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UniProtKB/Swiss-Prot entry Q05431


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

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Entry information
Entry name APX1_ARATH
Primary accession number Q05431
Secondary accession numbers Q0WLU2 Q2V4P8 Q2V4P9
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 82)
Name and origin of the protein
Protein name L-ascorbate peroxidase 1, cytosolic
Synonyms AP
AtAPx01
EC 1.11.1.11
Gene name
Name: APX1
OrderedLocusNames: At1g07890
ORFNames: F24B9.2
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-17.
STRAIN=cv. Columbia;
TISSUE=Leaf;
DOI=10.1007/BF00020011; PubMed=1558944 [NCBI, ExPASy, EBI, Israel, Japan]
Kubo A., Saji H., Tanaka K., Tanaka K., Kondo N.;
"Cloning and sequencing of a cDNA encoding ascorbate peroxidase from Arabidopsis thaliana.";
Plant Mol. Biol. 18:691-701(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1016/0014-5793(93)81185-3; PubMed=8422923 [NCBI, ExPASy, EBI, Israel, Japan]
Kubo A., Saji H., Tanaka K., Kondo N.;
"Genomic DNA structure of a gene encoding cytosolic ascorbate peroxidase from Arabidopsis thaliana.";
FEBS Lett. 315:313-317(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Tremousaygue D., Bardet C., Dabos P., Regad F., Pelese F., Lescure B.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[5]
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).
[6]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
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.
[8]
INDUCTION.
DOI=10.1007/BF00020979; PubMed=8534847 [NCBI, ExPASy, EBI, Israel, Japan]
Kubo A., Saji H., Tanaka K., Kondo N.;
"Expression of Arabidopsis cytosolic ascorbate peroxidase gene in response to ozone or sulfur dioxide.";
Plant Mol. Biol. 29:479-489(1995).
[9]
INDUCTION.
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).
[10]
TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1104/pp.118.3.1005; PubMed=9808745 [NCBI, ExPASy, EBI, Israel, Japan]
Storozhenko S., De Pauw P., Van Montagu M., Inze D., Kushnir S.;
"The heat-shock element is a functional component of the Arabidopsis APX1 gene promoter.";
Plant Physiol. 118:1005-1014(1998).
[11]
INDUCTION.
DOI=10.1104/pp.103.029876; PubMed=14739345 [NCBI, ExPASy, EBI, Israel, Japan]
Fourcroy P., Vansuyt G., Kushnir S., Inze D., Briat J.-F.;
"Iron-regulated expression of a cytosolic ascorbate peroxidase encoded by the APX1 gene in Arabidopsis seedlings.";
Plant Physiol. 134:605-613(2004).
[12]
FUNCTION.
DOI=10.1105/tpc.104.026971; PubMed=15608336 [NCBI, ExPASy, EBI, Israel, Japan]
Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J., Coutu J., Shulaev V., Schlauch K., Mittler R.;
"Cytosolic ascorbate peroxidase 1 is a central component of the reactive oxygen gene network of Arabidopsis.";
Plant Cell 17:268-281(2005).
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
X59600; CAA42168.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D14442; BAA03334.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U63815; AAB07880.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007583; AAF75066.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY039879; AAK63983.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056395; AAL08251.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY094002; AAM16263.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK230096; BAF01915.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086425; AAM63427.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D86214; D86214.
S20866; S20866.
RefSeq NP_001030991.2; -.
NP_001030992.2; -.
NP_001077482.1; -.
NP_001117244.1; -.
NP_172267.1; -.
NP_849607.1; -.
NP_973786.1; -.
UniGene At.47584
3D structure databases
HSSP Q43758; 1OAF. [HSSP ENTRY / PDB]
SMR Q05431; 3-250.
ModBase Q05431.
Protein-protein interaction databases
IntAct Q05431; -.
Protein family/group databases
PeroxiBase 1890; AtAPx01.
2D gel databases
SWISS-2DPAGE Q05431; -.
Organism-specific databases
GeneFarm 1942; 146.
TAIR At1g07890; -.
Gene expression databases
ArrayExpress Q05431; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
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 Q05431.
Proteomic databases
ProMEX Q05431; -.
Genome annotation databases
GeneID 837304; -.
GenomeReviews CT485782_GR; AT1G07890.
KEGG ath:AT1G07890; -.
NMPDR fig|3702.1.peg.984; -.
Other
ProtoNet Q05431.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; 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. 
CHAIN   2   250  249     L-ascorbate peroxidase 1, cytosolic. PRO_0000055592
ACT_SITE   42    42        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   38    38  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 250 AA [This is the length of the unprocessed precursor] Molecular weight: 27561 Da [This is the MW of the unprocessed precursor] CRC64: 33A536D85B2CAA6C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTKNYPTVSE DYKKAVEKCR RKLRGLIAEK NCAPIMVRLA WHSAGTFDCQ SRTGGPFGTM 

        70         80         90        100        110        120 
RFDAEQAHGA NSGIHIALRL LDPIREQFPT ISFADFHQLA GVVAVEVTGG PDIPFHPGRE 

       130        140        150        160        170        180 
DKPQPPPEGR LPDATKGCDH LRDVFAKQMG LSDKDIVALS GAHTLGRCHK DRSGFEGAWT 

       190        200        210        220        230        240 
SNPLIFDNSY FKELLSGEKE GLLQLVSDKA LLDDPVFRPL VEKYAADEDA FFADYAEAHM 

       250 
KLSELGFADA 

Q05431 in FASTA format

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