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UniProtKB/Swiss-Prot entry Q42592


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

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Entry information
Entry name APXS_ARATH
Primary accession number Q42592
Secondary accession number Q9STM9
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 51)
Name and origin of the protein
Protein name L-ascorbate peroxidase S, chloroplastic/mitochondrial [Precursor]
Synonyms EC 1.11.1.11
Stromal ascorbate peroxidase
sAPX
AtAPx05
Gene name
Name: APXS
OrderedLocusNames: At4g08390
ORFNames: T28D5.80
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 [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).
[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]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M307525200; PubMed=12954611 [NCBI, ExPASy, EBI, Israel, Japan]
Chew O., Whelan J., Millar A.H.;
"Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants.";
J. Biol. Chem. 278:46869-46877(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
X98925; CAA67425.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109819; CAB52561.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161511; CAB77964.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056319; AAL07168.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY114065; AAM45113.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T14193; T14193.
RefSeq NP_192579.1; -.
NP_974520.1; -.
UniGene At.22866
3D structure databases
HSSP Q8LNY5; 1IYN. [HSSP ENTRY / PDB]
SMR Q42592; 100-369.
ModBase Q42592.
Organism-specific databases
GeneFarm 1956; 146.
TAIR At4g08390; -.
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; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q42592.
Proteomic databases
ProMEX Q42592; -.
Genome annotation databases
GeneID 826396; -.
GenomeReviews CT486007_GR; AT4G08390.
NMPDR fig|3702.1.peg.18492; -.
Other
ProtoNet Q42592.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Chloroplast; Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Peroxidase; Plastid; Potassium; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Chloroplast and mitochondrion (Potential). 
CHAIN   ?   372        L-ascorbate peroxidase S, chloroplastic/mitochondrial. PRO_0000261326
ACT_SITE   133   133        Proton acceptor (By similarity). 
METAL   262   262        Iron (heme axial ligand) (By similarity). 
METAL   263   263        Potassium or calcium (By similarity). 
METAL   295   295        Potassium or calcium (By similarity). 
METAL   302   302        Potassium or calcium (By similarity). 
SITE   129   129  1     Transition state stabilizer (By similarity). 
CONFLICT   11    11        G -> V (in Ref. 1; CAA67425). 
CONFLICT   75    75        S -> P (in Ref. 1; CAA67425). 
CONFLICT   81    81        Y -> C (in Ref. 1; CAA67425). 
CONFLICT   371   371        V -> I (in Ref. 1; CAA67425). 
Sequence information
Length: 372 AA [This is the length of the unprocessed precursor] Molecular weight: 40407 Da [This is the MW of the unprocessed precursor] CRC64: A5D94B9A20720B87 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAERVSLTLN GTLLSPPPTT TTTTMSSSLR STTAASLLLR SSSSSSRSTL TLSASSSLSF 

        70         80         90        100        110        120 
VRSLVSSPRL SSSSSLSQKK YRIASVNRSF NSTTAATKSS SSDPDQLKNA REDIKELLST 

       130        140        150        160        170        180 
KFCHPILVRL GWHDAGTYNK NIKEWPQRGG ANGSLRFDIE LKHAANAGLV NALNLIKDIK 

       190        200        210        220        230        240 
EKYSGISYAD LFQLASATAI EEAGGPKIPM KYGRVDASGP EDCPEEGRLP DAGPPSPATH 

       250        260        270        280        290        300 
LREVFYRMGL DDKDIVALSG AHTLGRSRPE RSGWGKPETK YTKEGPGAPG GQSWTPEWLK 

       310        320        330        340        350        360 
FDNSYFKEIK EKRDEDLLVL PTDAAIFEDS SFKVYAEKYA ADQDAFFKDY AVAHAKLSNL 

       370 
GAEFNPPEGI VI 

Q42592 in FASTA format

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