ID   ICI1_CANLI              Reviewed;          65 AA.
AC   P81712;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Subtilisin inhibitor CLSI-I;
OS   Canavalia lineata (Beach bean) (Dolichos lineatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX   NCBI_TaxID=28957;
RN   [1]
RP   PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   TISSUE=Seed;
RX   PubMed=7765594; DOI=10.1271/bbb.58.2004;
RA   Katayama H., Soezima Y., Fujimura S., Terada S., Kimoto E.;
RT   "Property and amino acid sequence of a subtilisin inhibitor from seeds of
RT   beach canavalia (Canavalia lineata).";
RL   Biosci. Biotechnol. Biochem. 58:2004-2008(1994).
CC   -!- FUNCTION: Inhibits subtilisin-type microbial serine proteases including
CC       proteinase K, subtilisin BPN', subtilisin Carlsberg, subtilisin E,
CC       A.oryzae protease and S.griseus alkaline protease. Weakly inhibits
CC       pronase E. Does not inhibit trypsin or chymotrypsin.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   PIR; JC2380; JC2380.
DR   AlphaFoldDB; P81712; -.
DR   SMR; P81712; -.
DR   MEROPS; I13.007; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR   InterPro; IPR000864; Prot_inh_pot1.
DR   InterPro; IPR036354; Prot_inh_pot1_sf.
DR   PANTHER; PTHR33091; PTHR33091; 1.
DR   Pfam; PF00280; potato_inhibit; 1.
DR   PRINTS; PR00292; POTATOINHBTR.
DR   SUPFAM; SSF54654; SSF54654; 1.
DR   PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..65
FT                   /note="Subtilisin inhibitor CLSI-I"
FT                   /id="PRO_0000217642"
FT   SITE            41..42
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   65 AA;  7192 MW;  B2837BC123B12BE3 CRC64;
     STRKTSWPEL VGVTAEEAEK IKEEMSGVEI QVVPPGSFVT ADYKPQRVRL YVDESNKVTR
     TPGIG