P52032 (GPX1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
Short name=PHGPx
EC=1.11.1.12

Gene names

Name:	GPX1
Ordered Locus Names:	At2g25080
ORF Names:	F13D4.40

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione By similarity.
Catalytic activity	2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O.
Subcellular location	Plastid › chloroplast stroma Ref.6.
Tissue specificity	Expressed in leaves, stems, flowers, green siliques and seeds. Ref.7
Induction	By salt stress, osmotic stress, metals and heat treatment. Up-regulated by abscisic acid (ABA) and auxin. Ref.7
Sequence similarities	Belongs to the glutathione peroxidase family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast envelope Inferred from direct assay Ref.6. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR chloroplast thylakoid membrane Inferred from direct assay. Source: TAIR
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: InterPro phospholipid-hydroperoxide glutathione peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 64	64	Chloroplast Potential
	Chain	65 – 236	172	Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic		PRO_0000013086
Sites
	Active site	111	1	By similarity
Experimental info
	Sequence conflict	18	1	V → F in CAA61965. Ref.1
	Sequence conflict	236	1	A → ELKNF Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P52032 [UniParc]. Last modified March 27, 2002. Version 2. Checksum: D676C0381526C37A	FASTA	236	26,016
	10 20 30 40 50 60 MVSMTTSSSS YGTFSTVVNS SRPNSSATFL VPSLKFSTGI SNFANLSNGF SLKSPINPGF 70 80 90 100 110 120 LFKSRPFTVQ ARAAAEKTVH DFTVKDIDGK DVALNKFKGK VMLIVNVASR CGLTSSNYSE 130 140 150 160 170 180 LSHLYEKYKT QGFEILAFPC NQFGFQEPGS NSEIKQFACT RFKAEFPIFD KVDVNGPSTA 190 200 210 220 230 PIYEFLKSNA GGFLGGLIKW NFEKFLIDKK GKVVERYPPT TSPFQIEKDI QKLLAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a glutathione peroxidase homologue from Arabidopsis thaliana." Gachotte D., Benveniste P. Plant Gene Register PGR95-133 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Identification of cDNAS encoding plastid-targeted glutathione peroxidase." Mullineaux P.M., Karpinski S., Jimenez A., Cleary S.P., Robinson C., Creissen G.P. Plant J. 13:375-379(1998) [PubMed: 9680987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana." Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N. Mol. Cell. Proteomics 2:325-345(2003) [PubMed: 12766230] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: cv. Wassilewskija.
[7]	"Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways." Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P. Plant J. 36:602-615(2003) [PubMed: 14617062] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X89866 mRNA. Translation: CAA61965.1. AJ000469 mRNA. Translation: CAA04112.1. CP002685 Genomic DNA. Translation: AEC07655.1. AY035153 mRNA. Translation: AAK59657.1. AY063024 mRNA. Translation: AAL34198.1.
IPI	IPI00520738.
PIR	A84644. S71250.
RefSeq	NP_180080.1. NM_128065.4.
UniGene	At.24670.
3D structure databases
ProteinModelPortal	P52032.
SMR	P52032. Positions 77-234.
ModBase	Search...
Protein-protein interaction databases
STRING	P52032.
Protein family/group databases
PeroxiBase	2499. AtGPx01.
Proteomic databases
PRIDE	P52032.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G25080.1; AT2G25080.1; AT2G25080.
GeneID	817046.
GenomeReviews	Gene locus AT2G25080 in contig CT485783_GR.
KEGG	ath:AT2G25080.
NMPDR	fig|3702.1.peg.9525.
Organism-specific databases
GeneFarm	2047. 163.
TAIR	At2g25080.
Phylogenomic databases
eggNOG	KOG1651.
GeneTree	EPGT00050000008661.
HOGENOM	HBG648990.
InParanoid	P52032.
OMA	SFCELNF.
PhylomeDB	P52032.
ProtClustDB	PLN02399.
Gene expression databases
ArrayExpress	P52032.
Genevestigator	P52032.
GermOnline	AT2G25080. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000889. Glutathione_peroxidase. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K00432.
PANTHER	PTHR11592. Glut_peroxidase. 1 hit.
Pfam	PF00255. GSHPx. 1 hit. [Graphical view]
PIRSF	PIRSF000303. Glutathion_perox. 1 hit.
PRINTS	PR01011. GLUTPROXDASE.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS00460. GLUTATHIONE_PEROXID_1. 1 hit. PS00763. GLUTATHIONE_PEROXID_2. 1 hit. PS51355. GLUTATHIONE_PEROXID_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPX1_ARATH

Accession

Primary (citable) accession number: P52032
Secondary accession number(s): O19985, O81717

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 27, 2002
Last modified:	November 16, 2011
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program