VSPF_BOTAT
ID VSPF_BOTAT Reviewed; 255 AA.
AC P04971;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Thrombin-like enzyme batroxobin;
DE Short=BX;
DE Short=SVTLE;
DE EC=3.4.21.74;
DE AltName: Full=Bothrops atrox serine proteinase;
DE AltName: Full=Defibrase;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Reptilase;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Venombin A;
DE Flags: Precursor;
OS Bothrops atrox (Barba amarilla) (Fer-de-lance).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8725;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=3546302; DOI=10.1016/s0021-9258(18)61479-6;
RA Itoh N., Tanaka N., Mihashi S., Yamashina I.;
RT "Molecular cloning and sequence analysis of cDNA for batroxobin, a
RT thrombin-like snake venom enzyme.";
RL J. Biol. Chem. 262:3132-3135(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3163691; DOI=10.1016/s0021-9258(18)68544-8;
RA Itoh N., Tanaka N., Funakoshi I., Kawasaki T., Mihashi S., Yamashina I.;
RT "Organization of the gene for batroxobin, a thrombin-like snake venom
RT enzyme. Homology with the trypsin/kallikrein gene family.";
RL J. Biol. Chem. 263:7628-7631(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3194214; DOI=10.1093/nar/16.21.10377;
RA Itoh N., Tanaka N., Funakoshi I., Kawasaki T., Mihashi S., Yamashima I.;
RT "The complete nucleotide sequence of the gene for batroxobin, a thrombin-
RT like snake venom enzyme.";
RL Nucleic Acids Res. 16:10377-10378(1988).
RN [4]
RP FUNCTION.
RX PubMed=1011993; DOI=10.1016/s0076-6879(76)45021-8;
RA Stocker K., Barlow G.H.;
RT "The coagulant enzyme from Bothrops atrox venom (batroxobin).";
RL Methods Enzymol. 45:214-223(1976).
RN [5]
RP GLYCOSYLATION AT ASN-170 AND ASN-249, AND STRUCTURE OF CARBOHYDRATE ON
RP ASN-170 AND ASN-249.
RX PubMed=7737180; DOI=10.1111/j.1432-1033.1995.0805m.x;
RA Lochnit G., Geyer R.;
RT "Carbohydrate structure analysis of batroxobin, a thrombin-like serine
RT protease from Bothrops moojeni venom.";
RL Eur. J. Biochem. 228:805-816(1995).
CC -!- FUNCTION: Thrombin-like snake venom serine protease. Cleaves Arg-Gly
CC bonds in fibrinogen alpha chains (FGA). {ECO:0000269|PubMed:1011993}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- BIOTECHNOLOGY: Is used for the investigation of the last phase of blood
CC coagulation. Due to its heparin insensitivity it can detect fibrinogen
CC polymerization disorders even in the presence of heparin.
CC -!- PHARMACEUTICAL: Available under the name Defibrase (Pentapharm) for the
CC treatment of thrombotic diseases.
CC -!- MISCELLANEOUS: Does not cleave beta-chains of fibrinogen (FGB).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA48553.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J02684; AAA48552.1; -; mRNA.
DR EMBL; X12747; CAA31240.1; -; Genomic_DNA.
DR EMBL; M20894; AAA48553.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M20890; AAA48553.1; JOINED; Genomic_DNA.
DR EMBL; M20891; AAA48553.1; JOINED; Genomic_DNA.
DR EMBL; M20892; AAA48553.1; JOINED; Genomic_DNA.
DR EMBL; M20893; AAA48553.1; JOINED; Genomic_DNA.
DR PIR; A28169; A28169.
DR AlphaFoldDB; P04971; -.
DR SMR; P04971; -.
DR MEROPS; S01.176; -.
DR GlyConnect; 68; 1 N-Linked glycan.
DR iPTMnet; P04971; -.
DR KEGG; ag:AAA48552; -.
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 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; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Pharmaceutical; Protease; Secreted;
KW Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /id="PRO_0000028379"
FT CHAIN 25..255
FT /note="Thrombin-like enzyme batroxobin"
FT /id="PRO_0000028380"
FT DOMAIN 25..247
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7737180"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7737180"
FT DISULFID 31..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 98..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 198..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 255 AA; 28189 MW; BE155BBC5DF8431B CRC64;
MVLIRVIANL LILQVSYAQK SSELVIGGDE CDINEHPFLA FMYYSPRYFC GMTLINQEWV
LTAAHCNRRF MRIHLGKHAG SVANYDEVVR YPKEKFICPN KKKNVITDKD IMLIRLDRPV
KNSEHIAPLS LPSNPPSVGS VCRIMGWGAI TTSEDTYPDV PHCANINLFN NTVCREAYNG
LPAKTLCAGV LQGGIDTCGG DSGGPLICNG QFQGILSWGS DPCAEPRKPA FYTKVFDYLP
WIQSIIAGNK TATCP
