ID   ICI2_CANLI              Reviewed;         190 AA.
AC   P81726; P81724;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Subtilisin inhibitor CLSI-II;
DE   Contains:
DE     RecName: Full=Subtilisin inhibitor CLSI-III;
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, REACTIVE SITE, AND DISULFIDE BONDS.
RC   TISSUE=Seed;
RX   PubMed=8056749; DOI=10.1093/oxfordjournals.jbchem.a124350;
RA   Terada S., Katayama H., Noda K., Fujimura S., Kimoto E.;
RT   "Amino acid sequences of Kunitz family subtilisin inhibitors from seeds of
RT   Canavalia lineata.";
RL   J. Biochem. 115:397-404(1994).
RN   [2]
RP   CHARACTERIZATION.
RC   TISSUE=Seed;
RX   PubMed=8056748; DOI=10.1093/oxfordjournals.jbchem.a124349;
RA   Terada S., Fujimura S., Katayama H., Nagasawa M., Kimoto E.;
RT   "Purification and characterization of two Kunitz family subtilisin
RT   inhibitors from seeds of Canavalia lineata.";
RL   J. Biochem. 115:392-396(1994).
CC   -!- FUNCTION: Inhibits subtilisin-type microbial serine proteases incuding
CC       proteinase K, subtilisin BPN', subtilisin Carlsberg and subtilisin E in
CC       a non-stoichiometric manner. Weakly inhibits A.oryzae protease and some
CC       metalloproteases including pronase E. Does not inhibit trypsin,
CC       chymotrypsin, S.griseus alkaline protease or A.lyticus lysyl
CC       endopeptidase. CLSI-II has a wider inhibitory specificity than CLSI-
CC       III.
CC   -!- SUBUNIT: Forms active dimers on storage in aqueous solution, possibly
CC       through formation of an intermolecular disulfide bond.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The N-terminal Asn is removed in about 50% of both the CLSI-II and
CC       CLSI-III chains.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   PIR; A59416; A59416.
DR   PIR; A59418; A59418.
DR   PIR; JX0310; JX0310.
DR   PIR; JX0311; JX0311.
DR   AlphaFoldDB; P81726; -.
DR   SMR; P81726; -.
DR   MEROPS; I03.025; -.
DR   GO; GO:0005576; C:extracellular region; 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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           1..190
FT                   /note="Subtilisin inhibitor CLSI-II"
FT                   /id="PRO_0000016933"
FT   CHAIN           1..183
FT                   /note="Subtilisin inhibitor CLSI-III"
FT                   /id="PRO_0000016934"
FT   SITE            68..69
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..88
FT                   /evidence="ECO:0000269|PubMed:8056749"
FT   DISULFID        106
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   DISULFID        142..149
FT                   /evidence="ECO:0000269|PubMed:8056749"
FT   VARIANT         1
FT                   /note="Missing"
SQ   SEQUENCE   190 AA;  20750 MW;  D0850BE176DA27DB CRC64;
     NDVDVVMDAS SKPIFPGGEY YIMPAIWGPP GGGVRLAKTR NSDCPVTVLQ DYGEVIFGQP
     VKFTLPGRGS GLIITNTPVE EFIKKPECAS SSKWSVFVDD EIEKACVGIG GHEDHPGEQV
     FSGTFTIQKS RTPYNSYKLV FCESDSSTCS DIGRYDNNEG GRRLILTHHN PFQVVFMDAS
     TFDGTIRSDG