ID   ID5A_ADEPA              Reviewed;         138 AA.
AC   P09941;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Trypsin inhibitor DE5 alpha chain;
OS   Adenanthera pavonina (Sandal bead tree) (Condori wood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Mimoseae; Adenanthera.
OX   NCBI_TaxID=3811;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RA   Richardson M., Campos F.A.P., Xavier-Filho J., Macedo M.L.R., Maia G.M.C.,
RA   Yarwood A.;
RT   "The amino acid sequence and reactive (inhibitory) site of the major
RT   trypsin isoinhibitor (DE5) isolated from seeds of the Brazilian Carolina
RT   tree (Adenanthera pavonina L.).";
RL   Biochim. Biophys. Acta 872:134-140(1986).
CC   -!- FUNCTION: Inhibition of trypsin.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain linked by a disulfide
CC       bond.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A24376; A24376.
DR   AlphaFoldDB; P09941; -.
DR   SMR; P09941; -.
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..138
FT                   /note="Trypsin inhibitor DE5 alpha chain"
FT                   /id="PRO_0000083292"
FT   SITE            64..65
FT                   /note="Reactive bond for trypsin"
FT   DISULFID        40..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        131
FT                   /note="Interchain (with beta chain)"
FT                   /evidence="ECO:0000250"
FT   VARIANT         4
FT                   /note="L -> F (in less than 10% of the chains)"
FT   VARIANT         6
FT                   /note="V -> A (in less than 10% of the chains)"
FT   VARIANT         11
FT                   /note="L -> F (in less than 10% of the chains)"
FT   VARIANT         22
FT                   /note="A -> V (in less than 10% of the chains)"
FT   VARIANT         49
FT                   /note="A -> S (in less than 10% of the chains)"
FT   VARIANT         52
FT                   /note="S -> Q (in less than 10% of the chains)"
FT   VARIANT         67
FT                   /note="Y -> F (in less than 10% of the chains)"
FT   VARIANT         89
FT                   /note="D -> G (in less than 10% of the chains)"
FT   VARIANT         97
FT                   /note="E -> D (in less than 10% of the chains)"
FT   VARIANT         108
FT                   /note="K -> E (in less than 10% of the chains)"
FT   VARIANT         112
FT                   /note="Q -> R (in less than 10% of the chains)"
FT   VARIANT         113
FT                   /note="L -> H (in less than 10% of the chains)"
FT   VARIANT         120
FT                   /note="K -> Q (in less than 10% of the chains)"
SQ   SEQUENCE   138 AA;  15688 MW;  3B418092188CC255 CRC64;
     RELLDVDGNF LRNGGSYYIV PAFRGKGGGL ELARTGSETC PRTVVQAPAE QSRGLPARLS
     TPPRIRYIGP EFYLTIEFEE QKPPSCLRDS NLQWKVEEES QIVKIASKEE EQLFGSFQIK
     PYRDDYKLVY CEPQQGGR