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UniProtKB/Swiss-Prot entry Q9LYB4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPX5_ARATH
Primary accession number Q9LYB4
Secondary accession numbers None
Integrated into Swiss-Prot on March 27, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 47)
Name and origin of the protein
Protein name Probable glutathione peroxidase 5
Synonym EC 1.11.1.9
Gene name
Name: GPX5
OrderedLocusNames: At3g63080
ORFNames: T20O10_180
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1046/j.1365-313X.2003.01901.x; PubMed=14617062 [NCBI, ExPASy, EBI, Israel, Japan]
Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.;
"Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways.";
Plant J. 36:602-615(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL163816; CAB87753.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT003821; AAO41874.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT005137; AAO50670.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085116; AAM61670.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T48097; T48097.
RefSeq NP_191867.1; -.
UniGene At.43439
3D structure databases
HSSP P00435; 1GP1. [HSSP ENTRY / PDB]
ModBase Q9LYB4.
Protein family/group databases
PeroxiBase 2475; AtGPx05.
Organism-specific databases
GeneFarm 2054; 163.
TAIR At3g63080; -.
Gene expression databases
ArrayExpress Q9LYB4; -.
GermOnline AT3G63080; Arabidopsis thaliana.
Family and domain databases
InterPro IPR000889; Glut_peroxidase.
IPR001452; SH3.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PANTHER PTHR11592; Glut_peroxidase; 1.
Pfam PF00255; GSHPx; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000303; Glutathion_perox; 1.
PRINTS PR01011; GLUTPROXDASE.
PR00452; SH3DOMAIN.
PROSITE PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9LYB4.
Genome annotation databases
GeneID 825483; -.
GenomeReviews BA000014_GR; AT3G63080.
KEGG ath:AT3G63080; -.
NMPDR fig|3702.1.peg.17696; -.
Other
ProtoNet Q9LYB4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase; Peroxidase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   173  173     Probable glutathione peroxidase 5. PRO_0000066639
ACT_SITE   46    46        By similarity. 
Sequence information
Length: 173 AA [This is the length of the unprocessed precursor] Molecular weight: 19327 Da [This is the MW of the unprocessed precursor] CRC64: CE3F15979C150C65 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGASSSSSVS EKSIHQFTVK DSSGKEVDLS VYQGKVLLVV NVASKCGFTE SNYTQLTELY 

        70         80         90        100        110        120 
RKYKDQGFVV LAFPCNQFLS QEPGTSEEAH QFACTRFKAE YPVFQKVRVN GQNAAPVYKF 

       130        140        150        160        170 
LKSKKPSFLG SRIKWNFTKF LVGKDGQVID RYGTTVSPLS IQKDIEKALA QEL 

Q9LYB4 in FASTA format

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