PER11_ARATH
ID PER11_ARATH Reviewed; 336 AA.
AC Q96519; P93723;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peroxidase 11;
DE Short=Atperox P11;
DE EC=1.11.1.7;
DE AltName: Full=ATP23a/ATP23b;
DE Flags: Precursor;
GN Name=PER11; Synonyms=P11; OrderedLocusNames=At1g68850;
GN ORFNames=F14K14.4, T6L1.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F.,
RA Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N., Rasmussen S.K.;
RT "From expressed sequence tags to structure, function, evolution and
RT expression of 28 ER-targeted Arabidopsis peroxidases.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=9738941; DOI=10.1016/s0014-5793(98)00849-7;
RA Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
RT "Computational analyses and annotations of the Arabidopsis peroxidase gene
RT family.";
RL FEBS Lett. 433:98-102(1998).
RN [5]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11158533; DOI=10.2307/3871157;
RA Schaffer R., Landgraf J., Accerbi M., Simon V., Larson M., Wisman E.;
RT "Microarray analysis of diurnal and circadian-regulated genes in
RT Arabidopsis.";
RL Plant Cell 13:113-123(2001).
RN [6]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12034502; DOI=10.1016/s0378-1119(02)00465-1;
RA Tognolli M., Penel C., Greppin H., Simon P.;
RT "Analysis and expression of the class III peroxidase large gene family in
RT Arabidopsis thaliana.";
RL Gene 288:129-138(2002).
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems.
CC -!- INDUCTION: Expressed under a diurnal rhythm.
CC {ECO:0000269|PubMed:11158533}.
CC -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR EMBL; Y08782; CAA70035.1; -; mRNA.
DR EMBL; Y11789; CAA72485.1; -; mRNA.
DR EMBL; AC011665; AAG51588.1; -; Genomic_DNA.
DR EMBL; AC011914; AAG52033.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34850.1; -; Genomic_DNA.
DR PIR; C96713; C96713.
DR RefSeq; NP_564948.1; NM_105559.4.
DR AlphaFoldDB; Q96519; -.
DR SMR; Q96519; -.
DR BioGRID; 28439; 2.
DR STRING; 3702.AT1G68850.1; -.
DR PeroxiBase; 92; AtPrx11.
DR PaxDb; Q96519; -.
DR PRIDE; Q96519; -.
DR ProteomicsDB; 236296; -.
DR EnsemblPlants; AT1G68850.1; AT1G68850.1; AT1G68850.
DR GeneID; 843218; -.
DR Gramene; AT1G68850.1; AT1G68850.1; AT1G68850.
DR KEGG; ath:AT1G68850; -.
DR Araport; AT1G68850; -.
DR TAIR; locus:2012428; AT1G68850.
DR eggNOG; ENOG502QT8W; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; Q96519; -.
DR OMA; RCENFRD; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q96519; -.
DR BioCyc; ARA:AT1G68850-MON; -.
DR PRO; PR:Q96519; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q96519; baseline and differential.
DR Genevisible; Q96519; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388; PTHR31388; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Calcium; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..336
FT /note="Peroxidase 11"
FT /id="PRO_0000023677"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 197
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 66
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 72..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 125..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 204..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 192..194
FT /note="ALI -> YLL (in Ref. 1; CAA72485)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="T -> M (in Ref. 1; CAA72485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37313 MW; 846D69A84530900B CRC64;
MMRLLFVFFM VHTIFIPCFS FDTPGKDLPL TLDYYKSTCP TVFDVIKKEM ECIVKEDPRN
AAIIIRLHFH DCFVQGCDGS VLLDETETLQ GEKKASPNIN SLKGYKIVDR IKNIIESECP
GVVSCADLLT IGARDATILV GGPYWDVPVG RKDSKTASYE LATTNLPTPE EGLISIIAKF
YSQGLSVEDM VALIGAHTIG KAQCRNFRSR IYGDFQVTSA LNPVSETYLA SLREICPASS
GEGDSNVTAI DNVTPNLFDN SIYHTLLRGE GLLNSDQEMY TSLFGIQTRR IVSKYAEDPV
AFFEQFSKSM VKMGNILNSE SLADGEVRRN CRFVNT
