ID   ITRY_ENTCO              Reviewed;         174 AA.
AC   P86451;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   02-JUN-2021, entry version 24.
DE   RecName: Full=Trypsin inhibitor {ECO:0000303|PubMed:8728712};
DE            Short=EcTI {ECO:0000303|PubMed:8728712};
DE   Contains:
DE     RecName: Full=Trypsin inhibitor alpha chain {ECO:0000303|PubMed:8728712};
DE   Contains:
DE     RecName: Full=Trypsin inhibitor beta chain {ECO:0000303|PubMed:8728712};
OS   Enterolobium contortisiliquum (Pacara earpod tree) (Mimosa
OS   contortisiliqua).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Ingeae; Enterolobium.
OX   NCBI_TaxID=55671;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   TISSUE=Seed {ECO:0000269|PubMed:8728712};
RX   PubMed=8728712; DOI=10.1016/0031-9422(95)00710-5;
RA   Batista I.F., Oliva M.L., Araujo M.S., Sampaio M.U., Richardson M.,
RA   Fritz H., Sampaio C.A.;
RT   "Primary structure of a Kunitz-type trypsin inhibitor from Enterolobium
RT   contortisiliquum seeds.";
RL   Phytochemistry 41:1017-1022(1996).
CC   -!- FUNCTION: Inhibits trypsin and chymotrypsin with a 1:1 stoichiometry,
CC       with dissociation constants of 1.56 nM and 120 nM respectively.
CC       Inhibits plasma kallikrein, factor XIIa and plasmin with dissociation
CC       constants of 5.0 nM, 150 nM and 18 nM respectively. Does not inhibit
CC       factor Xa, thrombin, tissue kallikrein or cysteine proteinases such as
CC       papain and bromelain. {ECO:0000269|PubMed:8728712}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Retains activity after incubation for 10 minutes at pH 2.0 to 12.0.
CC         {ECO:0000269|PubMed:8728712};
CC       Temperature dependence:
CC         Activity is retained when heated for 10 minutes up to 60 degrees
CC         Celsius. Inactive at 100 degrees Celsius.
CC         {ECO:0000269|PubMed:8728712};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain linked by a disulfide
CC       bond. {ECO:0000269|PubMed:8728712}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000255}.
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DR   PDB; 4J2K; X-ray; 1.75 A; A/B=1-174.
DR   PDB; 4J2Y; X-ray; 2.00 A; A=1-174.
DR   PDBsum; 4J2K; -.
DR   PDBsum; 4J2Y; -.
DR   SMR; P86451; -.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..134
FT                   /note="Trypsin inhibitor alpha chain"
FT                   /evidence="ECO:0000269|PubMed:8728712"
FT                   /id="PRO_0000392635"
FT   CHAIN           135..174
FT                   /note="Trypsin inhibitor beta chain"
FT                   /evidence="ECO:0000269|PubMed:8728712"
FT                   /id="PRO_0000392636"
FT   SITE            64..65
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P32733"
FT   DISULFID        40..86
FT                   /evidence="ECO:0000250|UniProtKB:P24924"
FT   DISULFID        131..140
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P24924"
FT   STRAND          15..26
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   TURN            85..89
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          125..131
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          140..147
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:4J2K"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:4J2K"
SQ   SEQUENCE   174 AA;  19457 MW;  A5D5C98D212C792A CRC64;
     KELLDSDGDI LRNGGTYYIL PALRGKGGGL ELAKTGDETC PLNVVQARGE TKRGRPAIIW
     TPPRIAILTP AFYLNIEFQT KDLPACLREY SRLPREEEQH SEVKLAPKEE AAAFGXEKLK
     PYRDDYKIVY CEGGSDDDSC KDLGISIDDE NNRRLVVKDG DPLAVRFVKA HRRG