ID   VSP1_BOTPA              Reviewed;          15 AA.
AC   P0DJF1;
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 BpSP-1;
DE            Short=SVTLE BpSP-1;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   AltName: Full=Thrombin-like enzyme BpSP-I;
DE            Short=SVTLE BpSP-I;
DE   Flags: Fragment;
OS   Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=1042543;
RN   [1]
RP   PROTEIN SEQUENCE, ACTIVITY REGULATION, GLYCOSYLATION, AND SIALIC ACID.
RC   TISSUE=Venom;
RX   PubMed=19539638; DOI=10.1016/j.toxicon.2009.05.040;
RA   Costa F.L., Rodrigues R.S., Izidoro L.F., Menaldo D.L., Hamaguchi A.,
RA   Homsi-Brandeburgo M.I., Fuly A.L., Soares S.G., Selistre-de-Araujo H.S.,
RA   Barraviera B., Soares A.M., Rodrigues V.M.;
RT   "Biochemical and functional properties of a thrombin-like enzyme isolated
RT   from Bothrops pauloensis snake venom.";
RL   Toxicon 54:725-735(2009).
CC   -!- FUNCTION: Thrombin-like enzyme that has high clotting activity upon
CC       bovine and human plasma. Has also fibrinogenoltic activity by rapidly
CC       hydrolyzing Aalpha chain of fibrinogen (FGA), and partially consumes
CC       Bbeta chain (FGB). Has high catalytic activity upon substrates such as
CC       TAME, and specific substrates for thrombin S-2238 and S-2288. Also
CC       hydrolyzes specific substrates for kallikrein (S-2266 and S-2302),
CC       however, no release of kinin upon plasma has been determined. When
CC       administered intraperitoneally in mice, causes defibrinogenation,
CC       making the plasma incoagulable.
CC   -!- ACTIVITY REGULATION: Inhibited PMSF, benzamidine, leupeptin, and
CC       Cu(2+). {ECO:0000269|PubMed:19539638}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: N-glycosylated. Contains sialic acid residues.
CC       {ECO:0000269|PubMed:19539638}.
CC   -!- MISCELLANEOUS: Does not act on the gamma chain of fibrinogen. Does not
CC       act upon factor Xa (F10) and plasmin substrates. Does not induce
CC       hemorrhage, myotoxicity or edema (PubMed:19539638).
CC       {ECO:0000305|PubMed:19539638}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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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; Sialic acid; Toxin.
FT   CHAIN           1..>15
FT                   /note="Thrombin-like enzyme BpSP-1"
FT                   /id="PRO_0000416021"
FT   DOMAIN          1..>15
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1658 MW;  81F3926227D52FD4 CRC64;
     VIGGDECDIN EHPFL