ID   VSP2_TRIAB              Reviewed;         260 AA.
AC   A7LAC7;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Thrombin-like enzyme 2;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Green pit viper thrombin-like enzyme 2;
DE            Short=GPV-TL2;
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].
RX   PubMed=16373075; DOI=10.1016/j.toxicon.2005.11.003;
RA   Rojnuckarin P., Muanpasitporn C., Chanhome L., Arpijuntarangkoon J.,
RA   Intragumtornchai T.;
RT   "Molecular cloning of novel serine proteases and phospholipases A2 from
RT   green pit viper (Trimeresurus albolabris) venom gland cDNA library.";
RL   Toxicon 47:279-287(2006).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; EF690366; ABS12075.1; -; mRNA.
DR   AlphaFoldDB; A7LAC7; -.
DR   SMR; A7LAC7; -.
DR   MEROPS; S01.181; -.
DR   PRIDE; A7LAC7; -.
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   2: Evidence at transcript level;
KW   Blood coagulation cascade activating toxin; Disulfide bond; 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_0000416388"
FT   CHAIN           25..260
FT                   /note="Thrombin-like enzyme 2"
FT                   /id="PRO_0000416389"
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        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;  29319 MW;  864461ADFFED29AF CRC64;
     MMLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRFLV ALYDVWSGDF LCGGTLINKE
     YVLTAAHCET RNMYIYLGMH NKMYQFDDEQ RRYPKKKYFF RCSNNFTRWD KDIMLIRLNR
     PVRNSEHIAP LSLPSSPPSV GSVCRVMGWG TITSPNETLP DVPRCANINL LNYTVCRGVF
     PRLPARSRTL CAGVLQGGID TCKRDSGGPL ICNGKLQGVV FWGPKPCAQP RKPALYTKVF
     DHLDWIQSII AGNTTVTCPP