ID   CPI8_SOLTU              Reviewed;         221 AA.
AC   O24384;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cysteine protease inhibitor 8;
DE   AltName: Full=PCPI-8;
DE            Short=Pcpi8;
DE   Flags: Precursor; Fragment;
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. Ulster Sceptre; TISSUE=Tuber;
RX   PubMed=9207847; DOI=10.1023/a:1005853026333;
RA   Gruden K., Strukelj B., Ravnikar M., Poljsak-Prijatelj M., Mavric I.,
RA   Brzin J., Pungercar J., Kregar I.;
RT   "Potato cysteine proteinase inhibitor gene family: molecular cloning,
RT   characterisation and immunocytochemical localisation studies.";
RL   Plant Mol. Biol. 34:317-323(1997).
CC   -!- FUNCTION: Inhibitor of cysteine proteases. May protect the plant by
CC       inhibiting proteases of invading organisms.
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; U59273; AAB63250.1; -; mRNA.
DR   PIR; T07750; T07750.
DR   AlphaFoldDB; O24384; -.
DR   SMR; O24384; -.
DR   STRING; 4113.PGSC0003DMT400026289; -.
DR   MEROPS; I03.017; -.
DR   PRIDE; O24384; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; O24384; baseline and differential.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004869; F:cysteine-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   SMART; SM00452; STI; 1.
DR   SUPFAM; SSF50386; SSF50386; 1.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Signal;
KW   Thiol protease inhibitor; Vacuole.
FT   SIGNAL          <1..26
FT                   /evidence="ECO:0000250"
FT   PROPEP          27..42
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016926"
FT   CHAIN           43..221
FT                   /note="Cysteine protease inhibitor 8"
FT                   /id="PRO_0000016927"
FT   MOTIF           29..34
FT                   /note="Vacuolar targeting signal"
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..190
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   221 AA;  24694 MW;  A518E207D28F7A86 CRC64;
     IPSINILSFL LLSSTLSLVA FARSFTSENP IVLPTTCHDD DNLVLPEVYD QDGNPLRIGE
     RYIIKNPLLG AGAVYLDNIG NLQCPNAVLQ HMSIPQFLGK GTPVVFIRKS ESDYGDVVRL
     MTAVYIKFFV KTTKLCVDET VWKVNNEQLV VTGGNVGNEN DIFKIKKTDL VIRGMKNVYK
     LLHCPSHLEC KNIGSTFKNG YPRLVTVNDE KDFIPFVFIK A