IBB1_AMBAC
ID IBB1_AMBAC Reviewed; 63 AA.
AC P83284;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Bowman-birk type proteinase inhibitor;
DE AltName: Full=TaTI;
OS Amburana acreana (Cerejeira) (Torresea acreana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; ADA clade; Amburaneae;
OC Amburana.
OX NCBI_TaxID=187148 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Seed;
RX PubMed=8895102; DOI=10.1007/bf01908537;
RA Tanaka A.S., Sampaio M.U., Mentele R., Auerswald E.A., Sampaio C.A.M.;
RT "Sequence of a new Bowman-Birk inhibitor from Torresea acreana seeds and
RT comparison with Torresea cearensis trypsin inhibitor (TcTI2).";
RL J. Protein Chem. 15:553-560(1996).
CC -!- FUNCTION: Inhibits trypsin, chymotrypsin, plasmin and factor XIIa. Does
CC not inhibit factor Xa, thrombin and plasma kallikrein.
CC {ECO:0000269|PubMed:8895102}.
CC -!- MASS SPECTROMETRY: Mass=8388; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8895102};
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P83284; -.
DR SMR; P83284; -.
DR MEROPS; I12.001; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
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 Pfam; PF00228; Bowman-Birk_leg; 2.
DR SMART; SM00269; BowB; 1.
DR SUPFAM; SSF57247; SSF57247; 1.
DR PROSITE; PS00281; BOWMAN_BIRK; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Serine protease inhibitor.
FT CHAIN 1..63
FT /note="Bowman-birk type proteinase inhibitor"
FT /id="PRO_0000105833"
FT SITE 14..15
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000255"
FT SITE 41..42
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000255"
FT DISULFID 7..61
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 8..23
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 11..57
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 13..21
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 31..38
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 35..50
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 40..48
FT /evidence="ECO:0000250|UniProtKB:P80321"
SQ SEQUENCE 63 AA; 6916 MW; 53F220A2F5E4C297 CRC64;
SSKWEACCDR CACTKSIPPQ CHCADIRLNS CHSACESCAC TRSIPAKCRC FDITDFCYKP
CSG