ID   VSP_PROJR               Reviewed;          21 AA.
AC   P0DM43;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Thrombin-like enzyme jerdonobin;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragment;
OS   Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=242841;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=10736476; DOI=10.1016/s0041-0101(99)00222-6;
RA   Lu Q.M., Jin Y., Li D.S., Wang W.Y., Xiong Y.L.;
RT   "Characterization of a thrombin-like enzyme from the venom of Trimeresurus
RT   jerdonii.";
RL   Toxicon 38:1225-1236(2000).
RN   [2]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=12091097; DOI=10.1016/s1096-4959(02)00069-6;
RA   Jin Y., Lu Q.M., Wang W.Y., Xiong Y.L.;
RT   "Actions of two serine proteases from Trimeresurus jerdonii venom on
RT   chromogenic substrates and fibrinogen.";
RL   Comp. Biochem. Physiol. 132:529-534(2002).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease that has
CC       fibrinogen-clotting activity (217 NIH units/mg). It releases
CC       fibrinopeptide A and a small amount of fibrinopeptide B from fibrinogen
CC       alpha (FGA) and beta (FGB). {ECO:0000269|PubMed:10736476,
CC       ECO:0000269|PubMed:12091097}.
CC   -!- ACTIVITY REGULATION: Amidolytic and clotting activities are completely
CC       inhibited by NPGB and PMSF, but not inhibited by EDTA.
CC       {ECO:0000269|PubMed:10736476}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=196 uM for H-D-Phe-Pip-Arg-pNA (S-2238)
CC         {ECO:0000269|PubMed:10736476, ECO:0000269|PubMed:12091097};
CC         KM=53 uM for H-D-Pro-Phe-Arg-pNA (S-2302)
CC         {ECO:0000269|PubMed:10736476, ECO:0000269|PubMed:12091097};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10736476}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10736476}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Represents a minor component of the venom, about 1% of
CC       the total venom proteins. {ECO:0000305|PubMed:10736476}.
CC   -!- MISCELLANEOUS: Does not activate factor XIII (F13). Does not have
CC       hemorrhagic activity. Does not cause platelet aggregation
CC       (PubMed:10736476). Does not degrade fibrinogen within 12 hours. Does
CC       not degrade H-D-Val-Leu-Lys-pNA (S-2251) (PubMed:12091097).
CC       {ECO:0000269|PubMed:12091097, ECO:0000305|PubMed:10736476}.
CC   -!- MISCELLANEOUS: Its molecular weight is estimated to be 38000.
CC       {ECO:0000269|PubMed:10736476}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DM43; -.
DR   SABIO-RK; P0DM43; -.
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   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>21
FT                   /note="Thrombin-like enzyme jerdonobin"
FT                   /id="PRO_0000422695"
FT   DOMAIN          1..>21
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2425 MW;  AB79E9EF62F343F3 CRC64;
     VIGGDECNIN EHRFLVALYD F