IBB_LENCU
ID IBB_LENCU Reviewed; 110 AA.
AC Q8W4Y8; Q8W4Y9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Bowman-Birk type proteinase inhibitor;
DE AltName: Full=LCTI;
DE AltName: Full=Trypsin/chymotrypsin inhibitor;
DE Flags: Precursor;
OS Lens culinaris (Lentil) (Cicer lens).
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; Hologalegina; IRL clade; Fabeae; Lens.
OX NCBI_TaxID=3864;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAD12253.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RC STRAIN=cv. Macrosperma group {ECO:0000269|PubMed:15655663}, and
RC cv. Microsperma group {ECO:0000269|PubMed:15655663};
RC TISSUE=Leaf {ECO:0000269|PubMed:15655663};
RX PubMed=15655663; DOI=10.1007/s00122-004-1888-1;
RA Sonnante G., De Paolis A., Pignone D.;
RT "Bowman-Birk inhibitors in Lens: identification and characterization of two
RT paralogous gene classes in cultivated lentil and wild relatives.";
RL Theor. Appl. Genet. 110:596-604(2005).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 43-110.
RC STRAIN=cv. Microsperma group {ECO:0000269|PubMed:15212472};
RC TISSUE=Seed {ECO:0000269|PubMed:15212472};
RX PubMed=15212472; DOI=10.1021/jf030768d;
RA Weder J.K.P., Hinkers S.C.;
RT "Complete amino acid sequence of the lentil trypsin-chymotrypsin inhibitor
RT LCI-1.7 and a discussion of atypical binding sites of Bowman-Birk
RT inhibitors.";
RL J. Agric. Food Chem. 52:4219-4226(2004).
RN [3]
RP PROTEIN SEQUENCE OF 43-110, FUNCTION, SUBUNIT, STRUCTURE BY NMR OF 43-109,
RP DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC STRAIN=cv. Macrosperma group; TISSUE=Seed;
RX PubMed=16889634; DOI=10.1111/j.1742-4658.2006.05406.x;
RA Ragg E.M., Galbusera V., Scarafoni A., Negri A., Tedeschi G., Consonni A.,
RA Sessa F., Duranti M.;
RT "Inhibitory properties and solution structure of a potent Bowman-Birk
RT protease inhibitor from lentil (Lens culinaris, L) seeds.";
RL FEBS J. 273:4024-4039(2006).
CC -!- FUNCTION: Inhibitor of trypsin and of chymotrypsin.
CC {ECO:0000269|PubMed:16889634}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16889634}.
CC -!- MASS SPECTROMETRY: Mass=7446.63; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16889634};
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000255}.
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DR EMBL; AJ420110; CAD12253.1; -; Genomic_DNA.
DR EMBL; AJ420109; CAD12252.1; -; Genomic_DNA.
DR PDB; 2AIH; NMR; -; A=43-109.
DR PDBsum; 2AIH; -.
DR AlphaFoldDB; Q8W4Y8; -.
DR BMRB; Q8W4Y8; -.
DR SMR; Q8W4Y8; -.
DR MEROPS; I12.003; -.
DR EvolutionaryTrace; Q8W4Y8; -.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Serine protease inhibitor; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..42
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15212472,
FT ECO:0000269|PubMed:16889634"
FT /id="PRO_0000003268"
FT CHAIN 43..110
FT /note="Bowman-Birk type proteinase inhibitor"
FT /evidence="ECO:0000269|PubMed:15212472,
FT ECO:0000269|PubMed:16889634"
FT /id="PRO_0000003269"
FT SITE 58..59
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P01065"
FT SITE 84..85
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250|UniProtKB:P01065"
FT DISULFID 50..103
FT /evidence="ECO:0000269|PubMed:16889634"
FT DISULFID 51..66
FT /evidence="ECO:0000269|PubMed:16889634"
FT DISULFID 54..99
FT /evidence="ECO:0000269|PubMed:16889634"
FT DISULFID 56..64
FT /evidence="ECO:0000269|PubMed:16889634"
FT DISULFID 73..80
FT /evidence="ECO:0000269|PubMed:16889634"
FT DISULFID 77..92
FT /evidence="ECO:0000269|PubMed:16889634"
FT DISULFID 82..90
FT /evidence="ECO:0000269|PubMed:16889634"
FT CONFLICT 27
FT /note="D -> N (in Ref. 1; CAD12252)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="K -> N (in Ref. 1; CAD12253/CAD12252)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="A -> T (in Ref. 1; CAD12253)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2AIH"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2AIH"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2AIH"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2AIH"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2AIH"
SQ SEQUENCE 110 AA; 12266 MW; 0FB31C642323D764 CRC64;
MVLMNKKAIM KLALMLFLLG FTANVVDARF DSTSFITQVL SNGDDVKSAC CDTCLCTRSQ
PPTCRCVDVR ESCHSACDKC VCAYSNPPQC QCYDTHKFCY KACHNSEIEE
