VSPF_LACMU
ID VSPF_LACMU Reviewed; 228 AA.
AC P33589;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Thrombin-like enzyme gyroxin analog;
DE Short=LM-TL;
DE Short=SVTLE;
DE EC=3.4.21.74;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Venombin A;
OS Lachesis muta muta (Bushmaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX NCBI_TaxID=8753;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=8354384; DOI=10.1016/0014-5793(93)80205-9;
RA Magalhaes A., Campos-Brasil da Fonseca B., Ribeiro Diniz C., Gilroy J.,
RA Richarson M.;
RT "The complete amino acid sequence of a thrombin-like enzyme/gyroxin
RT analogue from venom of the bushmaster snake (Lachesis muta muta).";
RL FEBS Lett. 329:116-120(1993).
RN [2]
RP PROTEIN SEQUENCE, SUBUNIT, AND 3D-STRUCTURE MODELING.
RX PubMed=11410274; DOI=10.1016/s0167-4838(01)00177-7;
RA Castro H.C., Silva D.M., Craik C., Zingali R.B.;
RT "Structural features of a snake venom thrombin-like enzyme: thrombin and
RT trypsin on a single catalytic platform?";
RL Biochim. Biophys. Acta 1547:183-195(2001).
RN [3]
RP FUNCTION.
RX PubMed=11137545; DOI=10.1016/s0041-0101(00)00222-1;
RA Camillo M.A., Arruda Paes P.C., Troncone L.R., Rogero J.R.;
RT "Gyroxin fails to modify in vitro release of labelled dopamine and
RT acetylcholine from rat and mouse striatal tissue.";
RL Toxicon 39:843-853(2001).
RN [4]
RP PROTEIN SEQUENCE OF 1-25, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=2781576; DOI=10.1016/0041-0101(89)90043-3;
RA da Silva N.J., Aird S.D., Seebart C., Kaiser I.I.;
RT "A gyroxin analog from the venom of the bushmaster (Lachesis muta muta).";
RL Toxicon 27:763-771(1989).
CC -!- FUNCTION: Thrombin-like snake venom serine protease, that cleaves
CC alpha-chain of fibrinogen (FGA) releases only fibrinopeptide A. Shows
CC coagulant, esterase and amidase activities. Induces the barrel rotation
CC syndrome in mice, which is manifested by gyroxin-like, rapid rolling
CC motions. May also reversibly increase the permeability of the blood
CC brain barrier (BBB) in mice. {ECO:0000269|PubMed:11137545,
CC ECO:0000269|PubMed:2781576, ECO:0000269|PubMed:8354384}.
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: Inhibited competitively by amidines and
CC guanidines, and irreversibly inhibited by diisopropylfluorophosphate.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11410274}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not have phospholipase activity, does not aggregate
CC platelet, and does not affect the release of the neurotransmitters
CC dopamine and acetylcholine in the nervous system.
CC {ECO:0000305|PubMed:11137545}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; S35689; S35689.
DR AlphaFoldDB; P33589; -.
DR SMR; P33589; -.
DR MEROPS; S01.432; -.
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 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.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Protease; Secreted; Serine protease; Toxin.
FT CHAIN 1..228
FT /note="Thrombin-like enzyme gyroxin analog"
FT /id="PRO_0000088740"
FT DOMAIN 1..222
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 43
FT /note="Charge relay system"
FT ACT_SITE 88
FT /note="Charge relay system"
FT ACT_SITE 177
FT /note="Charge relay system"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 28..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 78..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 117..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 149..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 102
FT /note="E -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="N -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 25629 MW; DA52305D2995C52D CRC64;
VIGGDECNIN EHRFLVALYD GLSGTFLCGG TLINQEWVLT AQHCNRSLMN IYLGMHNKNV
KFDDEQRRYP KKKYFFRCNK NFTKWDEDIR LNRPVRFSAH IEPLSLPSNP PSEDSVCRVM
GWGQITSPPE TLPDVPHCAN INLFNYTVCR GAYPRMPTKV LCAGVLEGGI DTCNRDSGGP
LICNGQFQGI VFWGPDPCAQ PDKPGVYTKV FDYLDWIQSV IAGNTTCS
