ID   IP2X_SOLTU              Reviewed;         158 AA.
AC   Q00782;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Proteinase inhibitor type-2;
DE   AltName: Full=Proteinase inhibitor type II;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Russet Burbank-0;
RA   Choi Y., Moon Y., Lee J.S.;
RT   "Primary structure of two proteinase inhibitor II genes closely linked in
RT   the potato genome.";
RL   Korean J. Biochem. 23:214-220(1990).
CC   -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC       proteinase inhibitor) family. {ECO:0000305}.
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DR   EMBL; Z12753; CAA78277.1; -; Genomic_DNA.
DR   PIR; T07597; T07597.
DR   AlphaFoldDB; Q00782; -.
DR   SMR; Q00782; -.
DR   STRING; 4113.PGSC0003DMT400011563; -.
DR   PRIDE; Q00782; -.
DR   eggNOG; ENOG502R7RQ; Eukaryota.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q00782; baseline.
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   3: Inferred from homology;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..158
FT                   /note="Proteinase inhibitor type-2"
FT                   /id="PRO_0000025318"
FT   REPEAT          29..86
FT                   /note="1"
FT   REPEAT          87..146
FT                   /note="2"
FT   SITE            35..36
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000305"
FT   SITE            92..93
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000305"
FT   DISULFID        33..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..94
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        120..138
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   158 AA;  17132 MW;  C84DF44B015F248E CRC64;
     MAIHKEVSFL AYLLVLGMLL FVSAMEHVDA KACTLECGNL GYGICPRSEG SPENPICTNC
     CAGYKGCNYY SANGTFICEG QSHPKNPKAC PRNCDPHIAY SKCPRSGGKT LIYPTGCTTC
     CTGYTDCYYF GKDGKFVCEG ESIEPKACTL ECDSRLHT