ID   IP25_SOLTU              Reviewed;         154 AA.
AC   Q41488;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Proteinase inhibitor type-2 P303.51;
DE   AltName: Full=Proteinase inhibitor type II P303.51;
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 [MRNA].
RC   STRAIN=cv. Bintje; TISSUE=Tuber;
RX   AGRICOLA=IND20549554; DOI=10.1007/BF01249702;
RA   Jongsma M.A., Bakker P.L., Stiekema W.J., Bosch D.D.;
RT   "Phage display of a double-headed proteinase inhibitor: analysis of the
RT   binding domains of potato proteinase inhibitor II.";
RL   Mol. Breed. 1:181-191(1995).
CC   -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC       proteinase inhibitor) family. {ECO:0000305}.
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DR   EMBL; L37519; AAA53278.1; -; mRNA.
DR   AlphaFoldDB; Q41488; -.
DR   SMR; Q41488; -.
DR   STRING; 4113.PGSC0003DMT400011562; -.
DR   MEROPS; I20.001; -.
DR   PRIDE; Q41488; -.
DR   eggNOG; ENOG502R7RQ; Eukaryota.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q41488; 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..154
FT                   /note="Proteinase inhibitor type-2 P303.51"
FT                   /id="PRO_0000025316"
FT   REPEAT          31..87
FT                   /note="1"
FT   REPEAT          88..147
FT                   /note="2"
FT   SITE            36..37
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000305"
FT   SITE            93..94
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000305"
FT   DISULFID        34..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..139
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   154 AA;  16660 MW;  AF0BFD1F26E6F224 CRC64;
     MAVHKEVNFV AYLLIVLGLL VLVSAMEHVD AKACTLECGN LGFGICPRSE GSPENRICTN
     CCAGYKGCNY YSANGAFICE GESDPKKPKA CPRNCDPHIA YSKCPRSEGK SLIYPTGCTT
     CCTGYKGCYY FGKNGKFVCE GESDEPKANM YPAM