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UniProtKB/Swiss-Prot entry Q9SI16


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

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Entry information
Entry name PER15_ARATH
Primary accession number Q9SI16
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 66)
Name and origin of the protein
Protein name Peroxidase 15 [Precursor]
Synonyms Atperox P15
EC 1.11.1.7
ATP36
Gene name
Name: PER15
Synonyms: P15
OrderedLocusNames: At2g18150
ORFNames: F8D23.7
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 [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.
[4]
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
AC007212; AAD31351.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY081298; AAL91187.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002557; AAO00917.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085060; AAM61616.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H84560; H84560.
RefSeq NP_179407.1; -.
UniGene At.28467
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q9SI16.
Protein family/group databases
PeroxiBase 96; AtPrx15.
Organism-specific databases
GeneFarm 1838; 61.
TAIR At2g18150; -.
Gene expression databases
ArrayExpress Q9SI16; -.
GermOnline AT2G18150; 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; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9SI16.
Genome annotation databases
GeneID 816328; -.
GenomeReviews CT485783_GR; AT2G18150.
KEGG ath:AT2G18150; -.
NMPDR fig|3702.1.peg.8809; -.
Other
ProtoNet Q9SI16.
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    22  22     Potential. 
CHAIN   23   338  316     Peroxidase 15. PRO_0000023681
ACT_SITE   76    76        Proton acceptor (By similarity). 
METAL   77    77        Calcium 1 (By similarity). 
METAL   80    80        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   82    82        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   84    84        Calcium 1 (By similarity). 
METAL   86    86        Calcium 1 (By similarity). 
METAL   203   203        Iron (heme axial ligand) (By similarity). 
METAL   204   204        Calcium 2 (By similarity). 
METAL   255   255        Calcium 2 (By similarity). 
METAL   258   258        Calcium 2 (By similarity). 
METAL   263   263        Calcium 2 (By similarity). 
BINDING   173   173        Substrate; via carbonyl oxygen (By similarity). 
SITE   72    72  1     Transition state stabilizer (By similarity). 
CARBOHYD   176   176        N-linked (GlcNAc...) (Potential). 
CARBOHYD   219   219        N-linked (GlcNAc...) (Potential). 
CARBOHYD   250   250        N-linked (GlcNAc...) (Potential). 
DISULFID   45   125        By similarity. 
DISULFID   78    83        By similarity. 
DISULFID   131   332        By similarity. 
DISULFID   210   242        By similarity. 
CONFLICT   14    14        I -> T (in Ref. 3; AAM61616). 
CONFLICT   21    21        I -> V (in Ref. 3; AAM61616). 
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 37079 Da [This is the MW of the unprocessed precursor] CRC64: 9496FE1962DEC27E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARIGSFLII LYLIYALTLC ICDDDESNYG GDKGNLFPGF YRSSCPRAEE IVRSVVAKAV 

        70         80         90        100        110        120 
ARETRMAASL MRLHFHDCFV QGCDGSLLLD TSGSIVTEKN SNPNSRSARG FEVVDEIKAA 

       130        140        150        160        170        180 
LENECPNTVS CADALTLAAR DSSVLTGGPS WMVPLGRRDS TSASLSGSNN NIPAPNNTFN 

       190        200        210        220        230        240 
TIVTRFNNQG LDLTDVVALS GSHTIGFSRC TSFRQRLYNQ SGNGSPDRTL EQSYAANLRQ 

       250        260        270        280        290        300 
RCPRSGGDQN LSELDINSAG RFDNSYFKNL IENMGLLNSD EVLFSSNEQS RELVKKYAED 

       310        320        330 
QEEFFEQFAE SMIKMGNISP LTGSSGEIRK NCRKINNS 

Q9SI16 in FASTA format

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