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UniProtKB/Swiss-Prot entry Q96510


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

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Entry information
Entry name PER35_ARATH
Primary accession number Q96510
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 72)
Name and origin of the protein
Protein name Peroxidase 35 [Precursor]
Synonyms Atperox P35
EC 1.11.1.7
ATP21a
Gene name
Name: PER35
Synonyms: P35
OrderedLocusNames: At3g49960
ORFNames: F3A4.40
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;
Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Hansen L.N., Rasmussen S.K.;
"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
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).
[4]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1105/tpc.003483; PubMed=12172015 [NCBI, ExPASy, EBI, Israel, Japan]
Fowler S., Thomashow M.F.;
"Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway.";
Plant Cell 14:1675-1690(2002).
[5]
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
X98807; CAA67339.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132978; CAB62104.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T45849; T45849.
RefSeq NP_190565.1; -.
UniGene At.19626
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q96510.
Protein family/group databases
PeroxiBase 201; AtPrx35.
Organism-specific databases
GeneFarm 1862; 61.
TAIR At3g49960; -.
Gene expression databases
ArrayExpress Q96510; -.
GermOnline AT3G49960; Arabidopsis thaliana.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004601; Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q96510; -.
Genome annotation databases
GeneID 824158; -.
GenomeReviews BA000014_GR; AT3G49960.
KEGG ath:AT3G49960; -.
NMPDR fig|3702.1.peg.16244; -.
Other
ProtoNet Q96510.
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; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    25  25     Potential. 
CHAIN   26   329  304     Peroxidase 35. PRO_0000023701
ACT_SITE   67    67        Proton acceptor (By similarity). 
METAL   68    68        Calcium 1 (By similarity). 
METAL   71    71        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   73    73        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   75    75        Calcium 1 (By similarity). 
METAL   77    77        Calcium 1 (By similarity). 
METAL   197   197        Iron (heme axial ligand) (By similarity). 
METAL   198   198        Calcium 2 (By similarity). 
METAL   249   249        Calcium 2 (By similarity). 
METAL   252   252        Calcium 2 (By similarity). 
METAL   257   257        Calcium 2 (By similarity). 
BINDING   167   167        Substrate; via carbonyl oxygen (By similarity). 
SITE   63    63  1     Transition state stabilizer (By similarity). 
MOD_RES   26    26        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   293   293        N-linked (GlcNAc...) (Potential). 
CARBOHYD   315   315        N-linked (GlcNAc...) (Potential). 
DISULFID   36   119        By similarity. 
DISULFID   69    74        By similarity. 
DISULFID   125   325        By similarity. 
DISULFID   204   236        By similarity. 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 35756 Da [This is the MW of the unprocessed precursor] CRC64: EDD91B0099A6A2C2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARFDIVLLI GLCLIISVFP DTTTAQLSRG FYSKTCPNVE QIVRNAVQKK IKKTFVAVPA 

        70         80         90        100        110        120 
TLRLFFHDCF VNGCDASVMI QSTPKNKAEK DHPDNISLAG DGFDVVIQAK KALDSNPSCR 

       130        140        150        160        170        180 
NKVSCADILT LATRDVVVAA GGPSYEVELG RFDGLVSTAS SVEGNLPGPS DNVDKLNALF 

       190        200        210        220        230        240 
TKNKLTQEDM IALSAAHTLG FAHCGKVFKR IHKFNGINSV DPTLNKAYAI ELQKACPKNV 

       250        260        270        280        290        300 
DPRIAINMDP VTPKTFDNTY FKNLQQGKGL FTSDQVLFTD GRSRPTVNAW ASNSTAFNRA 

       310        320 
FVIAMTKLGR VGVKNSSNGN IRRDCGAFN 

Q96510 in FASTA format

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