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UniProtKB/Swiss-Prot entry Q9LHB9


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

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Entry information
Entry name PER32_ARATH
Primary accession number Q9LHB9
Secondary accession numbers Q43732 Q6K1J2
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on February 5, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Peroxidase 32 [Precursor]
Synonyms Atperox P32
EC 1.11.1.7
PRXR3
ATP16a
Gene name
Name: PER32
Synonyms: P32
OrderedLocusNames: At3g32980
ORFNames: T15D2.7, T15D2.9
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;
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;
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 (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Tognolli M., Greppin H., Simon P.;
"Structure of the gene encoding Arabidopsis thaliana PRXR3 peroxidase.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
Nakamura Y.;
"Structural analysis of Arabidopsis thaliana chromosome 3. III.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[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]
CHARACTERIZATION.
STRAIN=cv. Columbia;
Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P., Penel C.;
"Identification and characterization of Ca(2+)-pectate binding peroxidases in Arabidopsis thaliana.";
J. Plant Physiol. 159:1165-1171(2002).
[9]
TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=9807821 [NCBI, ExPASy, EBI, Israel, Japan]
Ruan Y., Gilmore J., Conner T.;
"Towards Arabidopsis genome analysis: monitoring expression profiles of 1400 genes using cDNA microarrays.";
Plant J. 15:821-833(1998).
[10]
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).
[11]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1074/jbc.M104863200; PubMed=11748215 [NCBI, ExPASy, EBI, Israel, Japan]
Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C., Vingron M., Slusarenko A.J., Hoheisel J.D.;
"Monitoring the switch from housekeeping to pathogen defense metabolism in Arabidopsis thaliana using cDNA arrays.";
J. Biol. Chem. 277:10555-10561(2002).
[12]
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
X98315; CAA66959.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98777; CAA67313.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133036; CAB37193.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP002054; BAB02631.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY080608; AAL86292.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY133730; AAM91664.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087285; AAM64838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_850652.1; -.
UniGene At.47588
3D structure databases
HSSP P00433; 2ATJ. [HSSP ENTRY / PDB]
SMR Q9LHB9; 30-334.
ModBase Q9LHB9.
Protein family/group databases
PeroxiBase 198; AtPrx32.
Organism-specific databases
GeneFarm 1859; 61.
TAIR At3g32980; -.
Gene expression databases
ArrayExpress Q9LHB9; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005773; Cellular component: vacuole (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).
BLOCKS Q9LHB9.
ProtoNet Q9LHB9.
Genome annotation databases
GeneID 823067; -.
GenomeReviews BA000014_GR; AT3G32980.
KEGG ath:AT3G32980; -.
Other
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; Vacuole.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    29  29     Potential. 
CHAIN   30   352  323     Peroxidase 32. PRO_0000023698
ACT_SITE   71    71        Proton acceptor. 
METAL   72    72        Calcium 1 (By similarity). 
METAL   75    75        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   77    77        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   79    79        Calcium 1 (By similarity). 
METAL   81    81        Calcium 1 (By similarity). 
METAL   199   199        Iron (heme axial ligand) (By similarity). 
METAL   200   200        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   168   168        Substrate; via carbonyl oxygen (By similarity). 
SITE   67    67  1     Transition state stabilizer (By similarity). 
MOD_RES   30    30        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   86    86        N-linked (GlcNAc...) (Potential). 
CARBOHYD   215   215        N-linked (GlcNAc...) (Potential). 
CARBOHYD   227   227        N-linked (GlcNAc...) (Potential). 
CARBOHYD   243   243        N-linked (GlcNAc...) (Potential). 
CARBOHYD   284   284        N-linked (GlcNAc...) (Potential). 
DISULFID   40   120        By similarity. 
DISULFID   73    78        By similarity. 
DISULFID   126   330        By similarity. 
DISULFID   206   238        By similarity. 
CONFLICT   24    24        S -> L (in Ref. 1, 2, 3 and 6). 
CONFLICT   145   145        S -> Y (in Ref. 6; AAM64838). 
Sequence information
Length: 352 AA [This is the length of the unprocessed precursor] Molecular weight: 38847 Da [This is the MW of the unprocessed precursor] CRC64: 765696B3869BA1DB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNFSYSSLST WTTLMTLGCL LLHSSISSAQ LTPTFYDNTC PSVFTIVRDT IVNELRSDPR 

        70         80         90        100        110        120 
IAASILRLHF HDCFVNGCDA SILLDNTTSF RTEKDAAPNA NSARGFPVID RMKAAVETAC 

       130        140        150        160        170        180 
PRTVSCADIL TIAAQQAVNL AGGPSWRVPL GRRDSLQAFF ALANTNLPAP FFTLPQLKAS 

       190        200        210        220        230        240 
FQNVGLDRPS DLVALSGGHT FGKNQCQFIM DRLYNFSNTG LPDPTLNTTY LQTLRGQCPR 

       250        260        270        280        290        300 
NGNQTVLVDF DLRTPTVFDN KYYVNLKELK GLIQTDQELF SSPNATDTIP LVREYADGTQ 

       310        320        330        340        350 
KFFNAFVEAM NRMGNITPLT GTQGQIRQNC RVVNSNSLLH DVVEIVDFVS SM 

Q9LHB9 in FASTA format

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