ID   IP23_SOLLC              Reviewed;         201 AA.
AC   Q43502;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Proteinase inhibitor type-2 CEVI57;
DE   AltName: Full=Proteinase inhibitor type II CEVI57;
DE   Flags: Precursor;
GN   Name=CEVI57;
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   STRAIN=cv. Rutgers; TISSUE=Leaf;
RX   PubMed=8672818; DOI=10.1094/mpmi-9-0409;
RA   Gadea J., Mayda E., Conejero V., Vera P.;
RT   "Characterization of defense-related genes ectopically expressed in viroid-
RT   infected tomato plants.";
RL   Mol. Plant Microbe Interact. 9:409-415(1996).
CC   -!- INDUCTION: By viroid infection.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC       proteinase inhibitor) family. {ECO:0000305}.
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DR   EMBL; X94946; CAA64416.1; -; mRNA.
DR   PIR; T07011; T07011.
DR   AlphaFoldDB; Q43502; -.
DR   SMR; Q43502; -.
DR   STRING; 4081.Solyc03g020050.2.1; -.
DR   MEROPS; I20.001; -.
DR   PaxDb; Q43502; -.
DR   PRIDE; Q43502; -.
DR   eggNOG; ENOG502R7RQ; Eukaryota.
DR   InParanoid; Q43502; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q43502; baseline and differential.
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; 3.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..201
FT                   /note="Proteinase inhibitor type-2 CEVI57"
FT                   /id="PRO_0000025312"
FT   REPEAT          27..83
FT                   /note="1"
FT   REPEAT          84..143
FT                   /note="2"
FT   REPEAT          144..199
FT                   /note="3"
FT   SITE            32..33
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000305"
FT   SITE            147..148
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000305"
FT   DISULFID        30..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..124
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..87
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        117..135
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  21419 MW;  A3FCAB93773D8590 CRC64;
     MAVYKVSFLA HLLVLGMYLL VSTVEHANAC TKECGNLGYG ICPGSEGSPE NPICTNCCSG
     YKGCNYYYAN GTFICEGTSD PKNPNICPSY CDPQIAYSKC PRSEGKTIIY PTGCTTCCTG
     YKGCYYFGQD GEFVCEGESI EPKGCTKECD PRVAYMTCPS SGLAKLNQVC VNCCSAGEGC
     KLYDNDGSLL CTGEPQSIST A