ID   IBB1_ARAHY              Reviewed;          70 AA.
AC   P01066;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor A-II;
DE   Contains:
DE     RecName: Full=Bowman-Birk type proteinase inhibitor A-I;
DE   Contains:
DE     RecName: Full=Bowman-Birk type proteinase inhibitor B-I;
DE   Contains:
DE     RecName: Full=Bowman-Birk type proteinase inhibitor B-III;
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 OF 1-19.
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 10-70.
RX   PubMed=6841347; DOI=10.1093/oxfordjournals.jbchem.a134202;
RA   Norioka S., Ikenaka T.;
RT   "Amino acid sequence of a trypsin-chymotrypsin inhibitor, B-III, of peanut
RT   (Arachis hypogaea).";
RL   J. Biochem. 93:479-485(1983).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX   PubMed=3571206;
RA   Suzuki A., Tsunogae Y., Tanaka I., Yamane T., Ashida T., Norioka S.,
RA   Hara S., Ikenaka T.;
RT   "The structure of Bowman-Birk type protease inhibitor A-II from peanut
RT   (Arachis hypogaea) at 3.3-A resolution.";
RL   J. Biochem. 101:267-274(1987).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=8254669; DOI=10.1006/jmbi.1993.1622;
RA   Suzuki A., Yamane T., Ashida T., Norioka S., Hara S., Ikenaka T.;
RT   "Crystallographic refinement of Bowman-Birk type protease inhibitor A-II
RT   from peanut (Arachis hypogaea) at 2.3-A resolution.";
RL   J. Mol. Biol. 234:722-734(1993).
CC   -!- FUNCTION: These proteins inhibit trypsin and chymotrypsin, having 2
CC       sites of interaction with trypsin. The site of interaction with
CC       chymotrypsin has not been determined but is not independent of the
CC       trypsin-reactive sites.
CC   -!- MISCELLANEOUS: Four inhibitors were found that are identical except at
CC       their amino ends and that probably arise by proteolytic degradation of
CC       a single gene product.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A91975; TINPA2.
DR   AlphaFoldDB; P01066; -.
DR   BMRB; P01066; -.
DR   SMR; P01066; -.
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..70
FT                   /note="Bowman-Birk type proteinase inhibitor A-II"
FT                   /id="PRO_0000003260"
FT   CHAIN           4..70
FT                   /note="Bowman-Birk type proteinase inhibitor A-I"
FT                   /id="PRO_0000003261"
FT   CHAIN           8..70
FT                   /note="Bowman-Birk type proteinase inhibitor B-I"
FT                   /id="PRO_0000003262"
FT   CHAIN           10..70
FT                   /note="Bowman-Birk type proteinase inhibitor B-III"
FT                   /id="PRO_0000003263"
FT   SITE            19..20
FT                   /note="Reactive bond for trypsin"
FT   SITE            47..48
FT                   /note="Reactive bond for trypsin"
FT   DISULFID        11..68
FT                   /evidence="ECO:0000269|PubMed:8254669"
FT   DISULFID        12..29
FT                   /evidence="ECO:0000269|PubMed:8254669"
FT   DISULFID        15..63
FT                   /evidence="ECO:0000269|PubMed:8254669"
FT   DISULFID        17..27
FT                   /evidence="ECO:0000269|PubMed:8254669"
FT   DISULFID        36..43
FT                   /evidence="ECO:0000269|PubMed:8254669"
FT   DISULFID        40..55
FT                   /evidence="ECO:0000269|PubMed:8254669"
FT   DISULFID        45..53
FT                   /evidence="ECO:0000269|PubMed:8254669"
SQ   SEQUENCE   70 AA;  7633 MW;  56CE31B690015CD5 CRC64;
     EASSSSDDNV CCNGCLCDRR APPYFECVCV DTFDHCPASC NSCVCTRSNP PQCRCTDKTQ
     GRCPVTECRS