PER16_ARATH
ID PER16_ARATH Reviewed; 323 AA.
AC Q96518;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxidase 16;
DE Short=Atperox P16;
DE EC=1.11.1.7;
DE AltName: Full=ATP22a;
DE Flags: Precursor;
GN Name=PER16; Synonyms=P16; OrderedLocusNames=At2g18980; ORFNames=F19F24.18;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-323.
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 (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 and leaves. {ECO:0000269|Ref.6}.
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; AC003673; AAC09031.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06835.1; -; Genomic_DNA.
DR EMBL; BT003082; AAO23647.1; -; mRNA.
DR EMBL; Y08781; CAA70034.1; -; mRNA.
DR PIR; T01626; T01626.
DR RefSeq; NP_179488.1; NM_127455.4.
DR AlphaFoldDB; Q96518; -.
DR SMR; Q96518; -.
DR STRING; 3702.AT2G18980.1; -.
DR PeroxiBase; 97; AtPrx16.
DR PaxDb; Q96518; -.
DR PRIDE; Q96518; -.
DR ProteomicsDB; 236414; -.
DR EnsemblPlants; AT2G18980.1; AT2G18980.1; AT2G18980.
DR GeneID; 816415; -.
DR Gramene; AT2G18980.1; AT2G18980.1; AT2G18980.
DR KEGG; ath:AT2G18980; -.
DR Araport; AT2G18980; -.
DR TAIR; locus:2044485; AT2G18980.
DR eggNOG; ENOG502QUMM; Eukaryota.
DR HOGENOM; CLU_010543_0_3_1; -.
DR InParanoid; Q96518; -.
DR OMA; NTMFSSH; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q96518; -.
DR BioCyc; ARA:AT2G18980-MON; -.
DR PRO; PR:Q96518; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q96518; baseline and differential.
DR Genevisible; Q96518; 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 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; PTHR31517; PTHR31517; 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 Calcium; Disulfide bond; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..323
FT /note="Peroxidase 16"
FT /id="PRO_0000023682"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 66
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 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 191
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 192
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 246
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 SITE 61
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 34..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 67..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 119..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 198..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 323 AA; 35832 MW; 43880AD393482989 CRC64;
MKNQSSFSIV ALLLIFFSSS VFAQLQTNFY RKSCPNVETI VRNAVRQKFQ QTFVTAPATL
RLFFHDCFVR GCDASILLAS PSEKDHPDDK SLAGDGFDTV AKAKQALDRD PNCRNKVSCA
DILALATRDV VVLTGGPNYP VELGRRDGRL STVASVQHSL PQPSFKLDQL NTMFARHGLS
QTDMIALSGA HTIGFAHCGK FSKRIYNFSP KRPIDPTLNI RYALQLRQMC PIRVDLRIAI
NMDPTSPNTF DNAYFKNLQK GMGLFTSDQV LFSDERSRST VNSFASSEAT FRQAFISAIT
KLGRVGVKTG NAGEIRRDCS RVN
