ID   ITRY_ARCEL              Reviewed;          20 AA.
AC   P84890;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Trypsin inhibitor AeTI;
DE   Flags: Fragment;
OS   Archidendron ellipticum (Albizia fasciculata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Ingeae; Archidendron.
OX   NCBI_TaxID=392766;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   TISSUE=Seed {ECO:0000269|PubMed:16376957};
RX   PubMed=16376957; DOI=10.1016/j.phytochem.2005.11.010;
RA   Bhattacharyya A., Mazumdar S., Leighton S.M., Babu C.R.;
RT   "A Kunitz proteinase inhibitor from Archidendron ellipticum seeds:
RT   purification, characterization, and kinetic properties.";
RL   Phytochemistry 67:232-241(2006).
CC   -!- FUNCTION: Competitively inhibits trypsin stoichiometrically at the
CC       molar ratio of 1:1. Also inhibits chymotrypsin.
CC       {ECO:0000269|PubMed:16376957}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Activity unaffected from pH 1-10. Loses 34% of its activity after 2
CC         hours at pH >12 and 65% of its activity after 4 hours at pH >12.
CC         {ECO:0000269|PubMed:16376957};
CC       Temperature dependence:
CC         Retains over 90% of its activity after incubation at between 25 and
CC         55 degrees Celsius for 1 hour. {ECO:0000269|PubMed:16376957};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain linked by a disulfide
CC       bond. {ECO:0000250|UniProtKB:P32733, ECO:0000269|PubMed:16376957}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; P84890; -.
DR   MEROPS; I03.029; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..>20
FT                   /note="Trypsin inhibitor AeTI"
FT                   /id="PRO_0000247650"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:16376957"
SQ   SEQUENCE   20 AA;  2239 MW;  51376C8395BAFF5E CRC64;
     AKELLDSDGI ILRNGANYYI