VSP1_OVOOK
ID VSP1_OVOOK Reviewed; 20 AA.
AC P20005;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Thrombin-like enzyme okinaxobin-1;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Okinaxobin I;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Fragment;
OS Ovophis okinavensis (Ryukyu Island pit viper) (Trimeresurus okinavensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Ovophis.
OX NCBI_TaxID=8769;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=1964457; DOI=10.1093/oxfordjournals.jbchem.a123287;
RA Iwasaki A., Shieh T.-C., Shimohigashi Y., Waki M., Kihara H., Ohno M.;
RT "Purification and characterization of a coagulant enzyme, okinaxobin I,
RT from the venom of Trimeresurus okinavensis (Himehabu snake) which releases
RT fibrinopeptide B.";
RL J. Biochem. 108:822-828(1990).
RN [2]
RP PROTEIN SEQUENCE, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RX PubMed=7725319; DOI=10.1016/0041-0101(94)90309-3;
RA Nose T., Shimohigashi Y., Hattori S., Kihara H., Ohno M.;
RT "Purification and characterization of a coagulant enzyme, okinaxobin II,
RT from Trimeresurus okinavensis (himehabu snake) venom which release
RT fibrinopeptides A and B.";
RL Toxicon 32:1509-1520(1994).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that releases
CC specifically fibrinopeptide B from fibrinogen (FGB) to form fibrin
CC clots. Shows a preferential cleavage at Arg-|-Gly bonds in fibrinogen
CC beta chains. Cleaves fibrinogen beta chains preferentially to alpha
CC chains. {ECO:0000269|PubMed:1964457, ECO:0000269|PubMed:7725319}.
CC -!- ACTIVITY REGULATION: Strongly inactivated by diisopropylfluorophosphate
CC (DFP) and phenylmethanesulfonyl fluoride (PMSF), and to a lesser extent
CC by tosyl-L-lysine chloromethyl ketone (TLCK).
CC {ECO:0000269|PubMed:1964457}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=73 uM for tosyl-L-arginine methyl ester (TAME)
CC {ECO:0000269|PubMed:7725319};
CC KM=40 uM for benzoyl-L-arginine p-nitroanilide (BAPA)
CC {ECO:0000269|PubMed:7725319};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1964457}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1964457}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:1964457}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1964457}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; PX0042; PX0042.
DR AlphaFoldDB; P20005; -.
DR MEROPS; S01.346; -.
DR SABIO-RK; P20005; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Toxin.
FT CHAIN 1..>20
FT /note="Thrombin-like enzyme okinaxobin-1"
FT /id="PRO_0000088742"
FT DOMAIN 1..>20
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2249 MW; 69E9EF62EC53F391 CRC64;
VIGGDECNIN EHRFLAALYD
