ID   VSP_CROVV               Reviewed;          30 AA.
AC   P0DJG6;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Crotalus viridis viridis (Prairie rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8742;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND ACTIVITY REGULATION.
RC   TISSUE=Venom;
RX   PubMed=3167099; DOI=10.1016/0304-4165(88)90193-6;
RA   Komori Y., Nikai T., Sugihara H.;
RT   "Biochemical and physiological studies on a kallikrein-like enzyme from the
RT   venom of Crotalus viridis viridis (prairie rattlesnake).";
RL   Biochim. Biophys. Acta 967:92-102(1988).
CC   -!- FUNCTION: Snake venom serine protease that catalyzes the hydrolysis of
CC       arginine esters, kallikrein substrates Pro-Phe-Arg-MCA and Z-Phe-Arg-
CC       MCA. Cleaves kininogen analogs to release bradykinin. Induces
CC       contraction of the isolated rat uterus directly at high concentrations,
CC       but provokes more forceful contractions when injected in presence of
CC       bovine plasma. Shows capillary permeability-increasing activity and
CC       hypotensive activity on the anesthetized rat.
CC       {ECO:0000269|PubMed:3167099}.
CC   -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP).
CC       {ECO:0000269|PubMed:3167099}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: N-Glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Has no proteolytic activity against dimethyl casein and
CC       fibrinogen. {ECO:0000305|PubMed:3167099}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DJG6; -.
DR   SMR; P0DJG6; -.
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.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Hypotensive agent; Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>30
FT                   /note="Snake venom serine protease"
FT                   /id="PRO_0000417007"
FT   DOMAIN          1..>30
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3235 MW;  4B798BC6DE7ED276 CRC64;
     VIGGDECNIN EHRFLVALYD PDGFLSGGIL