ID   IP2T_SOLTU              Reviewed;         147 AA.
AC   Q41435;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Proteinase inhibitor type-2 T;
DE   AltName: Full=Proteinase inhibitor type II T;
DE   Flags: Precursor;
GN   Name=PIN2T;
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   Park S., Thornburg R.W.;
RT   "Isolation and characterization of a proteinase inhibitor II gene that is
RT   not wound-inducible.";
RL   (er) Plant Gene Register PGR96-007(1996).
CC   -!- FUNCTION: Inhibitor of trypsin and chymotrypsin.
CC   -!- INDUCTION: Not induced by wounding.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC       proteinase inhibitor) family. {ECO:0000305}.
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DR   EMBL; U45450; AAD09849.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q41435; -.
DR   SMR; Q41435; -.
DR   MEROPS; I20.003; -.
DR   PRIDE; Q41435; -.
DR   InParanoid; Q41435; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q41435; 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; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..147
FT                   /note="Proteinase inhibitor type-2 T"
FT                   /id="PRO_0000025315"
FT   REPEAT          25..82
FT                   /note="1"
FT   REPEAT          83..142
FT                   /note="2"
FT   SITE            30..31
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000305"
FT   SITE            87..88
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000305"
FT   DISULFID        28..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        115..133
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   147 AA;  15860 MW;  895D2F3102B8C2AE CRC64;
     MAVHKEVSFV AYLLIVLGMF LYVDALGCTK ECGNLGFGIC PRSEGSPTNP ICINCCSGYK
     GCNYYSAFGD LICQGESDPK NPKACPLNCD TNIAYSRCPR SEGKSLIYPT GCTTCCTGYK
     GCYYFGTNGK FVCEGESDEP KPYMSTA