ID   VSP2_OVOOK              Reviewed;          20 AA.
AC   P0C578;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Thrombin-like enzyme okinaxobin-2;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Okinaxobin II;
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, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   GLYCOSYLATION.
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. Releases both
CC       fibrinopeptides A and B from fibrinogen (FGA and FGB) to form fibrin
CC       clots. {ECO:0000269|PubMed:7725319}.
CC   -!- ACTIVITY REGULATION: Strongly inactivated by diisopropylfluorophosphate
CC       (DFP) and to a lesser extent by tosyl-L-lysine chloromethyl ketone
CC       (TLCK). {ECO:0000269|PubMed:7725319}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=118 uM for tosyl-L-arginine methyl ester (TAME)
CC         {ECO:0000269|PubMed:7725319};
CC         KM=67 uM for benzoyl-L-arginine p-nitroanilide (BAPA)
CC         {ECO:0000269|PubMed:7725319};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:7725319};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7725319}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7725319}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:7725319}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:7725319}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0C578; -.
DR   SABIO-RK; P0C578; -.
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-2"
FT                   /id="PRO_0000295002"
FT   DOMAIN          1..>20
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2312 MW;  7819F90E2343F391 CRC64;
     VVGGDECNIN EHRFLVALYY