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UniProtKB/Swiss-Prot entry Q96519


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

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Entry information
Entry name PER11_ARATH
Primary accession number Q96519
Secondary accession number P93723
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 69)
Name and origin of the protein
Protein name Peroxidase 11 [Precursor]
Synonyms Atperox P11
EC 1.11.1.7
ATP23a/ATP23b
Gene name
Name: PER11
Synonyms: P11
OrderedLocusNames: At1g68850
ORFNames: T6L1.4, F14K14.4
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., Jensen R.B., Hansen L.N., Rasmussen S.K.;
"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(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.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).
[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
Y08782; CAA70035.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11789; CAA72485.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011914; AAG52033.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011665; AAG51588.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C96713; C96713.
RefSeq NP_564948.1; -.
UniGene At.87
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q96519.
Protein family/group databases
PeroxiBase 92; AtPrx11.
Organism-specific databases
GeneFarm 1473; 61.
TAIR At1g68850; -.
Gene expression databases
GermOnline AT1G68850; 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:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
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).
GO:0048511; Biological process: rhythmic process (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).
BLOCKS Q96519.
ProtoNet Q96519.
Genome annotation databases
GeneID 843218; -.
GenomeReviews CT485782_GR; AT1G68850.
KEGG ath:AT1G68850; -.
NMPDR fig|3702.1.peg.6343; -.
Other
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    20  20     Potential. 
CHAIN   21   336  316     Peroxidase 11. PRO_0000023677
ACT_SITE   70    70        Proton acceptor (By similarity). 
METAL   71    71        Calcium 1 (By similarity). 
METAL   74    74        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   76    76        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   78    78        Calcium 1 (By similarity). 
METAL   80    80        Calcium 1 (By similarity). 
METAL   197   197        Iron (heme axial ligand) (By similarity). 
METAL   198   198        Calcium 2 (By similarity). 
METAL   251   251        Calcium 2 (By similarity). 
METAL   254   254        Calcium 2 (By similarity). 
METAL   259   259        Calcium 2 (By similarity). 
BINDING   167   167        Substrate; via carbonyl oxygen (By similarity). 
SITE   66    66  1     Transition state stabilizer (By similarity). 
CARBOHYD   246   246        N-linked (GlcNAc...) (Potential). 
DISULFID   39   119        By similarity. 
DISULFID   72    77        By similarity. 
DISULFID   125   331        By similarity. 
DISULFID   204   236        By similarity. 
CONFLICT   192   194        ALI -> YLL (in Ref. 1; CAA72485). 
CONFLICT   218   218        T -> M (in Ref. 1; CAA72485). 
Sequence information
Length: 336 AA [This is the length of the unprocessed precursor] Molecular weight: 37313 Da [This is the MW of the unprocessed precursor] CRC64: 846D69A84530900B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMRLLFVFFM VHTIFIPCFS FDTPGKDLPL TLDYYKSTCP TVFDVIKKEM ECIVKEDPRN 

        70         80         90        100        110        120 
AAIIIRLHFH DCFVQGCDGS VLLDETETLQ GEKKASPNIN SLKGYKIVDR IKNIIESECP 

       130        140        150        160        170        180 
GVVSCADLLT IGARDATILV GGPYWDVPVG RKDSKTASYE LATTNLPTPE EGLISIIAKF 

       190        200        210        220        230        240 
YSQGLSVEDM VALIGAHTIG KAQCRNFRSR IYGDFQVTSA LNPVSETYLA SLREICPASS 

       250        260        270        280        290        300 
GEGDSNVTAI DNVTPNLFDN SIYHTLLRGE GLLNSDQEMY TSLFGIQTRR IVSKYAEDPV 

       310        320        330 
AFFEQFSKSM VKMGNILNSE SLADGEVRRN CRFVNT 

Q96519 in FASTA format

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