VSPL_BOTAS
ID VSPL_BOTAS Reviewed; 259 AA.
AC Q072L6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Thrombin-like enzyme asperase;
DE Short=SVTLE;
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 Bothrops asper (Terciopelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8722;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Arce V., Azofeifa G., Flores M., Alape A.;
RT "Molecular cloning and sequence analysis of a thrombin-like enzyme from
RT Bothops asper snake venom.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 25-72, MASS SPECTROMETRY, FUNCTION, ACTIVITY
RP REGULATION, AND SIALIC ACID.
RC TISSUE=Venom;
RX PubMed=17994164; DOI=10.1590/s0100-879x2006005000189;
RA Perez A.V., Rucavado A., Sanz L., Calvete J.J., Gutierrez J.M.;
RT "Isolation and characterization of a serine proteinase with thrombin-like
RT activity from the venom of the snake Bothrops asper.";
RL Braz. J. Med. Biol. Res. 41:12-17(2008).
CC -!- FUNCTION: Snake venom serine protease that clots human plasma and
CC bovine fibrinogen. Upon intravenous injection in mice, this protease
CC renders blood unclottable (defibri(ogen)ation). Intravenous
CC administration (10 and 5 ug) induces a gyroxin-like effect: loss of the
CC righting reflex, opisthotonus, and intermittent rotations over the long
CC axis of the body. These effects persisted during approximately 10
CC minutes, after which the animals apparently recovers.
CC {ECO:0000269|PubMed:17994164}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:17994164}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The different mass observed by mass spectrometry may represent 3
CC different glycoforms that bear a single non- (27066), mono- (27357),
CC and di-sialylated (27649), fucosylated complex-type dianntenary glycan
CC chain. {ECO:0000269|PubMed:17994164}.
CC -!- MASS SPECTROMETRY: Mass=27066; Method=MALDI; Note=Glycoform 1.;
CC Evidence={ECO:0000269|PubMed:17994164};
CC -!- MASS SPECTROMETRY: Mass=27357; Method=MALDI; Note=Glycoform 2.;
CC Evidence={ECO:0000269|PubMed:17994164};
CC -!- MASS SPECTROMETRY: Mass=27649; Method=MALDI; Note=Glycoform 3.;
CC Evidence={ECO:0000269|PubMed:17994164};
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; DQ247724; ABB76280.1; -; mRNA.
DR AlphaFoldDB; Q072L6; -.
DR SMR; Q072L6; -.
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; IPR033116; TRYPSIN_SER.
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; PS00135; TRYPSIN_SER; 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; Sialic acid; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:17994164"
FT /id="PRO_0000294984"
FT CHAIN 25..259
FT /note="Thrombin-like enzyme asperase"
FT /id="PRO_0000294985"
FT DOMAIN 25..250
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 82..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 99..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 143..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 201..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 259 AA; 28019 MW; 2809853F0F5487F8 CRC64;
MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRSLV VLFNSSGFLC AGTLVQDEWV
LTAANCDSKN FQMQLGVHSK KVLNEDEQTR DPKEEASLCP NRKKDDEVDK DIMLIKLDSR
VSNSEHIAPL SLPSSPPSVG SVCRIMGWGT ISPTKETYPD VPHCANINIL DHAVCRAAYP
WQPVSSTTLC AGILQGGKDT CWGDSGGPLI CNGEFQGIVS WGAHPCGQPH NPGVYTKVSD
YTEWIKSIIA GNTAAACPP
