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Thrombin-like enzyme batroxobin (BX) (SVTLE) (EC 3.4.21.74) (Bothrops atrox serine proteinase) (Defibrase) (Fibrinogen-clotting enzyme) (Reptilase) (Snake venom serine protease) (SVSP) (Venombin A)

 VSPF_BOTAT              Reviewed;         255 AA.
P04971;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
10-MAY-2017, entry version 103.
RecName: Full=Thrombin-like enzyme batroxobin;
Short=BX;
Short=SVTLE;
EC=3.4.21.74;
AltName: Full=Bothrops atrox serine proteinase;
AltName: Full=Defibrase;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Reptilase;
AltName: Full=Snake venom serine protease;
Short=SVSP;
AltName: Full=Venombin A;
Flags: Precursor;
Bothrops atrox (Barba amarilla) (Fer-de-lance).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=8725;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=3546302;
Itoh N., Tanaka N., Mihashi S., Yamashina I.;
"Molecular cloning and sequence analysis of cDNA for batroxobin, a
thrombin-like snake venom enzyme.";
J. Biol. Chem. 262:3132-3135(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3163691;
Itoh N., Tanaka N., Funakoshi I., Kawasaki T., Mihashi S.,
Yamashina I.;
"Organization of the gene for batroxobin, a thrombin-like snake venom
enzyme. Homology with the trypsin/kallikrein gene family.";
J. Biol. Chem. 263:7628-7631(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3194214; DOI=10.1093/nar/16.21.10377;
Itoh N., Tanaka N., Funakoshi I., Kawasaki T., Mihashi S.,
Yamashima I.;
"The complete nucleotide sequence of the gene for batroxobin, a
thrombin-like snake venom enzyme.";
Nucleic Acids Res. 16:10377-10378(1988).
[4]
FUNCTION.
PubMed=1011993; DOI=10.1016/S0076-6879(76)45021-8;
Stocker K., Barlow G.H.;
"The coagulant enzyme from Bothrops atrox venom (batroxobin).";
Methods Enzymol. 45:214-223(1976).
[5]
STRUCTURE OF CARBOHYDRATE ON ASN-170 AND ASN-249.
PubMed=7737180; DOI=10.1111/j.1432-1033.1995.0805m.x;
Lochnit G., Geyer R.;
"Carbohydrate structure analysis of batroxobin, a thrombin-like serine
protease from Bothrops moojeni venom.";
Eur. J. Biochem. 228:805-816(1995).
-!- FUNCTION: Thrombin-like snake venom serine protease. Cleaves Arg-
Gly bonds in fibrinogen alpha chains (FGA).
{ECO:0000269|PubMed:1011993}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Xaa bond in
fibrinogen, to form fibrin, and release fibrinopeptide A. The
specificity of further degradation of fibrinogen varies with
species origin of the enzyme.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- BIOTECHNOLOGY: Is used for the investigation of the last phase of
blood coagulation. Due to its heparin insensitivity it can detect
fibrinogen polymerization disorders even in the presence of
heparin.
-!- PHARMACEUTICAL: Available under the name Defibrase (Pentapharm)
for the treatment of thrombotic diseases.
-!- MISCELLANEOUS: Does not cleave beta-chains of fibrinogen (FGB).
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=AAA48553.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J02684; AAA48552.1; -; mRNA.
EMBL; X12747; CAA31240.1; -; Genomic_DNA.
EMBL; M20894; AAA48553.1; ALT_SEQ; Genomic_DNA.
EMBL; M20890; AAA48553.1; JOINED; Genomic_DNA.
EMBL; M20891; AAA48553.1; JOINED; Genomic_DNA.
EMBL; M20892; AAA48553.1; JOINED; Genomic_DNA.
EMBL; M20893; AAA48553.1; JOINED; Genomic_DNA.
PIR; A28169; A28169.
ProteinModelPortal; P04971; -.
SMR; P04971; -.
MEROPS; S01.176; -.
KEGG; ag:AAA48552; -.
HOVERGEN; HBG013304; -.
KO; K20137; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation cascade activating toxin; Disulfide bond;
Glycoprotein; Hemostasis impairing toxin; Hydrolase; Pharmaceutical;
Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
SIGNAL 1 18 {ECO:0000250}.
PROPEP 19 24
/FTId=PRO_0000028379.
CHAIN 25 255 Thrombin-like enzyme batroxobin.
/FTId=PRO_0000028380.
DOMAIN 25 247 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system. {ECO:0000250}.
ACT_SITE 110 110 Charge relay system. {ECO:0000250}.
ACT_SITE 202 202 Charge relay system. {ECO:0000250}.
SITE 196 196 Required for specificity. {ECO:0000250}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
DISULFID 31 163 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 50 66 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 98 254 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 142 208 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 174 187 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 198 223 {ECO:0000255|PROSITE-ProRule:PRU00274}.
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


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