ID   PER2_CAPAN              Reviewed;          12 AA.
AC   P86000;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   11-DEC-2019, entry version 22.
DE   RecName: Full=Suberization-associated anionic peroxidase 2 {ECO:0000250|UniProtKB:P15004};
DE            EC=1.11.1.7;
DE   Flags: Fragment;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Sabater Jara A.B., Almagro L., Pedreno M.A.;
RL   Submitted (JUL-2008) to UniProtKB.
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. {ECO:0000305}.
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       {ECO:0000250|UniProtKB:P15004}.
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:0000250|UniProtKB:P15004,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:P15004, ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P15004,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P15004,
CC       ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15004,
CC       ECO:0000255|PROSITE-ProRule:PRU00297}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC       III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Secreted.
FT   CHAIN           <1..>12
FT                   /note="Suberization-associated anionic peroxidase 2"
FT                   /id="PRO_0000363729"
FT   UNSURE          7
FT                   /note="I or L"
FT   NON_TER         1
FT   NON_TER         12
SQ   SEQUENCE   12 AA;  1232 MW;  8F0767C441A05DC5 CRC64;
     GVVDSAIDAE TR