IBB4_LATSA
ID IBB4_LATSA Reviewed; 30 AA.
AC B3EWN8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Bowman-Birk type proteinase inhibitor 4;
DE AltName: Full=LSI-4 {ECO:0000303|PubMed:21647515};
DE Flags: Fragment;
OS Lathyrus sativus (White vetchling).
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; Lathyrus.
OX NCBI_TaxID=3860;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|PubMed:21647515};
RX PubMed=21647515; DOI=10.1039/c1mb05141e;
RA Rocco M., Malorni L., Chambery A., Poerio E., Parente A., Di Maro A.;
RT "A Bowman-Birk inhibitor with anti-elastase activity from Lathyrus sativus
RT L. seeds.";
RL Mol. Biosyst. 7:2500-2507(2011).
CC -!- FUNCTION: Inhibits trypsin (IC(50)=17.60 nM) and, to a lesser extent,
CC alpha-chymotrypsin (IC(50)=2.38 uM). {ECO:0000269|PubMed:21647515}.
CC -!- MASS SPECTROMETRY: Mass=7460.01; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21647515};
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000255}.
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DR AlphaFoldDB; B3EWN8; -.
DR SMR; B3EWN8; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
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 SUPFAM; SSF57247; SSF57247; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Serine protease inhibitor.
FT CHAIN 1..>30
FT /note="Bowman-Birk type proteinase inhibitor 4"
FT /id="PRO_0000419011"
FT SITE 16..17
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 8..?
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 9..24
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 12..?
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT DISULFID 14..22
FT /evidence="ECO:0000250|UniProtKB:P01055"
FT NON_TER 30
FT /evidence="ECO:0000303|PubMed:21647515"
SQ SEQUENCE 30 AA; 3247 MW; 9A5B6616C3043C22 CRC64;
GDDVKSACCD TCLCTKSNPP ICRCVDIRET