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UniProtKB/Swiss-Prot entry Q43872


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

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Entry information
Entry name PER64_ARATH
Primary accession number Q43872
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 72)
Name and origin of the protein
Protein name Peroxidase 64 [Precursor]
Synonyms Atperox P64
EC 1.11.1.7
PRXR4
ATP17a
Gene name
Name: PER64
Synonyms: P64
OrderedLocusNames: At5g42180
ORFNames: MJC20.29
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 (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/6.3.183; PubMed=10470850 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[4]
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).
[5]
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).
[6]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1007/BF00019954; PubMed=8425063 [NCBI, ExPASy, EBI, Israel, Japan]
Trezzini G.F., Horrichs A., Somssich I.E.;
"Isolation of putative defense-related genes from Arabidopsis thaliana and expression in fungal elicitor-treated cells.";
Plant Mol. Biol. 21:385-389(1993).
[7]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1105/tpc.003483; PubMed=12172015 [NCBI, ExPASy, EBI, Israel, Japan]
Fowler S., Thomashow M.F.;
"Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway.";
Plant Cell 14:1675-1690(2002).
[8]
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
X98316; CAA66960.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X99096; CAA67550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB017067; BAB08451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY063962; AAL36318.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY096403; AAM20043.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_199033.1; -.
UniGene At.23304
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q43872.
Protein family/group databases
PeroxiBase 230; AtPrx64.
Organism-specific databases
GeneFarm 1923; 61.
TAIR At5g42180; -.
Gene expression databases
ArrayExpress Q43872; -.
GermOnline AT5G42180; 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; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q43872.
Genome annotation databases
GeneID 834223; -.
GenomeReviews BA000015_GR; AT5G42180.
KEGG ath:AT5G42180; -.
NMPDR fig|3702.1.peg.25939; -.
Other
ProtoNet Q43872.
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   317  295     Peroxidase 64. PRO_0000023729
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   188   188        Iron (heme axial ligand) (By similarity). 
METAL   189   189        Calcium 2 (By similarity). 
METAL   241   241        Calcium 2 (By similarity). 
METAL   243   243        Calcium 2 (By similarity). 
METAL   248   248        Calcium 2 (By similarity). 
BINDING   158   158        Substrate; via carbonyl oxygen (By similarity). 
SITE   59    59  1     Transition state stabilizer (By similarity). 
CARBOHYD   163   163        N-linked (GlcNAc...) (Potential). 
DISULFID   32   111        By similarity. 
DISULFID   65    70        By similarity. 
DISULFID   117   313        By similarity. 
DISULFID   195   227        By similarity. 
Sequence information
Length: 317 AA [This is the length of the unprocessed precursor] Molecular weight: 34706 Da [This is the MW of the unprocessed precursor] CRC64: 79536112BA918690 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNAHMLNLLV IVIFVVSFDV QALSPHYYDH TCPQADHIVT NAVKKAMSND QTVPAALLRM 

        70         80         90        100        110        120 
HFHDCFVRGC DGSVLLDSKG KNKAEKDGPP NISLHAFYVI DNAKKALEEQ CPGIVSCADI 

       130        140        150        160        170        180 
LSLAARDAVA LSGGPTWAVP KGRKDGRISK AIETRQLPAP TFNISQLRQN FGQRGLSMHD 

       190        200        210        220        230        240 
LVALSGGHTL GFAHCSSFQN RLHKFNTQKE VDPTLNPSFA ARLEGVCPAH NTVKNAGSNM 

       250        260        270        280        290        300 
DGTVTSFDNI YYKMLIQGKS LFSSDESLLA VPSTKKLVAK YANSNEEFER AFVKSMIKMS 

       310 
SISGNGNEVR LNCRRVR 

Q43872 in FASTA format

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