PER2_SOLLC
ID PER2_SOLLC Reviewed; 363 AA.
AC P15004;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Suberization-associated anionic peroxidase 2;
DE EC=1.11.1.7;
DE AltName: Full=TMP2;
DE Flags: Precursor;
GN Name=TAP2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Castlemart II;
RX PubMed=2528055; DOI=10.1007/bf02464885;
RA Roberts E., Kolattukudy P.E.;
RT "Molecular cloning, nucleotide sequence, and abscisic acid induction of a
RT suberization-associated highly anionic peroxidase.";
RL Mol. Gen. Genet. 217:223-232(1989).
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 -!- FUNCTION: Suggested to catalyze the deposition of the aromatic residues
CC of suberin on the cell wall and thus play a role in cell-suberization.
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15854; CAA33853.1; -; Genomic_DNA.
DR PIR; S04764; S04764.
DR RefSeq; NP_001295320.1; NM_001308391.1.
DR AlphaFoldDB; P15004; -.
DR SMR; P15004; -.
DR STRING; 4081.Solyc02g079510.2.1; -.
DR Allergome; 1094; Sola l Peroxidase.
DR PeroxiBase; 7; LePrx75.
DR PaxDb; P15004; -.
DR PRIDE; P15004; -.
DR GeneID; 101245316; -.
DR KEGG; sly:101245316; -.
DR eggNOG; ENOG502QU1K; Eukaryota.
DR HOGENOM; CLU_010543_0_0_1; -.
DR InParanoid; P15004; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; P15004; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P15004; baseline and differential.
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; 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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..363
FT /note="Suberization-associated anionic peroxidase 2"
FT /id="PRO_0000023759"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 238
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 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 105
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 111..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 166..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 245..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 363 AA; 38547 MW; 438C4B98F991FAA2 CRC64;
MGFRLSLLSL AVSLVALALA GVAIYRNTYE AMIMNNGSLL QNISPDIDSL ESGEVSILIL
NDKKKNSDKY LSQQLTQESC VFSAVKGVVD SAIDNETRMG ASLIRLHFHD CFVDGCDGGI
LLDDINGTFT GEQNSPPNNN SVRGFEVIAQ AKQSVVDSCP NISVSCADIL AIAARDSLAK
LGGQTYTVAL GRSDATTANF SGAINQLPAP SDNLTVQIQK FSDKNFTVRE MVALAGAHTV
GFARCSTVCT SGNVNPAAQL QCNCSATLTD SDLQQLDTTP AVFDKVYYDN LNNNQGIMFS
DQVLTGNTTT AGFVTTYSNN VTVFLEDFAA AMIKMGNLPP SAGAQLEIRD VCSRVNPTSV
ASM
