PER4_ARATH
ID PER4_ARATH Reviewed; 315 AA.
AC Q9LE15;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peroxidase 4;
DE Short=Atperox P4;
DE EC=1.11.1.7;
DE AltName: Full=ATP46;
DE Flags: Precursor;
GN Name=PER4; Synonyms=P4; OrderedLocusNames=At1g14540;
GN ORFNames=F14L17.32, T5E21.4;
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 [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 [2]
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 [3]
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 -!- 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; AC010657; AAF63178.1; -; Genomic_DNA.
DR EMBL; AC012188; AAF43954.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29178.1; -; Genomic_DNA.
DR RefSeq; NP_172906.1; NM_101321.4.
DR AlphaFoldDB; Q9LE15; -.
DR SMR; Q9LE15; -.
DR STRING; 3702.AT1G14540.1; -.
DR PeroxiBase; 80; AtPrx04.
DR PaxDb; Q9LE15; -.
DR PRIDE; Q9LE15; -.
DR ProteomicsDB; 236305; -.
DR EnsemblPlants; AT1G14540.1; AT1G14540.1; AT1G14540.
DR GeneID; 838016; -.
DR Gramene; AT1G14540.1; AT1G14540.1; AT1G14540.
DR KEGG; ath:AT1G14540; -.
DR Araport; AT1G14540; -.
DR TAIR; locus:2012597; AT1G14540.
DR eggNOG; ENOG502QSXF; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; Q9LE15; -.
DR OMA; CLTFKGR; -.
DR OrthoDB; 986353at2759; -.
DR PhylomeDB; Q9LE15; -.
DR BioCyc; ARA:AT1G14540-MON; -.
DR PRO; PR:Q9LE15; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LE15; baseline and differential.
DR Genevisible; Q9LE15; 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; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
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; 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 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..315
FT /note="Peroxidase 4"
FT /id="PRO_0000023670"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 65
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 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 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 57
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P00434,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 63..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 116..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 195..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 315 AA; 34411 MW; 2DE6FA79CD16836D CRC64;
MAIFKILVLL LSLCCFSQAQ LSPTFYDQTC QNALSTIRSS IRTAISRERR MAASLIRLHF
HDCFVNGCDA SVMLVATPTM ESERDSLANF QSARGFEVID QAKSAVESVC PGVVSCADII
AVAARDASEY VGGPRYDVKV GRRDSTNAFR AIADRDLPNF RASLNDLSEL FLRKGLNTRD
LVALSGAHTL GQAQCLTFKG RLYDNSSDID AGFSSTRKRR CPVNGGDTTL APLDQVTPNS
FDNNYYRNLM QKKGLLESDQ VLFGTGASTD SIVTEYSRNP SRFASDFSAA MIKMGDIQTL
TGSDGQIRRI CSAVN
