ID5B_ADEPA
ID ID5B_ADEPA Reviewed; 38 AA.
AC P09942;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Trypsin inhibitor DE5 beta 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}.
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DR PIR; B24376; B24376.
DR AlphaFoldDB; P09942; -.
DR SMR; P09942; -.
DR MEROPS; I03.019; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR Pfam; PF00197; Kunitz_legume; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Serine protease inhibitor.
FT CHAIN 1..38
FT /note="Trypsin inhibitor DE5 beta chain"
FT /id="PRO_0000083293"
FT DISULFID 3
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000250"
FT VARIANT 1
FT /note="L -> P"
SQ SEQUENCE 38 AA; 4229 MW; E51F7F924F53FAC7 CRC64;
LECKDLGISI DDDNNRRLAV KEGDPLVVQF VNADREGN