ID   ITRA_ALBKA              Reviewed;          53 AA.
AC   P85498;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Kunitz-type trypsin inhibitor alpha chain;
DE   AltName: Full=AKTI;
DE   Flags: Fragments;
OS   Albizia kalkora (Kalkora mimosa) (Mimosa kalkora).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Ingeae; Albizia.
OX   NCBI_TaxID=199156;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:18368297};
RX   PubMed=18368297; DOI=10.1007/s10529-008-9699-0;
RA   Zhou J.-Y., Liao H., Zhang N.-H., Tang L., Xu Y., Chen F.;
RT   "Identification of a Kunitz inhibitor from Albizzia kalkora and its
RT   inhibitory effect against pest midgut proteases.";
RL   Biotechnol. Lett. 30:1495-1499(2008).
CC   -!- FUNCTION: Inhibits trypsin with a Ki of 0.25 uM. Inhibits the trypsin-
CC       like proteases in midguts of larval H.armigera, S.exigua, and P.rapae.
CC       {ECO:0000269|PubMed:18368297}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable from pH 2.0 to 12.0. {ECO:0000269|PubMed:18368297};
CC       Temperature dependence:
CC         Retains almost 100% of its activity after heating for 10 minutes at
CC         70 degrees Celsius, activity is lost rapidly above 70 degrees
CC         Celsius. {ECO:0000269|PubMed:18368297};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain linked by a disulfide
CC       bond. {ECO:0000269|PubMed:18368297}.
CC   -!- MASS SPECTROMETRY: Mass=19768.23; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18368297};
CC   -!- MISCELLANEOUS: The reactive bond is likely to include a lysine residue.
CC       {ECO:0000269|PubMed:18368297}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000255}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:18368297}.
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DR   AlphaFoldDB; P85498; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..>53
FT                   /note="Kunitz-type trypsin inhibitor alpha chain"
FT                   /id="PRO_0000337168"
FT   REGION          33..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        45..?
FT                   /evidence="ECO:0000250|UniProtKB:P83036"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000303|PubMed:18368297"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000303|PubMed:18368297"
FT   NON_CONS        39..40
FT                   /evidence="ECO:0000303|PubMed:18368297"
FT   NON_TER         53
FT                   /evidence="ECO:0000303|PubMed:18368297"
SQ   SEQUENCE   53 AA;  5631 MW;  514C443309E65B93 CRC64;
     KELLDADGDI LRNGGPAYPG LMPGVERDLP ASGWGLPRRT GDESCPLNVK AVR