ID   IP21_SOLLC              Reviewed;         148 AA.
AC   P05119;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Wound-induced proteinase inhibitor 2;
DE   AltName: Full=Wound-induced proteinase inhibitor II;
DE   Flags: Precursor;
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 [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=3838986; DOI=10.1016/s0021-9258(18)88818-4;
RA   Graham J.S., Pearce G., Merryweather J., Titani K., Ericsson L.H.,
RA   Ryan C.A.;
RT   "Wound-induced proteinase inhibitors from tomato leaves. II. The cDNA-
RT   deduced primary structure of pre-inhibitor II.";
RL   J. Biol. Chem. 260:6561-6564(1985).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 31-141 IN COMPLEX WITH SUBTILISIN.
RX   PubMed=12684499; DOI=10.1074/jbc.m302020200;
RA   Barrette-Ng I.H., Ng K.K.-S., Cherney M.M., Pearce G., Ryan C.A.,
RA   James M.N.G.;
RT   "Structural basis of inhibition revealed by a 1:2 complex of the two-headed
RT   tomato inhibitor-II and subtilisin Carlsberg.";
RL   J. Biol. Chem. 278:24062-24071(2003).
CC   -!- FUNCTION: Potent inhibitor of both trypsin and chymotrypsin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: Mechanical damage (i.e. insect chewing) to this plant
CC       results in the systemic release of a factor from the wound site. Within
CC       the leaves it induces the cytoplasmic synthesis of proteinase
CC       inhibitors I and II.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC       proteinase inhibitor) family. {ECO:0000305}.
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DR   EMBL; K03291; AAA34201.1; -; mRNA.
DR   PIR; B24048; B24048.
DR   PDB; 1OYV; X-ray; 2.50 A; I=26-148.
DR   PDB; 1PJU; X-ray; 2.15 A; A/B/C/D=26-148.
DR   PDBsum; 1OYV; -.
DR   PDBsum; 1PJU; -.
DR   AlphaFoldDB; P05119; -.
DR   SMR; P05119; -.
DR   MEROPS; I20.003; -.
DR   MEROPS; I20.953; -.
DR   PRIDE; P05119; -.
DR   EvolutionaryTrace; P05119; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P05119; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR003465; Prot_inh_I20.
DR   Pfam; PF02428; Prot_inhib_II; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Protease inhibitor; Reference proteome;
KW   Repeat; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..148
FT                   /note="Wound-induced proteinase inhibitor 2"
FT                   /id="PRO_0000025310"
FT   REPEAT          26..81
FT                   /note="1; trypsin-inhibitory"
FT   REPEAT          83..141
FT                   /note="2; chymotrypsin-inhibitory"
FT   SITE            30..31
FT                   /note="Reactive bond for trypsin"
FT   SITE            87..88
FT                   /note="Reactive bond for chymotrypsin"
FT   DISULFID        28..116
FT   DISULFID        32..112
FT   DISULFID        40..122
FT   DISULFID        52..89
FT   DISULFID        55..73
FT   DISULFID        56..85
FT   DISULFID        62..98
FT   DISULFID        115..133
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:1OYV"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:1OYV"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1OYV"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:1PJU"
FT   STRAND          131..134
FT                   /evidence="ECO:0007829|PDB:1PJU"
SQ   SEQUENCE   148 AA;  16293 MW;  468A2F653971AAFC CRC64;
     MAVHKEVNFV AYLLIVLGMF LYVDAKACTR ECGNLGFGIC PRSEGSPLNP ICINCCSGYK
     GCNYYNSFGK FICEGESDPK RPNACTFNCD PNIAYSRCPR SQGKSLIYPT GCTTCCTGYK
     GCYYFGKDGK FVCEGESDEP KANMYPVM