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