IBBC1_HYAOR
ID IBBC1_HYAOR Reviewed; 60 AA.
AC C0HLT4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Bowman-Birk type proteinase inhibitor C1 {ECO:0000303|PubMed:33666645};
DE Short=HOSPI-C1 {ECO:0000303|PubMed:33666645};
OS Hyacinthus orientalis (Common hyacinth).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Hyacinthaceae;
OC Hyacinthoideae; Hyacintheae; Hyacinthus.
OX NCBI_TaxID=82025;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Bulb {ECO:0000303|PubMed:33666645};
RX PubMed=33666645; DOI=10.1042/bcj20201005;
RA Aoki-Shioi N., Terada S., Hellinger R., Furuta Y., Gruber C.W.;
RT "Isolation and functional diversity of Bowman-Birk type serine proteinase
RT inhibitors from Hyacinthus orientalis.";
RL Biochem. J. 478:1287-1301(2021).
CC -!- FUNCTION: Serine protease inhibitor (PubMed:33666645). Strongly
CC inhibits trypsin (Ki = 0.22 nM) and very weakly inhibits chymotrypsin
CC (Ki = 1200 nM) (PubMed:33666645). Does not inhibit bacterial subtilisin
CC (PubMed:33666645). {ECO:0000269|PubMed:33666645}.
CC -!- TISSUE SPECIFICITY: Expressed in bulb (at protein level).
CC {ECO:0000269|PubMed:33666645}.
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR AlphaFoldDB; C0HLT4; -.
DR SMR; C0HLT4; -.
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 SMART; SM00269; BowB; 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..60
FT /note="Bowman-Birk type proteinase inhibitor C1"
FT /id="PRO_0000452984"
FT SITE 13..14
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 5..21
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 11..19
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 28..35
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 32..49
FT /evidence="ECO:0000250|UniProtKB:P80321"
SQ SEQUENCE 60 AA; 7013 MW; 96FD348DC3413F52 CRC64;
ERPLCNECFI CDRSGDPRCL CEDHVPQCHE GCHQCEKVDT RSGTTMYQCR SFEYYDCANE