ID   CPI1_SOLTU              Reviewed;         222 AA.
AC   P20347; Q41497;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cysteine protease inhibitor 1;
DE   AltName: Full=P340;
DE   AltName: Full=P34021;
DE   AltName: Full=PCPI 8.3;
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] OF 3-222.
RC   STRAIN=cv. Bintje; TISSUE=Tuber;
RX   AGRICOLA=IND92000050; DOI=10.1007/BF00027383;
RA   Stiekema W.J., Heidekamp F., Dirkse W.G., van Beckum J., de Haan P.,
RA   ten Bosch C., Louwerse J.D.;
RT   "Molecular cloning and analysis of four potato tuber mRNAs.";
RL   Plant Mol. Biol. 11:255-269(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 43-52.
RX   PubMed=3264506; DOI=10.1515/bchm3.1988.369.1.233;
RA   Brzin J., Popovic T., Drobnic-Kosorok M., Kotnik M., Turk V.;
RT   "Inhibitors of cysteine proteinases from potato.";
RL   Biol. Chem. Hoppe-Seyler Suppl. 369:233-238(1988).
RN   [3]
RP   SEQUENCE REVISION TO 59-87.
RX   PubMed=16667716; DOI=10.1104/pp.94.1.40;
RA   Suh S.-C., Peterson J.E., Stiekema W.J., Hannapel D.J.;
RT   "Purification and characterization of the 22-kilodalton potato tuber
RT   proteins.";
RL   Plant Physiol. 94:40-45(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 43-222.
RC   TISSUE=Tuber;
RX   PubMed=8224155; DOI=10.1016/0014-5793(93)80366-3;
RA   Krizaj I., Drobnic-Kosorok M., Brzin J., Jerala R., Turk V.;
RT   "The primary structure of inhibitor of cysteine proteinases from potato.";
RL   FEBS Lett. 333:15-20(1993).
RN   [5]
RP   FUNCTION.
RX   PubMed=2401357; DOI=10.1016/0014-5793(90)81186-r;
RA   Rowan A.D., Brzin J., Buttle D.J., Barrett A.J.;
RT   "Inhibition of cysteine proteinases by a protein inhibitor from potato.";
RL   FEBS Lett. 269:328-330(1990).
RN   [6]
RP   INDUCTION.
RA   Suh S.-C., Stiekema W.J., Hannapel D.J.;
RT   "Proteinase-inhibitor activity and wound-inducible gene expression of the
RT   22-kDa potato-tuber proteins.";
RL   Planta 184:423-430(1991).
CC   -!- FUNCTION: Potent inhibitor of cathepsin l (cysteine protease). Does not
CC       inhibit trypsin or chymotrypsin (serine proteases). May protect the
CC       plant by inhibiting proteases of invading organisms.
CC       {ECO:0000269|PubMed:2401357}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Tubers, leaves.
CC   -!- INDUCTION: By wounding. Also expressed in upper non-wounded systemic
CC       leaves. {ECO:0000269|Ref.6}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33844.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X13181; CAA31578.1; ALT_FRAME; mRNA.
DR   EMBL; M22144; AAA33846.1; ALT_FRAME; mRNA.
DR   EMBL; M22145; AAA33845.1; -; mRNA.
DR   EMBL; M22143; AAA33844.1; ALT_FRAME; mRNA.
DR   PIR; S05595; S05595.
DR   PIR; S38742; S38742.
DR   AlphaFoldDB; P20347; -.
DR   SMR; P20347; -.
DR   STRING; 4113.PGSC0003DMT400026285; -.
DR   Allergome; 1670; Sola t 3.0102.
DR   Allergome; 641; Sola t 3.
DR   MEROPS; I03.017; -.
DR   PRIDE; P20347; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P20347; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Signal; Thiol protease inhibitor; Vacuole.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   PROPEP          27..42
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016924"
FT   CHAIN           43..222
FT                   /note="Cysteine protease inhibitor 1"
FT                   /id="PRO_0000016925"
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"
FT   CONFLICT        50
FT                   /note="D -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="G -> R (in Ref. 1; CAA31578/AAA33846)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   222 AA;  24684 MW;  D397D9D3DE2C8A88 CRC64;
     MKSINILSFL LLSSTLSLVA FARSFTSENP IVLPTTCHDD DNLVLPEVYD QDGNPLRIGE
     RYIINNPLLG AGAVYLYNIG NLQCPNAVLQ HMSIPQFLGE GTPVVFVRKS ESDYGDVVRV
     MTVVYIKFFV KTTKLCVDQT VWKVNDEQLV VTGGKVGNEN DIFKIMKTDL VTPGGSKYVY
     KLLHCPSHLG CKNIGGNFKN GYPRLVTVDD DKDFIPFVFI KA