PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
TISSUE=Venom;
DOI=10.1016/0041-0101(92)90515-7; PubMed=1485336 [NCBI, ExPASy, EBI, Israel, Japan]
Laraba-Djebari F., Martin-Eauclaire M.-F., Marchot P.;
"A fibrinogen-clotting serine proteinase from Cerastes cerastes (horned viper) venom with arginine-esterase and amidase activities. Purification, characterization and kinetic parameter determination.";
Toxicon 30:1399-1410(1992).

Comments

FUNCTION: Thrombin-like snake venom serine protease. Displays proteolytic activity toward the natural substrate casein as well as clotting activity on fibrinogen. Shows both arginine-ester hydrolase and amidase activities on synthetic substrates.
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: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
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

PIR

A44181; A44181.

3D structure databases

ModBase

Q9PS28.

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

InterPro

IPR001254; Peptidase_S1_S6.
Graphical view of domain structure.

PROSITE

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

ProtoNet

Q9PS28.

Phylogenomic databases

HOVERGEN

Q9PS28; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >33`	`>33`	`Proteinase RP34.`	`PRO_0000294991`
`DOMAIN`	`1 >33`	`>33`	`Peptidase S1.`
`NON_TER`	`33 33`

Sequence information

Length: 33 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 3786 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 123F8467054D32E3 [This is a checksum on the sequence]

        10         20         30 
VIGGDEXDIN EHRSLALMYX SWSHRFIXXG XLI

Q9PS28 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