VKTC_BUNCA
ID VKTC_BUNCA Reviewed; 83 AA.
AC Q8AY41;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Kunitz-type serine protease inhibitor C;
DE AltName: Full=Kunitz inhibitor C;
DE Flags: Precursor;
OS Bungarus candidus (Malayan krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=92438;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Tsai I.H., Wang Y.M., Hsu H.Y.;
RT "Structural and functional genomics of Bungarus candidus.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine protease inhibitor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL30070.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY057888; AAL30070.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8AY41; -.
DR SMR; Q8AY41; -.
DR MEROPS; I02.031; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..83
FT /note="Kunitz-type serine protease inhibitor C"
FT /id="PRO_0000376873"
FT DOMAIN 31..81
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 41..42
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT DISULFID 31..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 40..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 56..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 83 AA; 9130 MW; 0DC4F159D38CC757 CRC64;
MSSGGLLLLL GLLTLWTELT PVSSKNRPPF CNLLPEPGRC NAIVRAFYYN SRLRKCLEFP
YGGCGGNANN FKTIDECQRT CAG