ID   ITRY_LEULE              Reviewed;         179 AA.
AC   P83036; P83037;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Trypsin inhibitor;
DE            Short=LTI;
DE            Short=LlTI;
DE   AltName: Full=Kunitz-type trypsin inhibitor LlTI;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor alpha chain;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor beta chain;
OS   Leucaena leucocephala (White popinac) (Leucaena glauca).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Mimoseae; Leucaena.
OX   NCBI_TaxID=3866;
RN   [1]
RP   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, FUNCTION, SUBUNIT,
RP   TISSUE SPECIFICITY, VARIANT ASP-179 EXT, AND MASS SPECTROMETRY.
RC   TISSUE=Cotyledon;
RX   PubMed=10708849; DOI=10.1016/s0167-4838(99)00285-x;
RA   Oliva M.L.V., Souza-Pinto J.C., Batista I.F.C., Araujo M.S., Silveira V.F.,
RA   Auerswald E.A., Mentele R., Eckerskorn C., Sampaio M.U., Sampaio C.A.M.;
RT   "Leucaena leucocephala serine proteinase inhibitor: primary structure and
RT   action on blood coagulation, kinin release and rat paw edema.";
RL   Biochim. Biophys. Acta 1477:64-74(2000).
RN   [2]
RP   SEQUENCE REVISION TO 3-4; 65 AND 67.
RA   Oliva M.L.V., Souza-Pinto J.C., Batista I.F.C., Araujo M.S., Silveira V.F.,
RA   Auerswald E.A., Mentele R., Eckerskorn C., Sampaio M.U., Sampaio C.A.M.;
RL   Submitted (JUN-2001) to UniProtKB.
RN   [3]
RP   3D-STRUCTURE MODELING, AND SUBUNIT.
RX   PubMed=14741700; DOI=10.1016/j.bbrc.2003.12.177;
RA   Sattar R., Ali S.A., Kamal M., Khan A.A., Abbasi A.;
RT   "Molecular mechanism of enzyme inhibition: prediction of the three-
RT   dimensional structure of the dimeric trypsin inhibitor from Leucaena
RT   leucocephala by homology modelling.";
RL   Biochem. Biophys. Res. Commun. 314:755-765(2004).
CC   -!- FUNCTION: Inhibits trypsin, plasmin, human plasma kallikrein,
CC       chymotrypsin and factor XIIa activity. {ECO:0000269|PubMed:10708849}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain linked by a disulfide
CC       bond. {ECO:0000269|PubMed:10708849, ECO:0000269|PubMed:14741700}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Abundant in dry seeds.
CC       {ECO:0000269|PubMed:10708849}.
CC   -!- MASS SPECTROMETRY: [Trypsin inhibitor beta chain]: Mass=4764;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:10708849};
CC   -!- MASS SPECTROMETRY: [Trypsin inhibitor beta chain]: Mass=4765;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:10708849};
CC   -!- MISCELLANEOUS: There are two isoforms of the beta chain with slightly
CC       different molecular masses: 4764 and 4765 Da. These isoforms differ in
CC       their N- and C-terminal amino acids.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; P83036; -.
DR   SMR; P83036; -.
DR   MEROPS; I03.024; -.
DR   PRIDE; P83036; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Pyrrolidone carboxylic acid; Secreted; Serine protease inhibitor.
FT   CHAIN           1..137
FT                   /note="Trypsin inhibitor alpha chain"
FT                   /id="PRO_0000083298"
FT   CHAIN           138..179
FT                   /note="Trypsin inhibitor beta chain"
FT                   /id="PRO_0000428644"
FT   SITE            64..65
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:10708849"
FT   DISULFID        40..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..143
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000250"
FT   VARIANT         138
FT                   /note="Missing (in 4764 Da polypeptide)"
FT   VARIANT         179
FT                   /note="D -> DD (in 4764 Da polypeptide)"
SQ   SEQUENCE   179 AA;  20104 MW;  EB3212B8C5F045E5 CRC64;
     QVLVDLDGDP LYNGMSYYIL PVARGKGGGL ELARTGSESC PRTVVQTRSE TSRGLPARLA
     SPYRILIGSN IPLTIEFQPQ KPYSCHGHSS RSLQWKVEKT QMVKIASSDE EQRLFGPFQI
     QPYRNHYKLV YCESESRNHH DDCRDLGISI DDQQNRLLVV KNGDPLVVQF AKANRGGDD