PER64_ARATH
ID PER64_ARATH Reviewed; 317 AA.
AC Q43872;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Peroxidase 64;
DE Short=Atperox P64;
DE EC=1.11.1.7;
DE AltName: Full=ATP17a;
DE AltName: Full=PRXR4;
DE Flags: Precursor;
GN Name=PER64; Synonyms=P64; OrderedLocusNames=At5g42180; ORFNames=MJC20.29;
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 Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H.,
RA Simon P.;
RT "Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases.";
RL (er) Plant Gene Register PGR96-066(1996).
RN [2]
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 (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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 [7]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8425063; DOI=10.1007/bf00019954;
RA Trezzini G.F., Horrichs A., Somssich I.E.;
RT "Isolation of putative defense-related genes from Arabidopsis thaliana and
RT expression in fungal elicitor-treated cells.";
RL Plant Mol. Biol. 21:385-389(1993).
RN [8]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12172015; DOI=10.1105/tpc.003483;
RA Fowler S., Thomashow M.F.;
RT "Arabidopsis transcriptome profiling indicates that multiple regulatory
RT pathways are activated during cold acclimation in addition to the CBF cold
RT response pathway.";
RL Plant Cell 14:1675-1690(2002).
RN [9]
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 the whole plant, but preferentially in
CC roots.
CC -!- INDUCTION: Pathogen and elicitor-induced. Up-regulated transiently by a
CC cold treatment. {ECO:0000269|PubMed:12172015,
CC ECO:0000269|PubMed:8425063}.
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; X98316; CAA66960.1; -; mRNA.
DR EMBL; X99096; CAA67550.1; -; mRNA.
DR EMBL; AB017067; BAB08451.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94776.1; -; Genomic_DNA.
DR EMBL; AY063962; AAL36318.1; -; mRNA.
DR EMBL; AY096403; AAM20043.1; -; mRNA.
DR RefSeq; NP_199033.1; NM_123583.4.
DR AlphaFoldDB; Q43872; -.
DR SMR; Q43872; -.
DR STRING; 3702.AT5G42180.1; -.
DR PeroxiBase; 230; AtPrx64.
DR iPTMnet; Q43872; -.
DR PaxDb; Q43872; -.
DR PRIDE; Q43872; -.
DR ProteomicsDB; 236452; -.
DR EnsemblPlants; AT5G42180.1; AT5G42180.1; AT5G42180.
DR GeneID; 834223; -.
DR Gramene; AT5G42180.1; AT5G42180.1; AT5G42180.
DR KEGG; ath:AT5G42180; -.
DR Araport; AT5G42180; -.
DR TAIR; locus:2165820; AT5G42180.
DR eggNOG; ENOG502QSER; Eukaryota.
DR HOGENOM; CLU_010543_0_3_1; -.
DR InParanoid; Q43872; -.
DR OMA; YDHTCPH; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q43872; -.
DR BioCyc; ARA:AT5G42180-MON; -.
DR PRO; PR:Q43872; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q43872; baseline and differential.
DR Genevisible; Q43872; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235; PTHR31235; 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; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..317
FT /note="Peroxidase 64"
FT /id="PRO_0000023729"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
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 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 188
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 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 59
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 65..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 117..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 195..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 317 AA; 34706 MW; 79536112BA918690 CRC64;
MNAHMLNLLV IVIFVVSFDV QALSPHYYDH TCPQADHIVT NAVKKAMSND QTVPAALLRM
HFHDCFVRGC DGSVLLDSKG KNKAEKDGPP NISLHAFYVI DNAKKALEEQ CPGIVSCADI
LSLAARDAVA LSGGPTWAVP KGRKDGRISK AIETRQLPAP TFNISQLRQN FGQRGLSMHD
LVALSGGHTL GFAHCSSFQN RLHKFNTQKE VDPTLNPSFA ARLEGVCPAH NTVKNAGSNM
DGTVTSFDNI YYKMLIQGKS LFSSDESLLA VPSTKKLVAK YANSNEEFER AFVKSMIKMS
SISGNGNEVR LNCRRVR
