; -.
DR ProteomicsDB; 220581; -.
DR DNASU; 825483; -.
DR EnsemblPlants; AT3G63080.1; AT3G63080.1; AT3G63080.
DR GeneID; 825483; -.
DR Gramene; AT3G63080.1; AT3G63080.1; AT3G63080.
DR KEGG; ath:AT3G63080; -.
DR Araport; AT3G63080; -.
DR TAIR; locus:2099252; AT3G63080.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_0_1_1; -.
DR InParanoid; Q9LYB4; -.
DR OMA; CAFAEAN; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; Q9LYB4; -.
DR BioCyc; ARA:AT3G63080-MON; -.
DR PRO; PR:Q9LYB4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYB4; baseline and differential.
DR Genevisible; Q9LYB4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:TAIR.
DR GO; GO:0005886; C:plasma membrane; 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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
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 PIRSF; PIRSF000303; Glutathion_perox; 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 Cell membrane; Lipoprotein; Membrane; Myristate; Oxidoreductase;
KW Peroxidase; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22223895,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..173
FT /note="Probable glutathione peroxidase 5"
FT /id="PRO_0000066639"
FT ACT_SITE 46
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:22223895"
SQ SEQUENCE 173 AA; 19327 MW; CE3F15979C150C65 CRC64;
MGASSSSSVS EKSIHQFTVK DSSGKEVDLS VYQGKVLLVV NVASKCGFTE SNYTQLTELY
RKYKDQGFVV LAFPCNQFLS QEPGTSEEAH QFACTRFKAE YPVFQKVRVN GQNAAPVYKF
LKSKKPSFLG SRIKWNFTKF LVGKDGQVID RYGTTVSPLS IQKDIEKALA QEL
