ID   CPI9_SOLTU              Reviewed;         222 AA.
AC   Q00652;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cysteine protease inhibitor 9;
DE   AltName: Full=PKIX;
DE   AltName: Full=pT1;
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. Irish Cobbler; TISSUE=Tuber;
RX   PubMed=1863783; DOI=10.1007/bf00039507;
RA   Yamagishi K., Mitsumori C., Kikuta Y.;
RT   "Nucleotide sequence of a cDNA encoding the putative trypsin inhibitor in
RT   potato tuber.";
RL   Plant Mol. Biol. 17:287-288(1991).
CC   -!- FUNCTION: Putative inhibitor of cysteine proteases. Does not inhibit
CC       papain. May protect the plant by inhibiting proteases of invading
CC       organisms.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Tuber.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:1863783 postulates an inhibition of trypsin but the
CC       sequence homology points to a cysteine protease inhibitor.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X56874; CAA40197.1; -; mRNA.
DR   PIR; S16575; S16575.
DR   AlphaFoldDB; Q00652; -.
DR   SMR; Q00652; -.
DR   MEROPS; I03.017; -.
DR   PRIDE; Q00652; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q00652; 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_0000016928"
FT   CHAIN           43..222
FT                   /note="Cysteine protease inhibitor 9"
FT                   /id="PRO_0000016929"
FT   MOTIF           29..34
FT                   /note="Vacuolar targeting signal"
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        185..191
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  24739 MW;  CE4F0EEAC5510665 CRC64;
     MKSINILSFL LLSSTLSLVA FARSFSSENP IVLPSTCHDD DNLVLPEVYD QDGHPLRIGQ
     RYIINNPLIG AGAVYLYNIG NLQCPNAVLQ HMSIPQFLGE GTPVVFVRKS ESDYGDVVRV
     MTGVYIKFFV KTTKLCVDQT VWKVNHEGLV VTGGQVGNEN DIFKIRKTDL VTPEGSKFVY
     KLLHCPSHLQ CKNIGGNFKN GYPRLVTVDD DKDFLPFVFI KA