ID   VASP1_VIPAA             Reviewed;         200 AA.
AC   P0DPS3;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Snake venom serine protease VaSP1 {ECO:0000303|PubMed:24269689};
DE   Flags: Fragment;
OS   Vipera ammodytes ammodytes (Western sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=8705;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=24269689; DOI=10.1016/j.toxicon.2013.11.007;
RA   Kurtovic T., Brgles M., Leonardi A., Lang Balija M., Sajevic T., Krizaj I.,
RA   Allmaier G., Marchetti-Deschmann M., Halassy B.;
RT   "VaSP1, catalytically active serine proteinase from Vipera ammodytes
RT   ammodytes venom with unconventional active site triad.";
RL   Toxicon 77:93-104(2014).
CC   -!- FUNCTION: Snake venom serine protease active on several blood
CC       coagulation enzymes. It completely cleaves fibrinogen Aalpha chain
CC       (FGA) after 120 minutes, partially cleaves Bbeta chain (FGB)
CC       (overnight) and has no activity on gamma chain. It does not release
CC       fibrinopeptides A and/or B exclusively, since the enzyme does not
CC       provoke fibrin polymerisation. It also degrades fibrin as efficiently
CC       as plasmin, and exhibits potent ability to cleave plasminogen and
CC       prothrombin, as well as heavy chain of factor X (F10). In vitro, it
CC       cleaves insulin B-chain (at positions His38-Leu39, Ala40-Leu41 and
CC       Tyr16-Leu17). {ECO:0000269|PubMed:24269689}.
CC   -!- ACTIVITY REGULATION: Inhibited by Pefabloc (90% inhibition), DTT (90%),
CC       Zn(2+) (80%), trypsin inhibitor II (50%), and benzamidine (45%), but
CC       not inhibited by EDTA, Ca(2+), Mg(2+) AND L-Cys.
CC       {ECO:0000269|PubMed:24269689}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=48.2 uM for N-benzoyl-Phe-Val-Arg-p-nitroanilide
CC         {ECO:0000269|PubMed:24269689};
CC       pH dependence:
CC         Optimum pH is 9.0. {ECO:0000269|PubMed:24269689};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24269689}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24269689}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24269689}.
CC   -!- PTM: N-glycosylated. The protein exist in multiple isoforms.
CC       {ECO:0000269|PubMed:24269689}.
CC   -!- MASS SPECTROMETRY: Mass=31500; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24269689};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Contains two of the three conventional residues of the
CC       catalytic triad: Asp and Ser are conserved, whereas the conventional
CC       His is replaced by an Arg. {ECO:0000305|PubMed:24269689}.
CC   -!- CAUTION: Residues 23 to 200 are identified by mass spectrometry.
CC       {ECO:0000305|PubMed:24269689}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Secreted; Toxin.
FT   CHAIN           1..>200
FT                   /note="Snake venom serine protease VaSP1"
FT                   /id="PRO_0000446021"
FT   DOMAIN          1..>200
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        88
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0C5B4"
FT   ACT_SITE        182
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0C5B4"
FT   SITE            182
FT                   /note="Forms a covalent bond with the inhibitor PMSF"
FT                   /evidence="ECO:0000250|UniProtKB:P0C5B4"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000305"
FT   NON_TER         200
SQ   SEQUENCE   200 AA;  22208 MW;  F7522FFEE14EEA43 CRC64;
     VIGGDECNIN EHPFLVALHT ARXXRFYCAG TLINQEWVLT AARCDRXXXX XILGVHSKXX
     XXXXXXXXXX XXXXXXXXXX TYTRWDKDIM LIRLKRXXXX XXXXXXXXXX XXXXXXXXXX
     XIMGWGTITT TKVTYPDVPH CADINMFDYS VCQKXXXKLP EKSRTLCAGI LQGGIDSCKG
     ISGGPLICNG EIQGIVSYGK