ID   VKTCI_OPHHA             Reviewed;          83 AA.
AC   P82966; B6RLX3;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Kunitz-type serine protease inhibitor;
DE   AltName: Full=Oh11-1;
DE   AltName: Full=Venom chymotrypsin inhibitor;
DE   Flags: Precursor;
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   He Y.-Y., Liu S.-B., Qian J.-Q., Lee W.-H., Zhang Y.;
RT   "Cloning and expression of chymotrypsin inhibitor Oh11-1 from king cobra.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 26-83, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=11350064; DOI=10.1006/bbrc.2001.4878;
RA   Chang L.-S., Chung C., Huang H.-B., Lin S.-R.;
RT   "Purification and characterization of a chymotrypsin inhibitor from the
RT   venom of Ophiophagus hannah (King Cobra).";
RL   Biochem. Biophys. Res. Commun. 283:862-867(2001).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits chymotrypsin (Ki=3520
CC       nM). {ECO:0000269|PubMed:11350064}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11350064}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11350064}.
CC   -!- MASS SPECTROMETRY: Mass=6493; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11350064};
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; EU246693; ABY74981.1; -; mRNA.
DR   AlphaFoldDB; P82966; -.
DR   SMR; P82966; -.
DR   MEROPS; I02.055; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:11350064"
FT   CHAIN           26..83
FT                   /note="Kunitz-type serine protease inhibitor"
FT                   /id="PRO_0000155442"
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;  9136 MW;  79B874FD49BDA849 CRC64;
     MSSGRLLLLL GLLTLWAELT PVSGLGRPKF CELPPEPGLC NARKTFFYYS LHSHACQKFI
     YGGCGGNANK FKTIDECHRT CVG