ID   VSPF_LACMR              Reviewed;          30 AA.
AC   Q9PRP4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Thrombin-like enzyme LMR-47;
DE            Short=SVTLE LM-47;
DE            Short=SVTLE LMR-47;
DE            EC=3.4.21.74;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Gyroxin analog;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   AltName: Full=Venombin A;
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;
RN   [1]
RP   PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=8783450; DOI=10.1016/0041-0101(95)00159-x;
RA   Aguiar A.S., Alves C.R., Melgarejo A., Giovanni-de-Simone S.;
RT   "Purification and partial characterization of a thrombin-like/gyroxin
RT   enzyme from bushmaster (Lachesis muta rhombeata) venom.";
RL   Toxicon 34:555-565(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-25.
RC   TISSUE=Venom;
RX   PubMed=15994137; DOI=10.1016/j.jchromb.2005.04.018;
RA   De-Simone S.G., Correa-Netto C., Antunes O.A., De-Alencastro R.B.,
RA   Silva F.P. Jr.;
RT   "Biochemical and molecular modeling analysis of the ability of two p-
RT   aminobenzamidine-based sorbents to selectively purify serine proteases
RT   (fibrinogenases) from snake venoms.";
RL   J. Chromatogr. B 822:1-9(2005).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease that specifically
CC       hydrolyzes the Aalpha chain of fibrinogen (FGA). Exhibits strong N-p-
CC       tosyl-L-arginine methyl esterase activity, and hydrolyzes tripeptide
CC       nitroanilide derivatives weakly or not at all.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form
CC         fibrin, and release fibrinopeptide A. The specificity of further
CC         degradation of fibrinogen varies with species origin of the enzyme.;
CC         EC=3.4.21.74;
CC   -!- ACTIVITY REGULATION: Inactivated by antipain, PMSF, TPCK, leupeptin,
CC       pepstatin, EDTA, and E-64 (trans-epoxysuccinylleucylamido(4-
CC       guanidino)butane).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12 uM for N-p-tosyl-L-arginine methyl ester (TAME)
CC         {ECO:0000269|PubMed:8783450};
CC         KM=589 uM for NBz-Pro-Phe-Arg-pNA {ECO:0000269|PubMed:8783450};
CC         KM=1320 uM for NBz-Val-Gly-Arg-pNA {ECO:0000269|PubMed:8783450};
CC         KM=857 uM for NBz-DL-Arg-pNA {ECO:0000269|PubMed:8783450};
CC         Vmax=877.0 nmol/sec/mg enzyme for N-p-tosyl-L-arginine methyl ester
CC         (TAME) {ECO:0000269|PubMed:8783450};
CC         Vmax=51.0 nmol/sec/mg enzyme for NBz-Pro-Phe-Arg-pNA
CC         {ECO:0000269|PubMed:8783450};
CC         Vmax=75.0 nmol/sec/mg enzyme for NBz-Val-Gly-Arg-pNA
CC         {ECO:0000269|PubMed:8783450};
CC         Vmax=39.3 nmol/sec/mg enzyme for NBz-DL-Arg-pNA
CC         {ECO:0000269|PubMed:8783450};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:8783450}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; Q9PRP4; -.
DR   SMR; Q9PRP4; -.
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.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Fibrinogenolytic toxin; Glycoprotein; Hemostasis impairing toxin;
KW   Hydrolase; Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>30
FT                   /note="Thrombin-like enzyme LMR-47"
FT                   /id="PRO_0000295178"
FT   DOMAIN          1..>30
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3171 MW;  FA1B2609921853DB CRC64;
     VIGGDECNIN EHRFLVALYD GLSGTFLCGG