VSPDV_BOTJR
ID VSPDV_BOTJR Reviewed; 10 AA.
AC P0DJE8;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Thrombin-like enzyme D-V;
DE Short=SVTLE D-V;
DE EC=3.4.21.-;
DE AltName: Full=Clotting factor;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Fragment;
OS Bothrops jararacussu (Jararacussu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8726;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Venom;
RX PubMed=9248003; DOI=10.1016/s0041-0101(96)00222-x;
RA Andriao-Escarso S.H., Sampaio S.V., Cunha O.A., Marangoni S., Oliveira B.,
RA Giglio J.R.;
RT "Isolation and characterization of a new clotting factor from Bothrops
RT jararacussu (jararacucu) venom.";
RL Toxicon 35:1043-1052(1997).
CC -!- FUNCTION: Thrombin-like enzyme that induces quick formation of fibrin
CC clots. Only degrades the Aalpha-chain of fibrinogen (FGA).
CC {ECO:0000269|PubMed:9248003}.
CC -!- ACTIVITY REGULATION: Is not inhibited by aprotinin.
CC {ECO:0000269|PubMed:9248003}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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..>10
FT /note="Thrombin-like enzyme D-V"
FT /id="PRO_0000416018"
FT DOMAIN 1..>10
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 7..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 10
SQ SEQUENCE 10 AA; 1052 MW; 3D854A4EB44AADD8 CRC64;
VVGADNCNFN