VSPST_TRIST
ID VSPST_TRIST Reviewed; 260 AA.
AC Q8AY81;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Thrombin-like enzyme stejnobin;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Lee W.-H., Zhang Y.;
RT "Molecular cloning and sequence comparison of serine proteases from the
RT venom of Trimeresurus stejnegeri.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 25-34, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=9604287; DOI=10.1016/s0041-0101(97)00050-0;
RA Zhang Y., Gao R., Lee W.-H., Zhu S.-W., Xiong Y.-L., Wang W.-Y.;
RT "Characterization of a fibrinogen-clotting enzyme from Trimeresurus
RT stejnegeri venom, and comparative study with other venom proteases.";
RL Toxicon 36:131-142(1998).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that has
CC fibrinogen-clotting activity (FGA or FGB).
CC {ECO:0000269|PubMed:9604287}.
CC -!- ACTIVITY REGULATION: Its activity is inhibited by
CC diisopropylfluorophosphate (DFP) and PMSF, whereas EDTA has no effect
CC on it. {ECO:0000269|PubMed:9604287}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=250 uM for H-D-Phe-Pip-Arg-pNA (S-2238)
CC {ECO:0000269|PubMed:9604287};
CC KM=50 uM for H-D-Pro-Phe-Arg-pNA (S-2302)
CC {ECO:0000269|PubMed:9604287};
CC KM=125 uM for H-D-Val-Leu-Arg-pNA (S-2266)
CC {ECO:0000269|PubMed:9604287};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9604287}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9604287}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:9604287}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9604287}.
CC -!- MISCELLANEOUS: Does not act on factor X, prothrombin and plasminogen.
CC {ECO:0000305|PubMed:9604287}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF545576; AAN52347.1; -; mRNA.
DR AlphaFoldDB; Q8AY81; -.
DR SMR; Q8AY81; -.
DR MEROPS; S01.181; -.
DR SABIO-RK; Q8AY81; -.
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 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 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.
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; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000296309"
FT CHAIN 25..260
FT /note="Thrombin-like enzyme stejnobin"
FT /id="PRO_0000296310"
FT DOMAIN 25..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 67
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 52..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 102..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 144..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 176..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 202..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 260 AA; 29328 MW; F1339FBB8F848A57 CRC64;
MMLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRFLV ALYDFWSGDF LCGGTLINQE
YVLTAAHCKT RNMYIYLGMH NKSVQFDDEQ RRYPKKKYFF RCRNNFTRWD KDIMLIRLNR
PVRNSAHIAP LSLPSSPPTV GSVCRVMGWG TITSPNETLP DVPRCANINL FNYTVCHGVF
PWLPARSRIL CAGVLQGGID TCKRDSGGPL ICNGQFQGIV SWGPKPCAQP RKPALYTKVF
DHLDWIQSII AGNTTVTCPP
