BGIA_MOMCH
ID BGIA_MOMCH Reviewed; 68 AA.
AC P24076;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Glu S.griseus protease inhibitor;
DE AltName: Full=BGIA;
OS Momordica charantia (Bitter gourd) (Balsam pear).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica.
OX NCBI_TaxID=3673;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC TISSUE=Seed;
RX PubMed=1679433; DOI=10.1016/s0021-9258(18)55360-6;
RA Ogata F., Miyata T., Fujii N., Yoshida N., Noda K., Makisumi S., Ito A.;
RT "Purification and amino acid sequence of a bitter gourd inhibitor against
RT an acidic amino acid-specific endopeptidase of Streptomyces griseus.";
RL J. Biol. Chem. 266:16715-16721(1991).
CC -!- FUNCTION: Competitively inhibits Glu S.griseus protease by forming
CC probably a 1:1 complex. BGIA has no inhibitory activity against 2 other
CC acidic amino acid-specific endopeptidases (S.aureus protease V8 and
CC B.subtilis proteinase), chymotrypsin, trypsin, pancreatic elastase, and
CC papain, although subtilisin Carlsberg was strongly inhibited.
CC -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC protease inhibitor) family. {ECO:0000305}.
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DR PIR; A41174; A41174.
DR AlphaFoldDB; P24076; -.
DR SMR; P24076; -.
DR MEROPS; I13.004; -.
DR iPTMnet; P24076; -.
DR Proteomes; UP000504603; Unplaced.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR InterPro; IPR000864; Prot_inh_pot1.
DR InterPro; IPR036354; Prot_inh_pot1_sf.
DR PANTHER; PTHR33091; PTHR33091; 1.
DR Pfam; PF00280; potato_inhibit; 1.
DR PRINTS; PR00292; POTATOINHBTR.
DR SUPFAM; SSF54654; SSF54654; 1.
DR PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor.
FT CHAIN 1..68
FT /note="Glu S.griseus protease inhibitor"
FT /id="PRO_0000217644"
FT SITE 44..45
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:1679433"
FT DISULFID 3..48
FT /evidence="ECO:0000305"
SQ SEQUENCE 68 AA; 7383 MW; 97C98BF4AD71E933 CRC64;
SQCQGKRSWP QLVGSTGAAA KAVIERENPR VRAVIVRVGS PVTADFRCDR VRVWVTERGI
VARPPAIG