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UniProtKB/Swiss-Prot entry Q9SZH2


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

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Entry information
Entry name PER43_ARATH
Primary accession number Q9SZH2
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on December 6, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 61)
Name and origin of the protein
Protein name Peroxidase 43 [Precursor]
Synonyms Atperox P43
EC 1.11.1.7
Gene name
Name: PER43
Synonyms: P43
OrderedLocusNames: At4g25980
ORFNames: F20B18.90, F14M9.7
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]
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
AL049483; CAB39663.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161564; CAB79453.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene At.50365
3D structure databases
HSSP Q42578; 1PA2. [HSSP ENTRY / PDB]
ModBase Q9SZH2.
Protein family/group databases
PeroxiBase 209; AtPrx43.
Organism-specific databases
GeneFarm 1872; 61.
TAIR At4g25980; -.
Gene expression databases
ArrayExpress Q9SZH2; -.
GermOnline AT4G25980; 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; 1.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9SZH2.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G25980.
NMPDR fig|3702.1.peg.20514; -.
Other
ProtoNet Q9SZH2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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    24  24     Potential. 
CHAIN   25   326  302     Peroxidase 43. PRO_0000023709
ACT_SITE   66    66        Proton acceptor (By similarity). 
METAL   67    67        Calcium 1 (By similarity). 
METAL   70    70        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   72    72        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   74    74        Calcium 1 (By similarity). 
METAL   76    76        Calcium 1 (By similarity). 
METAL   189   189        Iron (heme axial ligand) (By similarity). 
METAL   190   190        Calcium 2 (By similarity). 
METAL   241   241        Calcium 2 (By similarity). 
METAL   244   244        Calcium 2 (By similarity). 
METAL   249   249        Calcium 2 (By similarity). 
BINDING   159   159        Substrate; via carbonyl oxygen (By similarity). 
SITE   62    62  1     Transition state stabilizer (By similarity). 
CARBOHYD   151   151        N-linked (GlcNAc...) (Potential). 
DISULFID   35   112        By similarity. 
DISULFID   68    73        By similarity. 
DISULFID   118   322        By similarity. 
DISULFID   196   228        By similarity. 
Sequence information
Length: 326 AA [This is the length of the unprocessed precursor] Molecular weight: 35365 Da [This is the MW of the unprocessed precursor] CRC64: E5BC1BC573EA2A96 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVWANAKMRL ALSLVTVFFG ISLANLEVGF YSNTCPQAES IVKRVVSGAA LSDPNLPAIL 

        70         80         90        100        110        120 
LRLHFHDCFV EGCDGSILVN NGAISEKNAF GHEGVRGFEI VEAVKAELEA ACPGVVSCSD 

       130        140        150        160        170        180 
IVALAARDAI SLANGPAYEV PTGRRDGRVS NMSLAKDMPE VSDSIEILKA KFMQKGLNAK 

       190        200        210        220        230        240 
DLVLLSAAHT IGTTACFFMS KRLYDFLPGG QPDPTINPTF LPELTTQCPQ NGDINVRLPI 

       250        260        270        280        290        300 
DRFSERLFDK QILQNIKDGF AVLQTDAGLY EDVTTRQVVD SYLGMLNPFF GPTFESDFVK 

       310        320 
AIVKMGKIGV KTGFKGEIRR VCSAFN 

Q9SZH2 in FASTA format

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