VKTCI_NAJNA
ID VKTCI_NAJNA Reviewed; 57 AA.
AC P19859;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Kunitz-type serine protease inhibitor;
DE AltName: Full=Venom chymotrypsin inhibitor;
OS Naja naja (Indian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=35670;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2262001; DOI=10.1016/0014-5793(90)81426-o;
RA Shafqat J., Zaidi Z.H., Joernvall H.;
RT "Purification and characterization of a chymotrypsin Kunitz inhibitor type
RT of polypeptide from the venom of cobra (Naja naja naja).";
RL FEBS Lett. 275:6-8(1990).
CC -!- FUNCTION: Serine protease inhibitor that inhibits chymotrypsin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR PIR; S12957; S12957.
DR AlphaFoldDB; P19859; -.
DR SMR; P19859; -.
DR MEROPS; I02.065; -.
DR Proteomes; UP000694559; Unplaced.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor.
FT CHAIN 1..57
FT /note="Kunitz-type serine protease inhibitor"
FT /id="PRO_0000155440"
FT DOMAIN 5..55
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 15..16
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT DISULFID 5..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 14..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 30..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 57 AA; 6508 MW; 4BFB26A010C1737A CRC64;
RPRFCELAPS AGSCFGFVSS YYYNRYSNTC HSFTYSGCGK NANRFRTIDE CNRTCVV