[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; PubMed=3546302 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1093/nar/16.21.10377; PubMed=3194214 [NCBI, ExPASy, EBI, Israel, Japan] 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]	CHARACTERIZATION. DOI=10.1016/S0076-6879(76)45021-8; PubMed=1011993 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Thrombin-like snake venom serine protease. Cleaves Arg-Gly bonds in fibrinogen alpha chains; does not cleave fibrinogen beta chains.
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.
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.
SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02684; AAA48552.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X12747; CAA31240.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20894; AAA48553.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20890; AAA48553.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20891; AAA48553.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20892; AAA48553.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20893; AAA48553.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A28169; A28169.

3D structure databases

HSSP

P00760; 1EZX. [HSSP ENTRY / PDB]

ModBase

P04971.

Protein family/group databases

MEROPS

S01.176; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

P04971; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Glycoprotein; Hydrolase; Pharmaceutical; Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`By similarity.`
`PROPEP`	`19 24`	`6`		`PRO_0000028379`
`CHAIN`	`25 255`	`231`	`Thrombin-like enzyme batroxobin.`	`PRO_0000028380`
`DOMAIN`	`25 247`	`223`	`Peptidase S1.`
`ACT_SITE`	`65 65`		`Charge relay system (By similarity).`
`ACT_SITE`	`110 110`		`Charge relay system (By similarity).`
`ACT_SITE`	`202 202`		`Charge relay system (By similarity).`
`SITE`	`196 196`	`1`	`Required for specificity (By similarity).`
`CARBOHYD`	`170 170`		`N-linked (GlcNAc...).`
`CARBOHYD`	`249 249`		`N-linked (GlcNAc...).`
`DISULFID`	`31 163`		`By similarity.`
`DISULFID`	`50 66`		`By similarity.`
`DISULFID`	`98 254`		`By similarity.`
`DISULFID`	`142 208`		`By similarity.`
`DISULFID`	`174 187`		`By similarity.`
`DISULFID`	`198 223`		`By similarity.`

Sequence information

Length: 255 AA [This is the length of the unprocessed precursor]

Molecular weight: 28189 Da [This is the MW of the unprocessed precursor]

CRC64: BE155BBC5DF8431B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLIRVIANL LILQVSYAQK SSELVIGGDE CDINEHPFLA FMYYSPRYFC GMTLINQEWV 

        70         80         90        100        110        120 
LTAAHCNRRF MRIHLGKHAG SVANYDEVVR YPKEKFICPN KKKNVITDKD IMLIRLDRPV 

       130        140        150        160        170        180 
KNSEHIAPLS LPSNPPSVGS VCRIMGWGAI TTSEDTYPDV PHCANINLFN NTVCREAYNG 

       190        200        210        220        230        240 
LPAKTLCAGV LQGGIDTCGG DSGGPLICNG QFQGILSWGS DPCAEPRKPA FYTKVFDYLP 

       250 
WIQSIIAGNK TATCP

P04971 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools