ID   ITRY_CASLE              Reviewed;          40 AA.
AC   C0HK48;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Trypsin inhibitor {ECO:0000303|Ref.1};
DE            Short=ClTI {ECO:0000303|Ref.1};
DE            EC=3.4.21.4 {ECO:0000269|Ref.1};
DE   Flags: Fragment;
OS   Cassia leiandra (Marimari).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; Cassia clade; Cassia.
OX   NCBI_TaxID=1884235;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000303|Ref.1};
RX   DOI=10.1016/j.procbio.2017.03.015;
RA   Dias L.P., Oliveira J.T., Rocha-Bezerra L.C., Sousa D.O., Costa H.P.,
RA   Araujo N.M., Carvalho A.F., Tabosa P.M., Monteiro-Moreira A.C., Lobo M.D.,
RA   Moreno F.B., Rocha B.A., Lopes J.L., Beltramini L.M., Vasconcelos I.M.;
RT   "A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal
RT   activity against Aedes aegypti.";
RL   Process Biochem. 57:228-238(2017).
CC   -!- FUNCTION: Inhibits trypsin but not chymotrypsin, papain or porcine
CC       pancreatic alpha-amylase. Has insecticidal activity against A.aegypti.
CC       Functions by inhibiting the A.aegypti midgut proteases to reduce the
CC       survival of larva and adults. {ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000269|Ref.1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable in the pH range 2.2-10.0. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Stable at temperatures up to 70 degrees Celsius. Incubation at
CC         temperatures above 70 degrees Celsius steadily decreases inhibitory
CC         activity. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=19484; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {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   AlphaFoldDB; C0HK48; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   SUPFAM; SSF50386; SSF50386; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..>40
FT                   /note="Trypsin inhibitor"
FT                   /id="PRO_0000437869"
FT   NON_TER         40
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   40 AA;  4097 MW;  DA6FBB79D917E61C CRC64;
     SVELDSDGEP IRNGGGLYYI LPVVQGKGGG LEFAKTGSQS