VSP13_CRODU
ID VSP13_CRODU Reviewed; 262 AA.
AC B0FXM1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Thrombin-like enzyme gyroxin B1.3;
DE Short=SVTLE gyroxin B1.3;
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).
RN [4]
RP FUNCTION.
RX PubMed=32161292; DOI=10.1038/s41598-020-61258-x;
RA Boldrini-Franca J., Pinheiro-Junior E.L., Peigneur S., Pucca M.B.,
RA Cerni F.A., Borges R.J., Costa T.R., Carone S.E.I., Fontes M.R.M.,
RA Sampaio S.V., Arantes E.C., Tytgat J.;
RT "Beyond hemostasis: a snake venom serine protease with potassium channel
RT blocking and potential antitumor activities.";
RL Sci. Rep. 10:4476-4476(2020).
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. Reversibly increases the
CC permeability of the blood brain barrier (BBB) in mice (PubMed:11137545,
CC PubMed:20637222). Induces the barrel rotation syndrome in mice, which
CC is manifested by gyroxin-like, rapid rolling motions (PubMed:11137545,
CC PubMed:20637222). 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 (PubMed:11137545, PubMed:20637222). Also shows a moderate inhibitory
CC activity on the human voltage-gated potassium channel Kv10.1/KCNH1/EAG1
CC (58% current inhibition at 5 uM) (PubMed:32161292). It blocks
CC Kv10.1/KCNH1/EAG1 in a time and dose-dependent manner and with a
CC mechanism independent of its enzymatic activity (By similarity). It may
CC have a preference in interacting with Kv10.1/KCNH1/EAG1 in its closed
CC state, since the inhibitory effect of the toxin is decreased at more
CC depolarized potentials (By similarity).
CC {ECO:0000250|UniProtKB:A0A0S4FKT4, ECO:0000269|PubMed:11137545,
CC ECO:0000269|PubMed:20637222, ECO:0000269|PubMed:32161292}.
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; EU360951; ABY65929.1; -; mRNA.
DR AlphaFoldDB; B0FXM1; -.
DR SMR; B0FXM1; -.
DR MEROPS; S01.181; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
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; Ion channel impairing toxin;
KW Potassium channel impairing toxin; Protease; Secreted; Serine protease;
KW Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..262
FT /evidence="ECO:0000250"
FT /id="PRO_5000301404"
FT CHAIN 25..262
FT /note="Thrombin-like enzyme gyroxin B1.3"
FT /id="PRO_5000301405"
FT DOMAIN 25..253
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 67
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 52..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 102..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 144..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 176..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 204..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 262 AA; 29347 MW; D494E637B2F4E3C5 CRC64;
MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHNFLV ALYEYWSQSF LCGGTLINGE
WVLTAAHCDR KHILIYVGVH DRSVQFDKEQ RRFPKEKYFF NCRNNFTKWD KDIMLIRLNK
PVSYSEHIAP LSLPSSPPIV GSVCRVMGWG TIKSPQETLP DVPHCANINL LDYEVCRTAH
PQFRLPATSR ILCAGVLEGG IDTCHRDSGG PLICNGEFQG IVSWGDGPCA QPDKPALYSK
VFDHLDWIQN IIAGSETVNC PS
