PER72_ARATH
ID PER72_ARATH Reviewed; 336 AA.
AC Q9FJZ9; Q43736;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxidase 72;
DE Short=Atperox P72;
DE EC=1.11.1.7;
DE AltName: Full=ATP6a;
DE AltName: Full=PRXR8;
DE Flags: Precursor;
GN Name=PER72; Synonyms=P72; OrderedLocusNames=At5g66390;
GN ORFNames=K1F13.4, K1L20.16;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RA Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
RT "Toward elucidating the global gene expression patterns of developing
RT Arabidopsis: parallel analysis of 8300 genes by a high-density
RT oligonucleotide probe array.";
RL Plant Physiol. Biochem. 39:221-242(2001).
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: Slightly expressed in roots. {ECO:0000269|Ref.7}.
CC -!- INDUCTION: Up-regulated transiently by a cold treatment.
CC {ECO:0000269|PubMed:12172015}.
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; X98320; CAA66964.1; -; mRNA.
DR EMBL; X98774; CAA67310.1; -; mRNA.
DR EMBL; AB013389; BAB10915.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98207.1; -; Genomic_DNA.
DR EMBL; BT008314; AAP37673.1; -; mRNA.
DR RefSeq; NP_201440.1; NM_126037.5.
DR AlphaFoldDB; Q9FJZ9; -.
DR SMR; Q9FJZ9; -.
DR STRING; 3702.AT5G66390.1; -.
DR PeroxiBase; 238; AtPrx72.
DR PaxDb; Q9FJZ9; -.
DR PRIDE; Q9FJZ9; -.
DR ProteomicsDB; 236301; -.
DR EnsemblPlants; AT5G66390.1; AT5G66390.1; AT5G66390.
DR GeneID; 836771; -.
DR Gramene; AT5G66390.1; AT5G66390.1; AT5G66390.
DR KEGG; ath:AT5G66390; -.
DR Araport; AT5G66390; -.
DR TAIR; locus:2154925; AT5G66390.
DR eggNOG; ENOG502QR5A; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; Q9FJZ9; -.
DR OMA; YCRKVNA; -.
DR OrthoDB; 820366at2759; -.
DR PhylomeDB; Q9FJZ9; -.
DR BioCyc; ARA:AT5G66390-MON; -.
DR PRO; PR:Q9FJZ9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJZ9; baseline and differential.
DR Genevisible; Q9FJZ9; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IDA: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; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
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; 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; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..336
FT /note="Peroxidase 72"
FT /id="PRO_0000023737"
FT ACT_SITE 73
FT /note="Proton acceptor"
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 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 200
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 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 69
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 75..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 128..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 207..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 151
FT /note="P -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="K -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37427 MW; 4DAD91C4693A0833 CRC64;
MAKSLNILIA ALSLIAFSPF CLCSKAYGSG GYLFPQFYDQ SCPKAQEIVQ SIVAKAFEHD
PRMPASLLRL HFHDCFVKGC DASILLDSSG TIISEKRSNP NRNSARGFEL IEEIKHALEQ
ECPETVSCAD ILALAARDST VITGGPSWEV PLGRRDARGA SLSGSNNDIP APNNTFQTIL
TKFKRQGLDL VDLVSLSGSH TIGNSRCTSF RQRLYNQSGN GKPDMTLSQY YATLLRQRCP
RSGGDQTLFF LDFATPFKFD NHYFKNLIMY KGLLSSDEIL FTKNKQSKEL VELYAENQEA
FFEQFAKSMV KMGNISPLTG AKGEIRRICR RVNHAY
