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UniProtKB/Swiss-Prot entry O81772


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

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Entry information
Entry name PER46_ARATH
Primary accession number O81772
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 64)
Name and origin of the protein
Protein name Peroxidase 46 [Precursor]
Synonyms Atperox P46
EC 1.11.1.7
ATP48
Gene name
Name: PER46
Synonyms: P46
OrderedLocusNames: At4g31760
ORFNames: F28M20.50
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
AL031004; CAA19747.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161579; CAB79894.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05094; T05094.
RefSeq NP_194904.1; -.
UniGene At.54570
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase O81772.
Protein family/group databases
PeroxiBase 212; AtPrx46.
Organism-specific databases
GeneFarm 1877; 61.
TAIR At4g31760; -.
Gene expression databases
ArrayExpress O81772; -.
GermOnline AT4G31760; 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 O81772.
Genome annotation databases
GeneID 829304; -.
GenomeReviews CT486007_GR; AT4G31760.
KEGG ath:AT4G31760; -.
NMPDR fig|3702.1.peg.21185; -.
Other
ProtoNet O81772.
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    27  27     Potential. 
CHAIN   28   326  299     Peroxidase 46. PRO_0000023712
ACT_SITE   69    69        Proton acceptor (By similarity). 
METAL   70    70        Calcium 1 (By similarity). 
METAL   73    73        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   75    75        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   77    77        Calcium 1 (By similarity). 
METAL   79    79        Calcium 1 (By similarity). 
METAL   192   192        Iron (heme axial ligand) (By similarity). 
METAL   193   193        Calcium 2 (By similarity). 
METAL   246   246        Calcium 2 (By similarity). 
METAL   249   249        Calcium 2 (By similarity). 
METAL   254   254        Calcium 2 (By similarity). 
SITE   65    65  1     Transition state stabilizer (By similarity). 
CARBOHYD   28    28        N-linked (GlcNAc...) (Potential). 
CARBOHYD   85    85        N-linked (GlcNAc...) (Potential). 
CARBOHYD   278   278        N-linked (GlcNAc...) (Potential). 
DISULFID   38   114        By similarity. 
DISULFID   71    76        By similarity. 
DISULFID   120   322        By similarity. 
DISULFID   199   233        By similarity. 
Sequence information
Length: 326 AA [This is the length of the unprocessed precursor] Molecular weight: 35244 Da [This is the MW of the unprocessed precursor] CRC64: 1FC9CA566895967B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASSYRINCS TLLHLLMFLS SLLTSSANLS FNFYASSCSV AEFLVRNTVR SATSSDPTIP 

        70         80         90        100        110        120 
GKLLRLFFHD CFVQGCDASV LIQGNSTEKS DPGNASLGGF SVIDTAKNAI ENLCPATVSC 

       130        140        150        160        170        180 
ADIVALAARD AVEAAGGPVV EIPTGRRDGK ESMAANVRPN IIDTDFTLDQ MIDAFSSKGL 

       190        200        210        220        230        240 
SIQDLVVLSG AHTIGASHCN AFNGRFQRDS KGNFEVIDAS LDNSYAETLM NKCSSSESSS 

       250        260        270        280        290        300 
LTVSNDPETS AVFDNQYYRN LETHKGLFQT DSALMEDNRT RTMVEELASD EESFFQRWSE 

       310        320 
SFVKLSMVGV RVGEDGEIRR SCSSVN 

O81772 in FASTA format

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