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UniProtKB/Swiss-Prot entry Q96518


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

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Entry information
Entry name PER16_ARATH
Primary accession number Q96518
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on November 1, 1998 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 69)
Name and origin of the protein
Protein name Peroxidase 16 [Precursor]
Synonyms Atperox P16
EC 1.11.1.7
ATP22a
Gene name
Name: PER16
Synonyms: P16
OrderedLocusNames: At2g18980
ORFNames: F19F24.18
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 1: Evidence at protein 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 2-323.
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 (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
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).
[6]
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
AC003673; AAC09031.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT003082; AAO23647.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y08781; CAA70034.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T01626; T01626.
RefSeq NP_179488.1; -.
UniGene At.86
3D structure databases
HSSP Q42578; 1PA2. [HSSP ENTRY / PDB]
ModBase Q96518.
Protein family/group databases
PeroxiBase 97; AtPrx16.
Organism-specific databases
GeneFarm 1840; 61.
TAIR At2g18980; -.
Gene expression databases
ArrayExpress Q96518; -.
GermOnline AT2G18980; 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 Q96518.
Genome annotation databases
GeneID 816415; -.
GenomeReviews CT485783_GR; AT2G18980.
KEGG ath:AT2G18980; -.
NMPDR fig|3702.1.peg.8895; -.
Other
ProtoNet Q96518.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; 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    23  23     Potential. 
CHAIN   24   323  300     Peroxidase 16. PRO_0000023682
ACT_SITE   65    65        Proton acceptor (By similarity). 
METAL   66    66        Calcium 1 (By similarity). 
METAL   69    69        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   71    71        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   73    73        Calcium 1 (By similarity). 
METAL   75    75        Calcium 1 (By similarity). 
METAL   191   191        Iron (heme axial ligand) (By similarity). 
METAL   192   192        Calcium 2 (By similarity). 
METAL   243   243        Calcium 2 (By similarity). 
METAL   246   246        Calcium 2 (By similarity). 
METAL   251   251        Calcium 2 (By similarity). 
BINDING   161   161        Substrate; via carbonyl oxygen (By similarity). 
SITE   61    61  1     Transition state stabilizer (By similarity). 
MOD_RES   24    24        Pyrrolidone carboxylic acid (By similarity). 
DISULFID   34   113        By similarity. 
DISULFID   67    72        By similarity. 
DISULFID   119   319        By similarity. 
DISULFID   198   230        By similarity. 
Sequence information
Length: 323 AA [This is the length of the unprocessed precursor] Molecular weight: 35832 Da [This is the MW of the unprocessed precursor] CRC64: 43880AD393482989 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKNQSSFSIV ALLLIFFSSS VFAQLQTNFY RKSCPNVETI VRNAVRQKFQ QTFVTAPATL 

        70         80         90        100        110        120 
RLFFHDCFVR GCDASILLAS PSEKDHPDDK SLAGDGFDTV AKAKQALDRD PNCRNKVSCA 

       130        140        150        160        170        180 
DILALATRDV VVLTGGPNYP VELGRRDGRL STVASVQHSL PQPSFKLDQL NTMFARHGLS 

       190        200        210        220        230        240 
QTDMIALSGA HTIGFAHCGK FSKRIYNFSP KRPIDPTLNI RYALQLRQMC PIRVDLRIAI 

       250        260        270        280        290        300 
NMDPTSPNTF DNAYFKNLQK GMGLFTSDQV LFSDERSRST VNSFASSEAT FRQAFISAIT 

       310        320 
KLGRVGVKTG NAGEIRRDCS RVN 

Q96518 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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