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UniProtKB/Swiss-Prot entry Q9SB81


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

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Entry information
Entry name PER42_ARATH
Primary accession number Q9SB81
Secondary accession numbers Q41937 Q42579 Q43730
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on December 6, 2002 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 70)
Name and origin of the protein
Protein name Peroxidase 42 [Precursor]
Synonyms Atperox P42
EC 1.11.1.7
PRXR1
ATP1a/ATP1b
Gene name
Name: PER42
Synonyms: P42
OrderedLocusNames: At4g21960
ORFNames: F1N20.3, T8O5.170
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;
TISSUE=Flower, Leaf, Root, Silique, and Stem;
Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P.;
"Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases.";
(er) Plant Gene Register PGR96-066.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1023/A:1005707813801; PubMed=9132061 [NCBI, ExPASy, EBI, Israel, Japan]
Kjaersgaard I.V.H., Jespersen H.M., Rasmussen S.K., Welinder K.G.;
"Sequence and RT-PCR expression analysis of two peroxidases from Arabidopsis thaliana belonging to a novel evolutionary branch of plant peroxidases.";
Plant Mol. Biol. 33:699-708(1997).
[3]
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).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168.
TISSUE=Leaf;
Stracke R., Palme K.;
"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-330.
STRAIN=cv. Columbia;
TISSUE=Green siliques;
DOI=10.1046/j.1365-313X.1993.04061051.x; PubMed=8281187 [NCBI, ExPASy, EBI, Israel, Japan]
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana.";
Plant J. 4:1051-1061(1993).
[7]
CHARACTERIZATION.
STRAIN=cv. Columbia;
DOI=10.1016/S0014-5793(98)00849-7; PubMed=9738941 [NCBI, ExPASy, EBI, Israel, Japan]
Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
"Computational analyses and annotations of the Arabidopsis peroxidase gene family.";
FEBS Lett. 433:98-102(1998).
[8]
TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array.";
Plant Physiol. Biochem. 39:221-242(2001).
[9]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1105/tpc.13.1.113; PubMed=11158533 [NCBI, ExPASy, EBI, Israel, Japan]
Schaffer R., Landgraf J., Accerbi M., Simon V., Larson M., Wisman E.;
"Microarray analysis of diurnal and circadian-regulated genes in Arabidopsis.";
Plant Cell 13:113-123(2001).
[10]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
DOI=10.1016/S0378-1119(02)00465-1; PubMed=12034502 [NCBI, ExPASy, EBI, Israel, Japan]
Tognolli M., Penel C., Greppin H., Simon P.;
"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana.";
Gene 288:129-138(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
X98313; CAA66957.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98189; CAA66862.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL021890; CAA17163.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161556; CAB79151.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022140; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AF325015; AAG40367.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428379; AAL16147.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056809; AAL10500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY058071; AAL24179.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY059810; AAL24292.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132009; AAM91042.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083767; AAN60325.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z17792; CAA79071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05478; T05478.
RefSeq NP_567641.1; -.
UniGene At.23508
3D structure databases
HSSP Q42578; 1PA2. [HSSP ENTRY / PDB]
ModBase Q9SB81.
Protein family/group databases
PeroxiBase 208; AtPrx42.
Organism-specific databases
GeneFarm 1871; 61.
TAIR At4g21960; -.
Gene expression databases
ArrayExpress Q9SB81; -.
GermOnline AT4G21960; Arabidopsis thaliana.
Family and domain databases
InterPro IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000823; Peroxidase_pln.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00458; PEROXIDASE.
PR00461; PLPEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; FALSE_NEG.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9SB81.
Genome annotation databases
GeneID 828285; -.
GenomeReviews CT486007_GR; AT4G21960.
KEGG ath:AT4G21960; -.
NMPDR fig|3702.1.peg.20045; -.
Other
ProtoNet Q9SB81.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Biological rhythms; Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    23  23     Potential. 
CHAIN   24   330  307     Peroxidase 42. PRO_0000023708
ACT_SITE   71    71        Proton acceptor (By similarity). 
METAL   72    72        Calcium 1 (By similarity). 
METAL   75    75        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   79    79        Calcium 1 (By similarity). 
METAL   81    81        Calcium 1 (By similarity). 
METAL   197   197        Iron (heme axial ligand) (By similarity). 
METAL   198   198        Calcium 2 (By similarity). 
METAL   247   247        Calcium 2 (By similarity). 
METAL   250   250        Calcium 2 (By similarity). 
METAL   255   255        Calcium 2 (By similarity). 
BINDING   167   167        Substrate; via carbonyl oxygen (By similarity). 
SITE   67    67  1     Transition state stabilizer (By similarity). 
CARBOHYD   170   170        N-linked (GlcNAc...) (Potential). 
DISULFID   40   119        By similarity. 
DISULFID   73    78        By similarity. 
DISULFID   125   323        By similarity. 
DISULFID   204   231        By similarity. 
CONFLICT   13    13        C -> F (in Ref. 2 and 5). 
CONFLICT   27    27        A -> T (in Ref. 2 and 5). 
CONFLICT   47    47        V -> I (in Ref. 2 and 5). 
Sequence information
Length: 330 AA [This is the length of the unprocessed precursor] Molecular weight: 37295 Da [This is the MW of the unprocessed precursor] CRC64: 3237E5DDAB9B6C45 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGGKGVMMVA ILCLWALSAT SEAVTEAEPG LMMNFYKDTC PQAEDIVREQ VKLLYKRHKN 

        70         80         90        100        110        120 
TAFSWLRNIF HDCAVESCDA SLLLDSTRRE LGEKEHDRSF GLRNFRYIEE IKEALERECP 

       130        140        150        160        170        180 
GVVSCSDILV LSAREGIEAV GGPYIPLKTG RRDGLKSRTD MLESYLPDHN ESISVVLEKF 

       190        200        210        220        230        240 
KSIGIDTPGL VALLGSHSVG RTHCVKLVHR LYPEVDPSLN PDHVPHMLHK CPDSIPDPKA 

       250        260        270        280        290        300 
VQYVRNDRGT PMVLDNNYYR NILDNKGLLL VDHQLAHDKR TRPIVKKMAK DQAYFFKEFT 

       310        320        330 
RAIQILSENN PLTGSKGEIR KQCNLANKNH 

Q9SB81 in FASTA format

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