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Thrombin-like enzyme stejnobin (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)

 VSPST_TRIST             Reviewed;         260 AA.
Q8AY81;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 70.
RecName: Full=Thrombin-like enzyme stejnobin;
Short=SVTLE;
EC=3.4.21.-;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Flags: Precursor;
Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
stejnegeri).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Trimeresurus.
NCBI_TaxID=39682;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Lee W.-H., Zhang Y.;
"Molecular cloning and sequence comparison of serine proteases from
the venom of Trimeresurus stejnegeri.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 25-34, FUNCTION, ACTIVITY REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND GLYCOSYLATION.
TISSUE=Venom;
PubMed=9604287; DOI=10.1016/S0041-0101(97)00050-0;
Zhang Y., Gao R., Lee W.-H., Zhu S.-W., Xiong Y.-L., Wang W.-Y.;
"Characterization of a fibrinogen-clotting enzyme from Trimeresurus
stejnegeri venom, and comparative study with other venom proteases.";
Toxicon 36:131-142(1998).
-!- FUNCTION: Thrombin-like snake venom serine protease that has
fibrinogen-clotting activity (FGA or FGB).
{ECO:0000269|PubMed:9604287}.
-!- ACTIVITY REGULATION: Its activity is inhibited by
diisopropylfluorophosphate (DFP) and PMSF, whereas EDTA has no
effect on it. {ECO:0000269|PubMed:9604287}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=250 uM for H-D-Phe-Pip-Arg-pNA (S-2238)
{ECO:0000269|PubMed:9604287};
KM=50 uM for H-D-Pro-Phe-Arg-pNA (S-2302)
{ECO:0000269|PubMed:9604287};
KM=125 uM for H-D-Val-Leu-Arg-pNA (S-2266)
{ECO:0000269|PubMed:9604287};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9604287}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9604287}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:9604287}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:9604287}.
-!- MISCELLANEOUS: Does not act on factor X, prothrombin and
plasminogen. {ECO:0000305|PubMed:9604287}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AF545576; AAN52347.1; -; mRNA.
ProteinModelPortal; Q8AY81; -.
SMR; Q8AY81; -.
MEROPS; S01.181; -.
HOVERGEN; HBG013304; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
1: Evidence at protein level;
Blood coagulation cascade activating toxin; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 24 {ECO:0000250}.
/FTId=PRO_0000296309.
CHAIN 25 260 Thrombin-like enzyme stejnobin.
/FTId=PRO_0000296310.
DOMAIN 25 251 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 67 67 Charge relay system. {ECO:0000250}.
ACT_SITE 112 112 Charge relay system. {ECO:0000250}.
ACT_SITE 206 206 Charge relay system. {ECO:0000250}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 165 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 52 68 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 102 258 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 144 212 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 176 191 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 202 227 {ECO:0000255|PROSITE-ProRule:PRU00274}.
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


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