VSP17_CRODU
ID VSP17_CRODU Reviewed; 259 AA.
AC B0FXM3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Thrombin-like enzyme gyroxin B1.7;
DE Short=SVTLE gyroxin B1.7;
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 Crotalus durissus terrificus (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8732;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19341755; DOI=10.1016/j.toxicon.2009.03.022;
RA Yonamine C.M., Prieto-da-Silva A.R., Magalhaes G.S., Radis-Baptista G.,
RA Morganti L., Ambiel F.C., Chura-Chambi R.M., Yamane T., Camillo M.A.;
RT "Cloning of serine protease cDNAs from Crotalus durissus terrificus venom
RT gland and expression of a functional Gyroxin homologue in COS-7 cells.";
RL Toxicon 54:110-120(2009).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=20637222; DOI=10.1016/j.toxicon.2010.06.027;
RA Alves da Silva J.A., Oliveira K.C., Camillo M.A.;
RT "Gyroxin increases blood-brain barrier permeability to Evans blue dye in
RT mice.";
RL Toxicon 57:162-167(2011).
CC -!- FUNCTION: Thrombin-like snake venom serine protease. Displays a
CC specificity similar to trypsin. Releases only fibrinopeptide A in the
CC conversion of fibrinogen to fibrin. Shows coagulant, esterase and
CC amidase activities (By similarity). Reversibly increases the
CC permeability of the blood brain barrier (BBB) in mice. Induces the
CC barrel rotation syndrome in mice, which is manifested by gyroxin-like,
CC rapid rolling motions. This syndrome may be due to its effect on BBB
CC permeability, and certainly also to other actions affecting endogenous
CC substrates present in the endothelium, nervous tissues or blood.
CC {ECO:0000250, ECO:0000269|PubMed:11137545,
CC ECO:0000269|PubMed:20637222}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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}.
CC -!- CAUTION: Information taken from PubMed:20637222 and PubMed:11137545 are
CC not linked to a specific sequence. Hence, it is not sure whether the
CC function corresponds to this protein or to a paralog. {ECO:0000305}.
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DR EMBL; EU360954; ABY65931.1; -; mRNA.
DR AlphaFoldDB; B0FXM3; -.
DR SMR; B0FXM3; -.
DR MEROPS; S01.497; -.
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.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..259
FT /evidence="ECO:0000250"
FT /id="PRO_5000301408"
FT CHAIN 25..259
FT /note="Thrombin-like enzyme gyroxin B1.7"
FT /id="PRO_5000301409"
FT DOMAIN 25..250
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 201..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 259 AA; 28184 MW; 254E25D4F7F8FC80 CRC64;
MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRLLA IVYTNSSQCA GTLINQEWVL
TAAHCDGENM DIYLGVHNES VQYDDEEGRV AAEKFFCLSS RNYTKWDKDI MLIRLNIPVR
NSTHIAPLSL PSSPPSVGSV CRVMGWGTIT SPNETYPDVP HCANINLFDY EVCLAAYPEF
GLPATSRTLC AGIQQGGKDT CGSDSGGSLI CNGQFQGIVS WGDNPCAQPH KPALYTKVLD
DTEWIQSIIA GNTAVTCPP
