ID   ITRY_ACACO              Reviewed;         176 AA.
AC   P24924; P24926;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Trypsin inhibitor;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor chain A;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor chain B;
DE   Flags: Precursor;
GN   Name=ACTI;
OS   Acacia confusa (Formosa acacia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Acacieae; Acacia.
OX   NCBI_TaxID=3809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1375466; DOI=10.1016/s0006-291x(05)80056-7;
RA   Hung C.-H., Lee M.-C., Lin J.-Y.;
RT   "Nucleotide sequence of cDNA for Acacia confusa trypsin inhibitor and
RT   implication of post-translation processing.";
RL   Biochem. Biophys. Res. Commun. 184:1524-1528(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20 AND 138-156.
RC   TISSUE=Seed;
RX   PubMed=1794977; DOI=10.1093/oxfordjournals.jbchem.a123683;
RA   Lin J.-Y., Chu S.-C., Wu H.-C., Hsieh Y.-S.;
RT   "Trypsin inhibitor from the seeds of Acacia confusa.";
RL   J. Biochem. 110:879-883(1991).
CC   -!- FUNCTION: Inhibits trypsin and alpha-chymotrypsin stoichiometrically at
CC       the molar ratio of 1:1 and 2:1 respectively.
CC   -!- SUBUNIT: Heterodimer of an 'A' and a 'B' chain linked by a disulfide
CC       bond.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   EMBL; M92852; AAA32618.1; -; mRNA.
DR   PIR; JH0607; JH0607.
DR   PIR; PS0236; PS0236.
DR   PIR; PX0059; PX0059.
DR   AlphaFoldDB; P24924; -.
DR   SMR; P24924; -.
DR   MEROPS; I03.010; -.
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.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..136
FT                   /note="Trypsin inhibitor chain A"
FT                   /id="PRO_0000016894"
FT   PROPEP          137
FT                   /evidence="ECO:0000269|PubMed:1794977"
FT                   /id="PRO_0000016895"
FT   CHAIN           138..176
FT                   /note="Trypsin inhibitor chain B"
FT                   /id="PRO_0000016896"
FT   DISULFID        40..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        133..142
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   176 AA;  19584 MW;  89092383E6F7D462 CRC64;
     KELLDADGDI LRNGGAYYIL PALRGKGGGL TLAKTGDESC PLTVVQAQSE TKRGLPAVIW
     TPPKIAILTP GFYLNFEFQP RDLPACLQKY STLPWKVEGE SQEVKIAPKE KEQFLVGSFK
     IKPYRDDYKL VYCEGNSDDE SCKDLGISID DENNRRLVVK DGHPLAVRFE KAHRSG