ID   SPI5_SOLTU              Reviewed;         213 AA.
AC   Q41484;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Serine protease inhibitor 5;
DE   AltName: Full=gCDI-B1;
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], AND PROTEIN SEQUENCE OF 29-38.
RX   PubMed=8069493;
RA   Ishikawa A., Ohta S., Matsuoka K., Hattori T., Nakamura K.;
RT   "A family of potato genes that encode Kunitz-type proteinase inhibitors:
RT   structural comparisons and differential expression.";
RL   Plant Cell Physiol. 35:303-312(1994).
CC   -!- FUNCTION: Inhibitor of trypsin (serine protease). Protects the plant by
CC       inhibiting proteases of invading organisms (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   EMBL; D17332; BAA04152.1; -; Genomic_DNA.
DR   PIR; T07414; T07414.
DR   AlphaFoldDB; Q41484; -.
DR   SMR; Q41484; -.
DR   MEROPS; I03.020; -.
DR   PRIDE; Q41484; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q41484; baseline.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00178; STI; 1.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   InterPro; IPR002160; Prot_inh_Kunz-lg.
DR   PANTHER; PTHR33107; PTHR33107; 1.
DR   Pfam; PF00197; Kunitz_legume; 1.
DR   PRINTS; PR00291; KUNITZINHBTR.
DR   SMART; SM00452; STI; 1.
DR   SUPFAM; SSF50386; SSF50386; 1.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Serine protease inhibitor; Signal; Vacuole.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   PROPEP          23..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016904"
FT   CHAIN           29..213
FT                   /note="Serine protease inhibitor 5"
FT                   /id="PRO_0000016905"
FT   MOTIF           25..30
FT                   /note="Vacuolar targeting signal"
FT                   /evidence="ECO:0000250"
FT   SITE            95..96
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            143..144
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        174..183
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23137 MW;  0AECA41392A69422 CRC64;
     MKCLFLLCLC LVPIVVFSST FTSQNPINLP SDATPVLDVT GKELDPRLSY RIISIGRGAL
     GGDVYLGKSP NSDAPCANGV FRFNSDVGPS GTPVRFIGSS SHFGPHIFEG ELLNIQFDIS
     TVKLCVSYTI WKVGDYDASL GTMLLETGGT IGQADSSWFK IVKSSQLGYN LLYCPFSSDD
     QFCLKVGVVH QNGKRRLALV KDNPLDVSFK QVQ