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UniProtKB/Swiss-Prot entry Q43731


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

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Entry information
Entry name PER50_ARATH
Primary accession number Q43731
Secondary accession numbers Q96523 Q9SBA1
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 80)
Name and origin of the protein
Protein name Peroxidase 50 [Precursor]
Synonyms Atperox P50
EC 1.11.1.7
PRXR2
ATP9a
Gene name
Name: PER50
Synonyms: P50
OrderedLocusNames: At4g37520
ORFNames: F19F18.10, F6G17.9
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.
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
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).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-329.
STRAIN=cv. Columbia;
TISSUE=Leaf;
DOI=10.1016/S0167-4781(98)00205-X; PubMed=9838086 [NCBI, ExPASy, EBI, Israel, Japan]
Justesen A.F., Jespersen H.M., Welinder K.G.;
"Analysis of two incompletely spliced Arabidopsis cDNAs encoding novel types of peroxidase.";
Biochim. Biophys. Acta 1443:149-154(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-206.
Stracke R., Palme K.;
"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[7]
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).
[8]
CHARACTERIZATION.
STRAIN=cv. Columbia;
Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P., Penel C.;
"Identification and characterization of Ca(2+)-pectate binding peroxidases in Arabidopsis thaliana.";
J. Plant Physiol. 159:1165-1171(2002).
[9]
DEVELOPMENTAL STAGE.
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).
[10]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1073/pnas.97.21.11655; PubMed=11027363 [NCBI, ExPASy, EBI, Israel, Japan]
Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M.;
"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis.";
Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000).
[11]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1105/tpc.13.1.113; PubMed=11158533 [NCBI, ExPASy, EBI, Israel, Japan]
Schaffer R., Landgraf J., Accerbi M., Simon V., Larson M., Wisman E.;
"Microarray analysis of diurnal and circadian-regulated genes in Arabidopsis.";
Plant Cell 13:113-123(2001).
[12]
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
X98314; CAA66958.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035605; CAB38291.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161591; CAB80417.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035601; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AY062816; AAL32894.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY081577; AAM10139.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086567; AAM63630.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98856; CAA67362.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ006960; CAA07352.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083762; AAN60320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04709; T04709.
RefSeq NP_195468.1; -.
UniGene At.22541
3D structure databases
HSSP Q42578; 1PA2. [HSSP ENTRY / PDB]
ModBase Q43731.
Protein family/group databases
PeroxiBase 216; AtPrx50.
Organism-specific databases
GeneFarm 1882; 61.
TAIR At4g37520; -.
Gene expression databases
ArrayExpress Q43731; -.
GermOnline AT4G37520; 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 Q43731.
Genome annotation databases
GeneID 829907; -.
GenomeReviews CT486007_GR; AT4G37520.
KEGG ath:AT4G37520; -.
NMPDR fig|3702.1.peg.21863; -.
Other
ProtoNet Q43731.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Biological rhythms; Calcium; Complete proteome; Glycoprotein; 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    25  25     Potential. 
CHAIN   26   329  304     Peroxidase 50. PRO_0000023715
ACT_SITE   67    67        Proton acceptor (By similarity). 
METAL   68    68        Calcium 1 (By similarity). 
METAL   71    71        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   73    73        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   75    75        Calcium 1 (By similarity). 
METAL   77    77        Calcium 1 (By similarity). 
METAL   197   197        Iron (heme axial ligand) (By similarity). 
METAL   198   198        Calcium 2 (By similarity). 
METAL   249   249        Calcium 2 (By similarity). 
METAL   252   252        Calcium 2 (By similarity). 
METAL   257   257        Calcium 2 (By similarity). 
BINDING   167   167        Substrate; via carbonyl oxygen (By similarity). 
SITE   63    63  1     Transition state stabilizer (By similarity). 
MOD_RES   26    26        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   215   215        N-linked (GlcNAc...) (Potential). 
DISULFID   36   119        By similarity. 
DISULFID   69    74        By similarity. 
DISULFID   125   325        By similarity. 
DISULFID   204   236        By similarity. 
CONFLICT   109   109        A -> T (in Ref. 4; AAM63630). 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 36076 Da [This is the MW of the unprocessed precursor] CRC64: 167FDDA36B279B1C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVVVNKTNLL LLLLSLCLTL DLSSAQLRRN FYAGSCPNVE QIVRNAVQKK VQQTFTTIPA 

        70         80         90        100        110        120 
TLRLYFHDCF VNGCDASVMI ASTNNNKAEK DHEENLSLAG DGFDTVIKAK EALDAVPNCR 

       130        140        150        160        170        180 
NKVSCADILT MATRDVVNLA GGPQYDVELG RLDGLSSTAA SVGGKLPHPT DDVNKLTSLF 

       190        200        210        220        230        240 
AKNGLSLNDM IALSGAHTLG FAHCTKVFNR IYTFNKTTKV DPTVNKDYVT ELKASCPRNI 

       250        260        270        280        290        300 
DPRVAINMDP TTPRQFDNVY YKNLQQGKGL FTSDQVLFTD RRSKPTVDLW ANNGQLFNQA 

       310        320 
FINSMIKLGR VGVKTGSNGN IRRDCGAFN 

Q43731 in FASTA format

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