ID   VSP1_GLOBL              Reviewed;         238 AA.
AC   P81176;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Thrombin-like enzyme halystase;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
OS   Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=242054;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND ACTIVITY REGULATION.
RC   TISSUE=Venom;
RX   PubMed=9546675; DOI=10.1046/j.1432-1327.1998.2520569.x;
RA   Matsui T., Sakurai Y., Fujimura Y., Hayashi I., Oh-Ishi S., Suzuki M.,
RA   Hamako J., Yamamoto Y., Yamazaki J., Kinoshita M., Titani K.;
RT   "Purification and amino acid sequence of halystase from snake venom of
RT   Agkistrodon halys blomhoffii, a serine protease that cleaves specifically
RT   fibrinogen and kininogen.";
RL   Eur. J. Biochem. 252:569-575(1998).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease. Cleaves fibrinogen
CC       (beta chain of fibrinogen (FGB) and more slowly alpha chain (FGA))
CC       without inducing fibrin clotting and cleaves kininogen to produce
CC       bradykinin (KNG), resulting in the reduction of blood pressure.
CC       {ECO:0000269|PubMed:9546675}.
CC   -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP),
CC       PMSF and leupeptin. {ECO:0000269|PubMed:9546675}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not coagulate human plasma. Does not inhibit
CC       platelet aggregation induced by ADP or collagen (PubMed:9546675).
CC       {ECO:0000305|PubMed:9546675}.
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   AlphaFoldDB; P81176; -.
DR   SMR; P81176; -.
DR   MEROPS; S01.253; -.
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:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
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   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
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.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Hypotensive agent;
KW   Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..238
FT                   /note="Thrombin-like enzyme halystase"
FT                   /id="PRO_0000088728"
FT   DOMAIN          1..229
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        43
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        184
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        7..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        76..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        120..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        152..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   VARIANT         21..23
FT                   /note="PRS -> SRY"
SQ   SEQUENCE   238 AA;  26483 MW;  00C658067DE27586 CRC64;
     IIGGDECNIN EHRFLVALYT PRSRTLFCGG TLINQEWVLT AAHCDRKNFR IKLGMHSKKV
     PNKDEQTRVP KEKFFCLSSK NYTLWDKDIM LIRLDSPVKN STHIEPFSLP SSPPSVGSVC
     RIMGWGRISP TEETFPDVPH CVNINLLEYE MCRAPYPEFE LPATSRTLCA GILEGGKDTC
     RGDSGGPLIC NGQFQGIASW GDDPCAQPHK PAAYTKVFDH LDWIKSIIAG NTDASCPP