IBB_MEDSC
ID IBB_MEDSC Reviewed; 62 AA.
AC P80321;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Bowman-Birk type proteinase inhibitor;
DE AltName: Full=MSTI;
OS Medicago scutellata (Snail medic) (Medicago polymorpha var. scutellata).
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; Trifolieae; Medicago.
OX NCBI_TaxID=36901;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC STRAIN=cv. Sava; TISSUE=Seed;
RX PubMed=9014368; DOI=10.1016/s0031-9422(96)00483-9;
RA Ceciliani F., Tava A., Iori R., Mortarino M., Odoardi M., Ronchi S.;
RT "A trypsin inhibitor from snail medic seeds active against pest
RT proteases.";
RL Phytochemistry 44:393-398(1997).
RN [2]
RP PROTEIN SEQUENCE, SUBUNIT, STRUCTURE BY NMR, AND DISULFIDE BONDS.
RC STRAIN=cv. Sava; TISSUE=Seed;
RX PubMed=12627949; DOI=10.1021/bi020576w;
RA Catalano M., Ragona L., Molinari H., Tava A., Zetta L.;
RT "Anticarcinogenic Bowman-Birk inhibitor isolated from snail medic seeds
RT (Medicago scutellata): solution structure and analysis of self-association
RT behavior.";
RL Biochemistry 42:2836-2846(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH TRYPSIN, AND
RP DISULFIDE BONDS.
RX PubMed=17142058; DOI=10.1016/j.jsb.2006.10.017;
RA Capaldi S., Perduca M., Faggion B., Carrizo M.E., Tava A., Ragona L.,
RA Monaco H.L.;
RT "Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail
RT medic (Medicago scutellata) seeds complexed with bovine trypsin.";
RL J. Struct. Biol. 158:71-79(2007).
CC -!- FUNCTION: Inhibits trypsin but not chymotrypsin. Inhibits the trypsin-
CC like proteinase activity present in larvae of the crop pests Adoxophyes
CC orana, Hyphantria cunea, Lobesia botrana and Ostrinia nubilalis.
CC {ECO:0000269|PubMed:9014368}.
CC -!- SUBUNIT: Forms a monomer at protein concentrations of below 1 mM. At
CC concentrations of above 2 mM, self-associates.
CC {ECO:0000269|PubMed:12627949, ECO:0000269|PubMed:17142058}.
CC -!- MASS SPECTROMETRY: Mass=6926; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9014368};
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR PDB; 1MVZ; NMR; -; A=1-62.
DR PDB; 2ILN; X-ray; 2.00 A; I=1-62.
DR PDBsum; 1MVZ; -.
DR PDBsum; 2ILN; -.
DR AlphaFoldDB; P80321; -.
DR SMR; P80321; -.
DR MEROPS; I12.003; -.
DR EvolutionaryTrace; P80321; -.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Serine protease inhibitor.
FT CHAIN 1..62
FT /note="Bowman-Birk type proteinase inhibitor"
FT /id="PRO_0000105845"
FT SITE 16..17
FT /note="Reactive bond for trypsin"
FT SITE 42..43
FT /note="Reactive bond for trypsin"
FT DISULFID 8..61
FT /evidence="ECO:0000269|PubMed:12627949,
FT ECO:0007744|PDB:1MVZ"
FT DISULFID 9..24
FT /evidence="ECO:0000269|PubMed:12627949,
FT ECO:0000269|PubMed:17142058, ECO:0007744|PDB:1MVZ,
FT ECO:0007744|PDB:2ILN"
FT DISULFID 12..57
FT /evidence="ECO:0000269|PubMed:12627949,
FT ECO:0000269|PubMed:17142058, ECO:0007744|PDB:1MVZ,
FT ECO:0007744|PDB:2ILN"
FT DISULFID 14..22
FT /evidence="ECO:0000269|PubMed:12627949,
FT ECO:0000269|PubMed:17142058, ECO:0007744|PDB:1MVZ,
FT ECO:0007744|PDB:2ILN"
FT DISULFID 31..38
FT /evidence="ECO:0000269|PubMed:12627949,
FT ECO:0000269|PubMed:17142058, ECO:0007744|PDB:1MVZ,
FT ECO:0007744|PDB:2ILN"
FT DISULFID 35..50
FT /evidence="ECO:0000269|PubMed:12627949,
FT ECO:0000269|PubMed:17142058, ECO:0007744|PDB:1MVZ,
FT ECO:0007744|PDB:2ILN"
FT DISULFID 40..48
FT /evidence="ECO:0000269|PubMed:12627949,
FT ECO:0000269|PubMed:17142058, ECO:0007744|PDB:1MVZ,
FT ECO:0007744|PDB:2ILN"
FT CONFLICT 42
FT /note="R -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="F -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="R -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1MVZ"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:2ILN"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2ILN"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2ILN"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2ILN"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2ILN"
SQ SEQUENCE 62 AA; 6932 MW; 075D742E8B075D63 CRC64;
TKSTTTACCD FCPCTRSIPP QCQCTDVREK CHSACKSCLC TRSFPPQCRC YDITDFCYPS
CS
