ID   IBB2_ARAHY              Reviewed;          63 AA.
AC   P01067;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor B-II;
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6630176; DOI=10.1093/oxfordjournals.jbchem.a134390;
RA   Norioka S., Ikenaka T.;
RT   "Amino acid sequences of trypsin-chymotrypsin inhibitors (A-I, A-II, B-I,
RT   and B-II) from peanut (Arachis hypogaea): a discussion on the molecular
RT   evolution of legume Bowman-Birk type inhibitors.";
RL   J. Biochem. 94:589-599(1983).
CC   -!- MISCELLANEOUS: One of the interaction site with trypsin probably also
CC       interacts with chymotrypsin.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A01306; TINPB2.
DR   AlphaFoldDB; P01067; -.
DR   SMR; P01067; -.
DR   MEROPS; I12.006; -.
DR   MEROPS; I12.017; -.
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   Pfam; PF00228; Bowman-Birk_leg; 1.
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 B-II"
FT                   /id="PRO_0000105835"
FT   SITE            13..14
FT                   /note="Reactive bond for trypsin"
FT   SITE            41..42
FT                   /note="Reactive bond for trypsin"
FT   DISULFID        5..62
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        6..23
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        9..57
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        11..21
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        30..37
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        34..49
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        39..47
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
SQ   SEQUENCE   63 AA;  6795 MW;  551E39DDF391318D CRC64;
     AASDCCSACI CDRRAPPYFE CTCGDTFDHC PAACNKCVCT RSIPPQCRCT DRTQGRCPLT
     PCA