ID   VSPC_TRIAB              Reviewed;         258 AA.
AC   P0DJF6;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Thrombin-like enzyme chitribrisin;
DE            Short=SVTLE chitribrisin;
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 albolabris (White-lipped pit viper) (Cryptelytrops
OS   albolabris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=8765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=19303445; DOI=10.1016/j.pep.2009.03.005;
RA   Lin Y., Yu X., He Q., Li H., Li D., Song X., Wang Y., Wen H., Deng H.,
RA   Deng J.;
RT   "Expression and functional characterization of chitribrisin, a thrombin-
RT   like enzyme, in the venom of the Chinese green pit viper (Trimeresurus
RT   albolabris).";
RL   Protein Expr. Purif. 67:48-52(2009).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC   TISSUE=Venom;
RA   Deng M., Yu X.D., Chen X., Li H., Lin Y.X., He Q.Y., Liu J.P.;
RT   "Purification and characterization of fibrinolytic enzyme from the snake
RT   (T. albolabris) venom.";
RL   Zhongguo Sheng Hua Yao Wu Za Zhi 3:156-160(2008).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease that activates
CC       fibrinogen by releasing both fibrinopeptides A and B. Has also
CC       fibrinogenolytic activity, with a complete digestion of alpha chain
CC       (FGA) at 30 min and of beta chain (FGB) at 60 min.
CC       {ECO:0000269|PubMed:19303445, ECO:0000269|Ref.2}.
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA, but not PMSF and beta-
CC       mercaptoethanole. {ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not activate factor XIII, and does not degrade
CC       gamma chain of fibrinogen. {ECO:0000305|PubMed:19303445}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DJF6; -.
DR   SMR; P0DJF6; -.
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   Blood coagulation cascade activating toxin; Disulfide bond;
KW   Fibrinogenolytic toxin; Glycoprotein; Hemostasis impairing toxin;
KW   Hydrolase; 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_0000416394"
FT   CHAIN           25..258
FT                   /note="Thrombin-like enzyme chitribrisin"
FT                   /id="PRO_0000416395"
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        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
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;  28020 MW;  3FB900C92FEF2ADE CRC64;
     MMLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRSLV VLFNSSGALC GGTLINQEYV
     LTAAHCDMPN MQILLGVHSA SVLNDDEQAR DPEEKYFCLS SNNDTKWDKD IMLIRLNRPV
     NNSVHIAPLT LPSSPPRLGA ICRIMGWGAI TSPNETYPDA SQCANINILR YSLCQAVYRG
     MPAQSRIVCA GILRGGKGSC KGDSGGPLIC NAQLQGIVSA GGDPCAQPRV PVLYIRVFDY
     TDWIQSIIEG NRTVTCPP