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UniProtKB/Swiss-Prot entry Q1PER6


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

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Entry information
Entry name APX2_ARATH
Primary accession number Q1PER6
Secondary accession numbers Q39006 Q67XB1 Q9SF39
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 21)
Name and origin of the protein
Protein name L-ascorbate peroxidase 2, cytosolic
Synonyms EC 1.11.1.11
L-ascorbate peroxidase 1b
APX1b
AtAPx02
Gene name
Name: APX2
Synonyms: APX1B
OrderedLocusNames: At3g09640
ORFNames: F11F8_23
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 [GENOMIC DNA].
DOI=10.1007/BF00197587; PubMed=8580771 [NCBI, ExPASy, EBI, Israel, Japan]
Santos M., Gosseau H., Lister C., Foyer C., Creissen G.P., Mullineaux P.M.;
"Cytosolic ascorbate peroxidase from Arabidopsis thaliana L. is encoded by a small multigene family.";
Planta 198:64-69(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=cv. Columbia;
TISSUE=Leaf;
DOI=10.1105/tpc.9.4.627; PubMed=9144965 [NCBI, ExPASy, EBI, Israel, Japan]
Karpinski S., Escobar C., Karpinski B., Creissen G.P., Mullineaux P.M.;
"Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress.";
Plant Cell 9:627-640(1997).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., Redman J.C., Wu H.C., Utterback T., Town C.D.;
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION.
DOI=10.1104/pp.001362; PubMed=12068123 [NCBI, ExPASy, EBI, Israel, Japan]
Panchuk I.I., Volkov R.A., Schoffl F.;
"Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis.";
Plant Physiol. 129:838-853(2002).
[7]
INDUCTION.
DOI=10.1111/j.1365-313X.2004.02066.x; PubMed=15086807 [NCBI, ExPASy, EBI, Israel, Japan]
Chang C.C., Ball L., Fryer M.J., Baker N.R., Karpinski S., Mullineaux P.M.;
"Induction of ASCORBATE PEROXIDASE 2 expression in wounded Arabidopsis leaves does not involve known wound-signalling pathways but is associated with changes in photosynthesis.";
Plant J. 38:499-511(2004).
[8]
INDUCTION, AND TISSUE SPECIFICITY.
DOI=10.1046/j.1365-313X.2003.01656.x; PubMed=12609042 [NCBI, ExPASy, EBI, Israel, Japan]
Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M., Baker N.R.;
"Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf water status during excess light stress reveals a functional organisation of Arabidopsis leaves.";
Plant J. 33:691-705(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
X80036; CAA56340.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98275; CAA66925.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC016661; AAF23294.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK176821; BAD44584.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK176908; BAD44671.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ446651; ABE65932.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001030664.1; -.
NP_187575.2; -.
UniGene At.129
3D structure databases
SMR Q1PER6; 4-249.
ModBase Q1PER6.
Organism-specific databases
GeneFarm 727; 146.
TAIR At3g09640; -.
Family and domain databases
InterPro IPR002207; Asc_perxdse.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00459; ASPEROXIDASE.
PR00458; PEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q1PER6.
Genome annotation databases
GeneID 820121; -.
KEGG ath:AT3G09640; -.
NMPDR fig|3702.1.peg.12979; -.
Other
ProtoNet Q1PER6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Potassium.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   251  250     L-ascorbate peroxidase 2, cytosolic. PRO_0000261322
ACT_SITE   43    43        Proton acceptor (By similarity). 
METAL   163   163        Iron (heme axial ligand) (By similarity). 
METAL   164   164        Potassium or calcium (By similarity). 
METAL   180   180        Potassium or calcium (By similarity). 
METAL   182   182        Potassium or calcium (By similarity). 
METAL   185   185        Potassium or calcium; via carbonyl oxygen (By similarity). 
METAL   187   187        Potassium or calcium (By similarity). 
SITE   39    39  1     Transition state stabilizer (By similarity). 
CONFLICT   6     6        Y -> F (in Ref. 5; ABE65932). 
CONFLICT   231   231        F -> S (in Ref. 1; CAA66925 and 2; CAA56340). 
Sequence information
Length: 251 AA [This is the length of the unprocessed precursor] Molecular weight: 28006 Da [This is the MW of the unprocessed precursor] CRC64: FFC7F6D82A4EF3E0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKKSYPEVK EEYKKAVQRC KRKLRGLIAE KHCAPIVLRL AWHSAGTFDV KTKTGGPFGT 

        70         80         90        100        110        120 
IRHPQELAHD ANNGLDIAVR LLDPIKELFP ILSYADFYQL AGVVAVEITG GPEIPFHPGR 

       130        140        150        160        170        180 
LDKVEPPPEG RLPQATKGVD HLRDVFGRMG LNDKDIVALS GGHTLGRCHK ERSGFEGAWT 

       190        200        210        220        230        240 
PNPLIFDNSY FKEILSGEKE GLLQLPTDKA LLDDPLFLPF VEKYAADEDA FFEDYTEAHL 

       250 
KLSELGFADK E 

Q1PER6 in FASTA format

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