VSP21_CRODU
ID VSP21_CRODU Reviewed; 238 AA.
AC Q58G94;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Thrombin-like enzyme gyroxin B2.1;
DE Short=SVTLE gyroxin B2.1;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
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], AND FUNCTION.
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 (FGA) to fibrin (By similarity). Shows
CC coagulant, esterase and amidase activities. 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, ECO:0000269|PubMed:19341755,
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; AY954040; AAX54679.1; -; mRNA.
DR AlphaFoldDB; Q58G94; -.
DR SMR; Q58G94; -.
DR MEROPS; S01.181; -.
DR PRIDE; Q58G94; -.
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 Toxin.
FT CHAIN 1..238
FT /note="Thrombin-like enzyme gyroxin B2.1"
FT /id="PRO_5000095392"
FT DOMAIN 1..229
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 184
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 28..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 78..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 120..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 180..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 238 AA; 26585 MW; 5A28015D41CCDDB5 CRC64;
VIGGDECNIN ERNFLVALYE YWSQSFLCGG TLINGEWVLT AAHCDRKHIL IYVGVHDRSV
QFDKEQRRFP KEKYFFNCRN NFTKWDKDIM LIRLNKPVSY SEHIAPLSLP SSPPIVGSVC
RVMGWGTIKS PQETLPDVPH CANINLLDYG VCRTAHPQFR LPATSRILCA GVLEGGIDTC
HRDSGGPLIC NGEFQGIVSW GDGSCAQPDK PALYSKVFDH LDWIQNIIAG SETVNCPS
