IBB_VIGUN
ID IBB_VIGUN Reviewed; 83 AA.
AC P17734;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 02-JUN-2021, entry version 77.
DE RecName: Full=Bowman-Birk type seed trypsin and chymotrypsin inhibitor;
DE Short=BTCI;
OS Vigna unguiculata (Cowpea).
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; Vigna.
OX NCBI_TaxID=3917;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=cv. Serido;
RX PubMed=3426000;
RA Morhy L., Ventura M.M.;
RT "The complete amino acid sequence of the Vigna unguiculata (L.) Walp. seed
RT trypsin and chymotrypsin inhibitor.";
RL An. Acad. Bras. Cienc. 59:71-81(1987).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-77, AND DISULFIDE BONDS.
RX PubMed=17142290; DOI=10.1529/biophysj.106.090555;
RA Barbosa J.A., Silva L.P., Teles R.C., Esteves G.F., Azevedo R.B.,
RA Ventura M.M., de Freitas S.M.;
RT "Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata
RT seeds in complex with beta-trypsin at 1.55 A resolution and its structural
RT properties in association with proteinases.";
RL Biophys. J. 92:1638-1650(2007).
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR PDB; 2G81; X-ray; 1.55 A; I=1-77.
DR PDB; 3RU4; X-ray; 1.68 A; B=14-74.
DR PDB; 6EAU; X-ray; 1.18 A; I=24-32.
DR PDB; 6EAW; X-ray; 1.29 A; I=24-28.
DR PDB; 6EAX; X-ray; 1.19 A; I=24-28.
DR PDBsum; 2G81; -.
DR PDBsum; 3RU4; -.
DR PDBsum; 6EAU; -.
DR PDBsum; 6EAW; -.
DR PDBsum; 6EAX; -.
DR SMR; P17734; -.
DR MEROPS; I12.001; -.
DR EvolutionaryTrace; P17734; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00023; BBI; 1.
DR Gene3D; 2.10.69.10; -; 1.
DR InterPro; IPR035995; Bowman-Birk_prot_inh.
DR InterPro; IPR000877; Prot_inh_BBI.
DR SMART; SM00269; BowB; 1.
DR SUPFAM; SSF57247; SSF57247; 1.
DR PROSITE; PS00281; BOWMAN_BIRK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Serine protease inhibitor.
FT CHAIN 1..83
FT /note="Bowman-Birk type seed trypsin and chymotrypsin
FT inhibitor"
FT /id="PRO_0000105856"
FT SITE 26..27
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT SITE 53..54
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT DISULFID 18..72
FT /evidence="ECO:0000269|PubMed:17142290"
FT DISULFID 19..34
FT /evidence="ECO:0000269|PubMed:17142290"
FT DISULFID 22..68
FT /evidence="ECO:0000269|PubMed:17142290"
FT DISULFID 24..32
FT /evidence="ECO:0000269|PubMed:17142290"
FT DISULFID 42..49
FT /evidence="ECO:0000269|PubMed:17142290"
FT DISULFID 46..61
FT /evidence="ECO:0000269|PubMed:17142290"
FT DISULFID 51..59
FT /evidence="ECO:0000269|PubMed:17142290"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3RU4"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:6EAU"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3RU4"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3RU4"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:3RU4"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:3RU4"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3RU4"
SQ SEQUENCE 83 AA; 9101 MW; 409C4D2D3A54B976 CRC64;
SGHHZBSTBZ ASZSSKPCCR ZCACTKSIPP ZCRCSZVRLN SCHSACKSCA CTFSIPAZCF
CGBIBBFCYK PCKSSHSBBB BWN