VKTK1_DABRR
ID VKTK1_DABRR Reviewed; 90 AA.
AC H6VC05;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Kunitz-type serine protease inhibitor DrKIn-I;
DE AltName: Full=Daboia russelii Kunitz Inhibitor-I;
DE Flags: Precursor;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOASSAY, PYROGLUTAMATE FORMATION AT
RP GLN-25, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=22416129; DOI=10.1074/jbc.m111.323063;
RA Cheng A.C., Wu H.L., Shi G.Y., Tsai I.H.;
RT "A novel heparin-dependent inhibitor of activated protein C that
RT potentiates consumptive coagulopathy in Russell's viper envenomation.";
RL J. Biol. Chem. 287:15739-15748(2012).
CC -!- FUNCTION: Serine protease inhibitor. Inhibits activated protein C (APC)
CC with an IC(50) of 3.5 nM in the presence of heparin (to which it
CC strongly binds) and an IC(50) of 88.9 nM in its absence. Other targets
CC are also significantly inhibited in presence of heparin: trypsin
CC (PRSS1) (45%), coagulation FXIa (F11) (40%), and plasmin (PLG) (70%).
CC In vivo, synergizes with RVV-X in promoting coagulation in mice and by
CC extension in Russell's viper bite patients.
CC {ECO:0000269|PubMed:22416129}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=7548.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22416129};
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR EMBL; JN825729; AFB74191.1; -; mRNA.
DR EMBL; JQ011382; AFD04723.1; -; mRNA.
DR AlphaFoldDB; H6VC05; -.
DR SMR; H6VC05; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin 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 Blood coagulation cascade activating toxin; Disulfide bond;
KW Hemostasis impairing toxin; Protease inhibitor;
KW Pyrrolidone carboxylic acid; Secreted; Serine protease inhibitor; Signal;
KW Toxin.
FT SIGNAL 1..24
FT CHAIN 25..90
FT /note="Kunitz-type serine protease inhibitor DrKIn-I"
FT /id="PRO_0000422088"
FT DOMAIN 31..81
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT REGION 73..79
FT /note="Putative heparin-binding motif"
FT REGION 84..89
FT /note="Putative heparin-binding motif"
FT SITE 41..42
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
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 90 AA; 10010 MW; 108733A3169B67AA CRC64;
MSSGGLLLLL GLLTLWAELT PISGQDRPKF CNLAPESGRC RGHLRRIYYN PDSNKCEVFF
YGGCGGNDNN FETRKKCRQT CGAPRKGRPT
