ID   VSP2_LACMR              Reviewed;          30 AA.
AC   C0HLA1;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Thrombin-like enzyme LmrSP-2 {ECO:0000303|PubMed:31131000};
DE            Short=SVTLE {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:P33589};
DE   AltName: Full=Snake venom serine protease {ECO:0000305};
DE            Short=SVSP {ECO:0000305};
DE   Flags: Fragment;
OS   Lachesis muta rhombeata (Bushmaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX   NCBI_TaxID=60219 {ECO:0000303|PubMed:31131000};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:31131000};
RX   PubMed=31131000; DOI=10.1590/1678-9199-jvatitd-1470-18;
RA   Wiezel G.A., Bordon K.C., Silva R.R., Gomes M.S., Cabral H.,
RA   Rodrigues V.M., Ueberheide B., Arantes E.C.;
RT   "Subproteome of Lachesis muta rhombeata venom and preliminary studies on
RT   LmrSP-4, a novel snake venom serine proteinase.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 25:E147018-E147018(2019).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease that cleaves alpha-
CC       chain of fibrinogen (FGA) releases only fibrinopeptide A. Shows
CC       coagulant, esterase and amidase activities.
CC       {ECO:0000250|UniProtKB:P33589}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31131000}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31131000}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HLA1; -.
DR   SMR; C0HLA1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Fibrinogenolytic toxin; Hemostasis impairing toxin; Hydrolase; Protease;
KW   Secreted; Serine protease; Toxin.
FT   CHAIN           1..>30
FT                   /note="Thrombin-like enzyme LmrSP-2"
FT                   /evidence="ECO:0000269|PubMed:31131000"
FT                   /id="PRO_0000447685"
FT   NON_TER         30
FT                   /evidence="ECO:0000305|PubMed:31131000"
SQ   SEQUENCE   30 AA;  3273 MW;  4B687BC6C5703276 CRC64;
     VIGGDECNIN EHRFLVALYD PDGFFCGGTL