VSPS2_TRIST
ID VSPS2_TRIST Reviewed; 258 AA.
AC Q8AY79;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Beta-fibrinogenase stejnefibrase-2;
DE EC=3.4.21.-;
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 FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=9637365; DOI=10.1016/s0041-0101(97)00150-5;
RA Gao R., Zhang Y., Meng Q.-X., Lee W.-H., Li D.-S., Xiong Y.-L., Wang W.-Y.;
RT "Characterization of three fibrinogenolytic enzymes from Chinese green tree
RT viper (Trimeresurus stejnegeri) venom.";
RL Toxicon 36:457-467(1998).
CC -!- FUNCTION: Snake venom serine protease that degrades preferentially
CC beta-chain of fibrinogen (FGB). {ECO:0000269|PubMed:9637365}.
CC -!- ACTIVITY REGULATION: Its activity is inhibited by PMSF and p-
CC nitrophenyl-p-guanidinobenzoate (NPGB). {ECO:0000269|PubMed:9637365}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=95 uM for S-2238 {ECO:0000269|PubMed:9637365};
CC KM=91 uM for S-2302 {ECO:0000269|PubMed:9637365};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9637365}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9637365}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:9637365}.
CC -!- MISCELLANEOUS: Does not degrade the gamma-chain of fibrinogen, does not
CC activate plasminogen and does not possess fibrinogen-clotting activity.
CC {ECO:0000305|PubMed:9637365}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF545578; AAN52349.1; -; mRNA.
DR AlphaFoldDB; Q8AY79; -.
DR SMR; Q8AY79; -.
DR MEROPS; S01.347; -.
DR SABIO-RK; Q8AY79; -.
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 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 Disulfide bond; Fibrinogenolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000295846"
FT CHAIN 25..258
FT /note="Beta-fibrinogenase stejnefibrase-2"
FT /id="PRO_0000295847"
FT DOMAIN 25..249
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 98..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 200..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 258 AA; 28028 MW; 2D65C42A30026D28 CRC64;
MELIRVLANL LILQLSYAQK SSELVVGGDE CNINEHRSLV AIFNSTGFFC SGTLINQEWV
VTAAHCDSKN FKMKFGAHSK KLLNEDEQIR NPKEKFICPN KKNNDVLDKD IMLIKLDSSV
SNSEHIAPLS LPSSPPSVGS DCRIIGWGSI TPIEVTYPDV PYCANINLLD DAECKPGYPE
LLPEYRTLCA GIVEGGKDTC GGDSGGPLIC NGQFHGIVSY GGHPCGQSLK PGIYTKVFDY
NDWMKSIIAG NTAATCPP