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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
 
 
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