PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
TISSUE=Venom;
DOI=10.1016/0041-0101(95)00159-X; PubMed=8783450 [NCBI, ExPASy, EBI, Israel, Japan]
Aguiar A.S., Alves C.R., Melgarejo A., Giovanni-de-Simone S.;
"Purification and partial characterization of a thrombin-like/gyroxin enzyme from bushmaster (Lachesis muta rhombeata) venom.";
Toxicon 34:555-565(1996).

Comments

FUNCTION: Thrombin-like snake venom serine protease. Exhibits strong N-p-tosyl-L-arginine methyl esterase activity, hydrolyzes tripeptide nitroanilide derivatives weakly or not at all, and specifically hydrolyzes the alpha chain of fibrinogen.
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.
ENZYME REGULATION: Inactivated by antipain, PMSF, TPCK, leupeptin, pepstatin, EDTA, and E-64 (trans-epoxysuccinylleucylamido(4-guanidino)butane).

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=12 µM for N-p-tosyl-L-arginine methyl ester (TAME);
	K_M=589 µM for NBz-Pro-Phe-Arg-pNA;
	K_M=1320 µM for NBz-Val-Gly-Arg-pNA;
	K_M=857 µM for NBz-DL-Arg-pNA;
	V_max=877.0 nmol/sec/mg enzyme for N-p-tosyl-L-arginine methyl ester (TAME);
	V_max=51.0 nmol/sec/mg enzyme for NBz-Pro-Phe-Arg-pNA;
	V_max=75.0 nmol/sec/mg enzyme for NBz-Val-Gly-Arg-pNA;
	V_max=39.3 nmol/sec/mg enzyme for NBz-DL-Arg-pNA;

SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Glycosylated.
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

3D structure databases

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0007596;	Biological process: blood coagulation (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

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

Phylogenomic databases

Other

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

Keywords

Blood coagulation; Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Toxin.

Features

Feature table viewer

Sequence information

Length: 30 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 3171 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: FA1B2609921853DB [This is a checksum on the sequence]

        10         20         30 
VIGGDECNIN EHRFLVALYD GLSGTFLCGG

	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