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Peroxidase 50 (Atperox P50) (EC 1.11.1.7) (ATP9a) (PRXR2)

 PER50_ARATH             Reviewed;         329 AA.
Q43731; Q96523; Q9SBA1;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 151.
RecName: Full=Peroxidase 50;
Short=Atperox P50;
EC=1.11.1.7;
AltName: Full=ATP9a;
AltName: Full=PRXR2;
Flags: Precursor;
Name=PER50; Synonyms=P50; OrderedLocusNames=At4g37520;
ORFNames=F19F18.10, F6G17.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[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(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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]
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.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-329.
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=9838086; DOI=10.1016/S0167-4781(98)00205-X;
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).
[7]
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.
[8]
CHARACTERIZATION.
STRAIN=cv. Columbia;
PubMed=9738941; DOI=10.1016/S0014-5793(98)00849-7;
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).
[9]
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).
[10]
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).
[11]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=11027363; DOI=10.1073/pnas.97.21.11655;
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).
[12]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=11158533; DOI=10.1105/tpc.13.1.113;
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).
[13]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=12034502; DOI=10.1016/S0378-1119(02)00465-1;
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).
-!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
biosynthesis and degradation of lignin, suberization, auxin
catabolism, response to environmental stresses such as wounding,
pathogen attack and oxidative stress. These functions might be
dependent on each isozyme/isoform in each plant tissue.
-!- FUNCTION: Exhibits a Ca(2+)-pectate binding affinity which could
be interpreted in vivo as a specificity to interact with the
pectic structure of the cell wall.
-!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
radical of the donor + 2 H(2)O.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000255|PROSITE-ProRule:PRU00297};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00297};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-
ProRule:PRU00297}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q43731-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in roots and leaves.
-!- DEVELOPMENTAL STAGE: Up-regulated during leaf development.
{ECO:0000269|Ref.10}.
-!- INDUCTION: Enhanced expression in response of mechanical wounding.
Induced either by incompatible fungal pathogen attack, or by
methyl jasmonate, a plant defense-related signaling molecule.
Expressed under a diurnal rhythm (circadian clock control).
{ECO:0000269|PubMed:11027363, ECO:0000269|PubMed:11158533}.
-!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
-!- SIMILARITY: Belongs to the peroxidase family. Classical plant
(class III) peroxidase subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X98314; CAA66958.1; -; mRNA.
EMBL; AL035601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL035605; CAB38291.1; -; Genomic_DNA.
EMBL; AL161591; CAB80417.1; -; Genomic_DNA.
EMBL; CP002687; AEE86804.1; -; Genomic_DNA.
EMBL; AY062816; AAL32894.1; -; mRNA.
EMBL; AY081577; AAM10139.1; -; mRNA.
EMBL; AY086567; AAM63630.1; -; mRNA.
EMBL; X98856; CAA67362.1; -; Genomic_DNA.
EMBL; AJ006960; CAA07352.1; -; Genomic_DNA.
EMBL; AF083762; AAN60320.1; -; mRNA.
PIR; T04709; T04709.
RefSeq; NP_195468.1; NM_119916.4. [Q43731-1]
UniGene; At.22541; -.
ProteinModelPortal; Q43731; -.
SMR; Q43731; -.
BioGrid; 15188; 1.
IntAct; Q43731; 1.
STRING; 3702.AT4G37520.1; -.
PeroxiBase; 216; AtPrx50.
PaxDb; Q43731; -.
EnsemblPlants; AT4G37520.1; AT4G37520.1; AT4G37520. [Q43731-1]
GeneID; 829907; -.
Gramene; AT4G37520.1; AT4G37520.1; AT4G37520.
KEGG; ath:AT4G37520; -.
Araport; AT4G37520; -.
TAIR; locus:2120051; AT4G37520.
eggNOG; ENOG410IJ72; Eukaryota.
eggNOG; ENOG4111FDS; LUCA.
HOGENOM; HOG000237556; -.
InParanoid; Q43731; -.
KO; K00430; -.
OMA; RIYTFNK; -.
OrthoDB; EOG09360FB9; -.
PhylomeDB; Q43731; -.
BioCyc; ARA:AT4G37520-MONOMER; -.
PRO; PR:Q43731; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q43731; baseline and differential.
Genevisible; Q43731; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
CDD; cd00693; secretory_peroxidase; 1.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR000823; Peroxidase_pln.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
InterPro; IPR033905; Secretory_peroxidase.
Pfam; PF00141; peroxidase; 1.
PRINTS; PR00458; PEROXIDASE.
PRINTS; PR00461; PLPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
Alternative splicing; Biological rhythms; Calcium; Complete proteome;
Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
Metal-binding; Oxidoreductase; Peroxidase; Reference proteome;
Secreted; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 329 Peroxidase 50.
/FTId=PRO_0000023715.
ACT_SITE 67 67 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 68 68 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 71 71 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 73 73 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 75 75 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 77 77 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 197 197 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 198 198 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 249 249 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 252 252 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 257 257 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
BINDING 167 167 Substrate; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
SITE 63 63 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 119 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 69 74 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 125 325 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 204 236 {ECO:0000255|PROSITE-ProRule:PRU00297}.
CONFLICT 109 109 A -> T (in Ref. 5; AAM63630).
{ECO:0000305}.
SEQUENCE 329 AA; 36076 MW; 167FDDA36B279B1C CRC64;
MVVVNKTNLL LLLLSLCLTL DLSSAQLRRN FYAGSCPNVE QIVRNAVQKK VQQTFTTIPA
TLRLYFHDCF VNGCDASVMI ASTNNNKAEK DHEENLSLAG DGFDTVIKAK EALDAVPNCR
NKVSCADILT MATRDVVNLA GGPQYDVELG RLDGLSSTAA SVGGKLPHPT DDVNKLTSLF
AKNGLSLNDM IALSGAHTLG FAHCTKVFNR IYTFNKTTKV DPTVNKDYVT ELKASCPRNI
DPRVAINMDP TTPRQFDNVY YKNLQQGKGL FTSDQVLFTD RRSKPTVDLW ANNGQLFNQA
FINSMIKLGR VGVKTGSNGN IRRDCGAFN


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