IBB1_LUPAL
ID IBB1_LUPAL Reviewed; 63 AA.
AC P85172;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Bowman-Birk type proteinase inhibitor {ECO:0000303|PubMed:18474386};
DE Short=LaBBI {ECO:0000303|PubMed:18474386};
OS Lupinus albus (White lupine) (Lupinus termis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3870;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS
RP SPECTROMETRY, AND VARIANT SER-63 DEL.
RC STRAIN=cv. Multitalia {ECO:0000269|PubMed:18474386};
RC TISSUE=Seed {ECO:0000269|PubMed:18474386};
RX PubMed=18474386; DOI=10.1016/j.phytochem.2008.03.023;
RA Scarafoni A., Consonni A., Galbusera V., Negri A., Tedeschi G.,
RA Rasmussen P., Magni C., Duranti M.;
RT "Identification and characterization of a Bowman-Birk inhibitor active
RT towards trypsin but not chymotrypsin in Lupinus albus seeds.";
RL Phytochemistry 69:1820-1825(2008).
CC -!- FUNCTION: Inhibits trypsin stoichiometrically at the molar ratio of
CC 1:2, with a dissociation constant of 4.2 nM. Does not inhibit
CC chymotrypsin. {ECO:0000269|PubMed:18474386}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable at low pH. {ECO:0000269|PubMed:18474386};
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:18474386};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18474386}.
CC -!- MASS SPECTROMETRY: Mass=6858.47; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18474386};
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P85172; -.
DR SMR; P85172; -.
DR MEROPS; I12.018; -.
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; 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_0000292940"
FT SITE 15..16
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT SITE 41..42
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 7..60
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 8..23
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 11..56
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 13..21
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 30..37
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 34..49
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 39..47
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT VARIANT 63
FT /note="Missing (in minor form)"
FT /evidence="ECO:0000269|PubMed:18474386"
SQ SEQUENCE 63 AA; 6872 MW; A124F653ECC9A052 CRC64;
SLASKPCCDS CLCTRSIPPQ CRCTDIGETC HSACKSCICT RSFPPQCRCS DITHFCYKPC
TSS
