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UniProtKB/Swiss-Prot entry Q7XZP5


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

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Entry information
Entry name APX5_ARATH
Primary accession number Q7XZP5
Secondary accession number O65634
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on November 28, 2006 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 34)
Name and origin of the protein
Protein name L-ascorbate peroxidase 5, peroxisomal [Precursor]
Synonyms AtAPx04
EC 1.11.1.11
Gene name
Name: APX5
OrderedLocusNames: At4g35970
ORFNames: T19K4.100, F4B14_240
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=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan]
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-279.
STRAIN=cv. Columbia;
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).
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
AL022373; CAA18491.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031986; CAA21483.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161588; CAB81506.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK119023; BAC43599.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006053; AAP04038.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF441714; AAP72144.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04707; T04707.
RefSeq NP_195321.1; -.
UniGene At.31367
3D structure databases
HSSP Q43758; 1OAF. [HSSP ENTRY / PDB]
ModBase Q7XZP5.
Organism-specific databases
GeneFarm 1983; 146.
TAIR At4g35970; -.
Ontologies
GO
GO:0005778; Cellular component: peroxisomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
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 Q7XZP5.
Genome annotation databases
GeneID 829751; -.
GenomeReviews CT486007_GR; AT4G35970.
KEGG ath:AT4G35970; -.
NMPDR fig|3702.1.peg.21690; -.
Other
ProtoNet Q7XZP5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding; Oxidoreductase; Peroxidase; Peroxisome; Potassium; Transit peptide; Transmembrane.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Peroxisome (Potential). 
CHAIN   ?   279        L-ascorbate peroxidase 5, peroxisomal. PRO_0000261324
TRANSMEM   251   271  21     Potential. 
ACT_SITE   39    39        Proton acceptor (By similarity). 
METAL   158   158        Iron (heme axial ligand) (By similarity). 
METAL   159   159        Potassium or calcium (By similarity). 
METAL   175   175        Potassium or calcium (By similarity). 
METAL   182   182        Potassium or calcium (By similarity). 
SITE   35    35  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 279 AA [This is the length of the unprocessed precursor] Molecular weight: 30895 Da [This is the MW of the unprocessed precursor] CRC64: 518836C729B1C745 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVNVDAEYL KEIEKTRRDL RALISSRNCA PIMLRLAWHD AGTYDAKKKT GGANGSIRFK 

        70         80         90        100        110        120 
EELNRPHNKG LEKAVAFCEE VKAKHPRVSY ADLYQLAGVV AVEVTGGPAI PFTPGRKDAD 

       130        140        150        160        170        180 
SADDGELPNP NEGASHLRTL FSRMGLLDRD IVALSGGHTL GRAHKERSDF EGPWTQDPLK 

       190        200        210        220        230        240 
FDNSYFVELL KGETPGLLQL KTDKALLDDP KFHPFVKLYA KDEDMFFKAY AISHKKLSEL 

       250        260        270 
GFNPPRRIPS AVTQQTLGIA VAAAVVIFTI CYEASRRGK 

Q7XZP5 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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