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UniProtKB/Swiss-Prot entry Q9SJZ2


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

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Entry information
Entry name PER17_ARATH
Primary accession number Q9SJZ2
Secondary accession number P93725
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 65)
Name and origin of the protein
Protein name Peroxidase 17 [Precursor]
Synonyms Atperox P17
EC 1.11.1.7
ATP25a
Gene name
Name: PER17
Synonyms: P17
OrderedLocusNames: At2g22420
ORFNames: F14M13.18
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=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 227-329.
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.
[4]
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).
[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
AC006592; AAD22357.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT004021; AAO42057.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT005050; AAO50583.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11790; CAA72486.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D84612; D84612.
RefSeq NP_179828.1; -.
UniGene At.24416
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q9SJZ2.
Protein family/group databases
PeroxiBase 98; AtPrx17.
Organism-specific databases
GeneFarm 1841; 61.
TAIR At2g22420; -.
Gene expression databases
ArrayExpress Q9SJZ2; -.
GermOnline AT2G22420; Arabidopsis thaliana.
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; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9SJZ2.
ProtoNet Q9SJZ2.
Genome annotation databases
GeneID 816773; -.
GenomeReviews CT485783_GR; AT2G22420.
KEGG ath:AT2G22420; -.
NMPDR fig|3702.1.peg.9260; -.
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; Secreted; Signal; Vacuole.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     Potential. 
CHAIN   20   329  310     Peroxidase 17. PRO_0000023683
ACT_SITE   63    63        Proton acceptor (By similarity). 
METAL   64    64        Calcium 1 (By similarity). 
METAL   67    67        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   69    69        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   71    71        Calcium 1 (By similarity). 
METAL   73    73        Calcium 1 (By similarity). 
METAL   190   190        Iron (heme axial ligand) (By similarity). 
METAL   191   191        Calcium 2 (By similarity). 
METAL   242   242        Calcium 2 (By similarity). 
METAL   244   244        Calcium 2 (By similarity). 
METAL   249   249        Calcium 2 (By similarity). 
BINDING   160   160        Substrate; via carbonyl oxygen (By similarity). 
SITE   59    59  1     Transition state stabilizer (By similarity). 
CARBOHYD   165   165        N-linked (GlcNAc...) (Potential). 
CARBOHYD   177   177        N-linked (GlcNAc...) (Potential). 
CARBOHYD   206   206        N-linked (GlcNAc...) (Potential). 
CARBOHYD   236   236        N-linked (GlcNAc...) (Potential). 
DISULFID   32   112        By similarity. 
DISULFID   65    70        By similarity. 
DISULFID   118   315        By similarity. 
DISULFID   197   229        By similarity. 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 36670 Da [This is the MW of the unprocessed precursor] CRC64: 6BF861DE592968BA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLLPHLILY LTLLTVVVTG ETLRPRFYSE TCPEAESIVR REMKKAMIKE ARSVASVMRF 

        70         80         90        100        110        120 
QFHDCFVNGC DASLLLDDTP NMLGEKLSLS NIDSLRSFEV VDDIKEALEK ACPATVSCAD 

       130        140        150        160        170        180 
IVIMAARDAV ALTGGPDWEV KLGRKDSLTA SQQDSDDIMP SPRANATFLI DLFERFNLSV 

       190        200        210        220        230        240 
KDMVALSGSH SIGQGRCFSI MFRLYNQSGS GKPDPALEPS YRKKLDKLCP LGGDENVTGD 

       250        260        270        280        290        300 
LDATPQVFDN QYFKDLVSGR GFLNSDQTLY TNLVTREYVK MFSEDQDEFF RAFAEGMVKL 

       310        320 
GDLQSGRPGE IRFNCRVVNR RPIDVLLVS 

Q9SJZ2 in FASTA format

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