ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q42564


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name APX3_ARATH
Primary accession number Q42564
Secondary accession number O81810
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 56)
Name and origin of the protein
Protein name L-ascorbate peroxidase 3, peroxisomal [Precursor]
Synonyms AtAPx03
EC 1.11.1.11
Gene name
Name: APX3
Synonyms: APX, APXIII
OrderedLocusNames: At4g35000
ORFNames: M4E13.60
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].
STRAIN=cv. Columbia;
PubMed=9291097 [NCBI, ExPASy, EBI, Israel, Japan]
Jespersen H.M., Kjaersgaard I.V.H., Oestergaard L., Welinder K.G.;
"From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase.";
Biochem. J. 326:305-310(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
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 [MRNA].
DOI=10.1023/A:1005814109732; PubMed=9290648 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Wang J., Nickel U., Allen R.D., Goodman H.M.;
"Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase.";
Plant Mol. Biol. 34:967-971(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Escobar C., Bradley D.J., Puente P., Harberd N., Creissen G.P., Mullineaux P.M.;
"Ascorbate peroxidase III gene from Arabidopsis thaliana is regulated by light and development.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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).
[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]
SUBCELLULAR LOCATION.
DOI=10.1093/jxb/erl060; PubMed=16873450 [NCBI, ExPASy, EBI, Israel, Japan]
Narendra S., Venkataramani S., Shen G., Wang J., Pasapula V., Lin Y., Kornyeyev D., Holaday A.S., Zhang H.;
"The Arabidopsis ascorbate peroxidase 3 is a peroxisomal membrane-bound antioxidant enzyme and is dispensable for Arabidopsis growth and development.";
J. Exp. Bot. 57:3033-3042(2006).
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
X98003; CAA66640.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98276; CAA66926.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U69138; AAB71493.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ006030; CAA06823.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022023; CAA17765.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161586; CAB80217.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY065143; AAL38319.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY081646; AAM10208.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086162; AAM63367.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S71279; S71279.
RefSeq NP_195226.1; -.
UniGene At.47586
3D structure databases
HSSP Q43758; 1OAF. [HSSP ENTRY / PDB]
ModBase Q42564.
Protein family/group databases
PeroxiBase 1891; AtAPx03.
Organism-specific databases
GeneFarm 1982; 146.
TAIR At4g35000; -.
Gene expression databases
GermOnline AT4G35000; Arabidopsis thaliana.
Ontologies
GO
GO:0046861; Cellular component: glyoxysomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
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 Q42564.
Proteomic databases
ProMEX Q42564; -.
Genome annotation databases
GeneID 829652; -.
GenomeReviews CT486007_GR; AT4G35000.
KEGG ath:AT4G35000; -.
NMPDR fig|3702.1.peg.21574; -.
Other
ProtoNet Q42564.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Glyoxysome; 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   ?   287        L-ascorbate peroxidase 3, peroxisomal. PRO_0000261323
TRANSMEM   259   279  21     Potential. 
ACT_SITE   40    40        Proton acceptor (By similarity). 
METAL   160   160        Iron (heme axial ligand) (By similarity). 
METAL   161   161        Potassium or calcium (By similarity). 
METAL   177   177        Potassium or calcium (By similarity). 
METAL   184   184        Potassium or calcium (By similarity). 
SITE   36    36  1     Transition state stabilizer (By similarity). 
CONFLICT   182   182        K -> N (in Ref. 4; CAA06823). 
CONFLICT   189   189        V -> VR (in Ref. 4; CAA06823). 
CONFLICT   223   223        Missing (in Ref. 4; CAA06823). 
Sequence information
Length: 287 AA [This is the length of the unprocessed precursor] Molecular weight: 31572 Da [This is the MW of the unprocessed precursor] CRC64: B348E74BA34115DE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAPIVDAEY LKEITKARRE LRSLIANKNC APIMLRLAWH DAGTYDAQSK TGGPNGSIRN 

        70         80         90        100        110        120 
EEEHTHGANS GLKIALDLCE GVKAKHPKIT YADLYQLAGV VAVEVTGGPD IVFVPGRKDS 

       130        140        150        160        170        180 
NVCPKEGRLP DAKQGFQHLR DVFYRMGLSD KDIVALSGGH TLGRAHPERS GFDGPWTQEP 

       190        200        210        220        230        240 
LKFDNSYFVE LLKGESEGLL KLPTDKTLLE DPEFRRLVEL YAKDEDAFFR DYAESHKKLS 

       250        260        270        280 
ELGFNPNSSA GKAVADSTIL AQSAFGVAVA AAVVAFGYFY EIRKRMK 

Q42564 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!