IDE3_ERYCA
ID IDE3_ERYCA Reviewed; 172 AA.
AC P09943;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Trypsin inhibitor DE-3;
OS Erythrina caffra (Kaffir tree) (Coastal coral tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Erythrina.
OX NCBI_TaxID=3842;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=3116706;
RA Joubert F.J., Dowdle E.B.D.;
RT "The primary structure of the inhibitor of tissue plasminogen activator
RT found in the seeds of Erythrina caffra.";
RL Thromb. Haemost. 57:356-360(1987).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=1988676; DOI=10.1016/0022-2836(91)90618-g;
RA Onesti S., Brick P., Blow D.M.;
RT "Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra
RT seeds.";
RL J. Mol. Biol. 217:153-176(1991).
CC -!- FUNCTION: Inhibition of trypsin.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR PIR; A27220; A27220.
DR PDB; 1TIE; X-ray; 2.50 A; A=1-172.
DR PDBsum; 1TIE; -.
DR AlphaFoldDB; P09943; -.
DR SMR; P09943; -.
DR MEROPS; I03.011; -.
DR EvolutionaryTrace; P09943; -.
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..172
FT /note="Trypsin inhibitor DE-3"
FT /id="PRO_0000083286"
FT SITE 63..64
FT /note="Reactive bond for trypsin"
FT DISULFID 39..83
FT /evidence="ECO:0000269|PubMed:1988676"
FT DISULFID 132..139
FT /evidence="ECO:0000269|PubMed:1988676"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1TIE"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1TIE"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1TIE"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1TIE"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1TIE"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1TIE"
SQ SEQUENCE 172 AA; 19276 MW; F9A1D27D2B655F22 CRC64;
VLLDGNGEVV QNGGTYYLLP QVWAQGGGVQ LAKTGEETCP LTVVQSPNEL SDGKPIRIES
RLRSAFIPDD DKVRIGFAYA PKCAPSPWWT VVEDEQEGLS VKLSEDESTQ FDYPFKFEQV
SDQLHSYKLL YCEGKHEKCA SIGINRDQKG YRRLVVTEDY PLTVVLKKDE SS
