ID   KTI1_INGVE              Reviewed;          29 AA.
AC   C0HKQ3;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Kunitz-type trypsin inhibitor IVTI {ECO:0000303|Ref.1};
DE   Flags: Fragment;
OS   Inga vera (River koko).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Ingeae; Inga.
OX   NCBI_TaxID=486092 {ECO:0000303|Ref.1};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000303|Ref.1};
RX   DOI=10.1016/j.procbio.2016.03.008;
RA   da Silva Bezerra C., de Oliveira C.F.R., Machado O.L.T., de Melloe G.S.V.,
RA   da Rocha Pittae M.G., de Melo Rego M.J.B., Napoleao T.H.,
RA   Guedes Paiva P.M., de Fatima Ferreira Ribera S., Gomes V.M., Silva O.N.,
RA   Maria-Neto S., Franco O.L., Macedo M.L.R.;
RT   "Exploiting the biological roles of the trypsin inhibitor from Inga vera
RT   seeds: A multifunctional Kunitz inhibitor.";
RL   Process Biochem. 51:792-803(2016).
CC   -!- FUNCTION: Inhibits bovine trypsin but not chymotrypsin. Also inhibits
CC       trypsin-like enzymes from midgut of several lepidopteran species and
CC       inhibits larval development in those species. Has fungicidal activity
CC       against yeast C.buinensis. Has a bacteriostatic effect against E.coli.
CC       Is not cytotoxic. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Activity is stable between pH 2 and 11. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Activity is stable up to 60 degrees Celsius and declines rapidly at
CC         higher temperatures. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer and dimer. {ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=19968.3; Method=MALDI; Note=Monomer.;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: Mass=40408.5; Method=MALDI; Note=Dimer.;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKQ3; -.
DR   SMR; C0HKQ3; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   InterPro; IPR002160; Prot_inh_Kunz-lg.
DR   SUPFAM; SSF50386; SSF50386; 1.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..>29
FT                   /note="Kunitz-type trypsin inhibitor IVTI"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000441098"
FT   NON_TER         29
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   29 AA;  2953 MW;  9C056804D0298DF9 CRC64;
     EVVLDSDGEM LRNGGKYYLS PASPIGGGA