DRTI_DELRE
ID DRTI_DELRE Reviewed; 185 AA.
AC P83667;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Kunitz-type serine protease inhibitor DrTI;
OS Delonix regia (Royal poinciana) (Poinciana regia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; Peltophorum clade;
OC Delonix.
OX NCBI_TaxID=72433 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Seed {ECO:0000269|PubMed:11397427};
RX PubMed=11397427; DOI=10.1016/s0031-9422(01)00080-2;
RA Pando S.C., Oliva M.L.V., Sampaio C.A.M., Di Ciero L., Novello J.C.,
RA Marangoni S.;
RT "Primary sequence determination of a Kunitz inhibitor isolated from Delonix
RT regia seeds.";
RL Phytochemistry 57:625-631(2001).
CC -!- FUNCTION: Inhibits bovine trypsin and human plasma kallikrein.
CC {ECO:0000269|PubMed:11397427}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
CC -!- CAUTION: The reactive bond has a Glu in position P1 instead of an
CC expected Arg or Lys. {ECO:0000305}.
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DR PDB; 1R8N; X-ray; 1.75 A; A=1-185.
DR PDBsum; 1R8N; -.
DR AlphaFoldDB; P83667; -.
DR SMR; P83667; -.
DR EvolutionaryTrace; P83667; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Secreted; Serine protease inhibitor.
FT CHAIN 1..185
FT /note="Kunitz-type serine protease inhibitor DrTI"
FT /id="PRO_0000083324"
FT SITE 68..69
FT /note="Reactive bond"
FT /evidence="ECO:0000255"
FT DISULFID 44..89
FT /evidence="ECO:0000250"
FT DISULFID 139..147
FT /evidence="ECO:0000250"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1R8N"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1R8N"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1R8N"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1R8N"
SQ SEQUENCE 185 AA; 20094 MW; 55CFF042CC50C7CC CRC64;
SDAEKVYDIE GYPVFLGSEY YIVSAIIGAG GGGVRPGRTR GSMCPMSIIQ EQSDLQMGLP
VRFSSPEESQ GKIYTDTELE IEFVEKPDCA ESSKWVIVKD SGEARVAIGG SEDHPQGELV
RGFFKIEKLG SLAYKLVFCP KSSSGSCSDI GINYEGRRSL VLKSSDDSPF RVVFVKPRSG
SETES