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UniProtKB/Swiss-Prot entry Q9LXG3


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

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Entry information
Entry name PER56_ARATH
Primary accession number Q9LXG3
Secondary accession number Q41955
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 64)
Name and origin of the protein
Protein name Peroxidase 56 [Precursor]
Synonyms Atperox P56
EC 1.11.1.7
ATP33
Gene name
Name: PER56
Synonyms: P56
OrderedLocusNames: At5g15180
ORFNames: F8M21_70
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=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[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] OF 3-136.
STRAIN=cv. Columbia;
TISSUE=Seedling;
DOI=10.1046/j.1365-313X.1993.04061051.x; PubMed=8281187 [NCBI, ExPASy, EBI, Israel, Japan]
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana.";
Plant J. 4:1051-1061(1993).
[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
AL353993; CAB89328.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY072172; AAL59994.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142591; AAN13160.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z18075; CAA79097.2; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T49953; T49953.
RefSeq NP_197022.1; -.
UniGene At.43105
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q9LXG3.
Protein family/group databases
PeroxiBase 222; AtPrx56.
Organism-specific databases
GeneFarm 1911; 61.
TAIR At5g15180; -.
Gene expression databases
ArrayExpress Q9LXG3; -.
GermOnline AT5G15180; 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 Q9LXG3.
Genome annotation databases
GeneID 831370; -.
GenomeReviews BA000015_GR; AT5G15180.
KEGG ath:AT5G15180; -.
NMPDR fig|3702.1.peg.23655; -.
Other
ProtoNet Q9LXG3.
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    31  31     Potential. 
CHAIN   32   329  298     Peroxidase 56. PRO_0000023721
ACT_SITE   72    72        Proton acceptor (By similarity). 
METAL   73    73        Calcium 1 (By similarity). 
METAL   76    76        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   78    78        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   80    80        Calcium 1 (By similarity). 
METAL   82    82        Calcium 1 (By similarity). 
METAL   197   197        Iron (heme axial ligand) (By similarity). 
METAL   198   198        Calcium 2 (By similarity). 
METAL   248   248        Calcium 2 (By similarity). 
METAL   251   251        Calcium 2 (By similarity). 
METAL   256   256        Calcium 2 (By similarity). 
BINDING   167   167        Substrate; via carbonyl oxygen (By similarity). 
SITE   68    68  1     Transition state stabilizer (By similarity). 
CARBOHYD   158   158        N-linked (GlcNAc...) (Potential). 
CARBOHYD   172   172        N-linked (GlcNAc...) (Potential). 
CARBOHYD   213   213        N-linked (GlcNAc...) (Potential). 
DISULFID   41   119        By similarity. 
DISULFID   74    79        By similarity. 
DISULFID   125   325        By similarity. 
DISULFID   204   236        By similarity. 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 36225 Da [This is the MW of the unprocessed precursor] CRC64: F50082FECD9FB644 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAALKMTISC FLFLQVIYCL LSSFAPTNVQ GLKVGFYDKA CPKAELIVKK SVFEAVKNDR 

        70         80         90        100        110        120 
TIAAPLLRMF FHDCFVRGCE GSVLLELKNK KDEKNSIPNL TLRGFEIIDN VKAALEKECP 

       130        140        150        160        170        180 
GIVSCSDVLA LVARDAMVAL NGPSWEVETG RRDGLVTNIT EALLNLPSPF NNISSLITQF 

       190        200        210        220        230        240 
QSKGLDKKDL VVLSGGHTIG NGHCPQITNR LYNFTGKGDS DPNLDTEYAV KLRGKCKPTD 

       250        260        270        280        290        300 
TTTALEMDPG SFKTFDESYF KLVSQRRGLF QSDAALLDNQ ETKSYVLKSL NSDGSTFFKD 

       310        320 
FGVSMVKMGR IGVLTGQVGE VRKKCRMVN 

Q9LXG3 in FASTA format

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