PROTEIN SEQUENCE.
TISSUE=Venom;
DOI=10.1016/0014-5793(92)80559-Y; PubMed=1544412 [NCBI, ExPASy, EBI, Israel, Japan]
Burkhart W., Simth G.F.H., Su J.-L., Parikh I., Levine H. III;
"Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Akistrodon rhodostoma.";
FEBS Lett. 297:297-301(1992).

Comments

FUNCTION: Thrombin-like snake venom serine protease. Cleaves fibrinopeptides AM, AO, and AY; the aberrant fibrinogen is then incapable of being cross-linked, forming easily dispersible clots.
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.
PHARMACEUTICAL: Used for the treatment of acute ischemic stroke. Until 2002 was available under the name Arvin (Knoll). Is actually available under the name Viprinex (Abbott).
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

S20407; S20407.

3D structure databases

HSSP

Q91516; 1BQY. [HSSP ENTRY / PDB]

ModBase

P26324.

Protein family/group databases

MEROPS

S01.178; -.

PTM databases

GlycoSuiteDB

P26324; -.

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 InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
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; FALSE_NEG.
PS00135; TRYPSIN_SER; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

P26324; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 234`	`234`	`Ancrod.`	`PRO_0000088730`
`DOMAIN`	`1 227`	`227`	`Peptidase S1.`
`ACT_SITE`	`43 43`		`Charge relay system (By similarity).`
`ACT_SITE`	`88 88`		`Charge relay system (By similarity).`
`ACT_SITE`	`182 182`		`Charge relay system (By similarity).`
`CARBOHYD`	`23 23`		`N-linked (GlcNAc...).`
`CARBOHYD`	`79 79`		`N-linked (GlcNAc...).`
`CARBOHYD`	`99 99`		`N-linked (GlcNAc...).`
`CARBOHYD`	`148 148`		`N-linked (GlcNAc...).`
`CARBOHYD`	`229 229`		`N-linked (GlcNAc...).`
`DISULFID`	`7 141`		`By similarity.`
`DISULFID`	`28 44`		`By similarity.`
`DISULFID`	`78 232`		`By similarity.`
`DISULFID`	`120 188`		`By similarity.`
`DISULFID`	`152 167`		`By similarity.`
`DISULFID`	`178 203`		`By similarity.`

Sequence information

Length: 234 AA [This is the length of the unprocessed precursor]

Molecular weight: 26570 Da [This is the MW of the unprocessed precursor]

CRC64: 3C55F0276B65E5CF [This is a checksum on the sequence]

        10         20         30         40         50         60 
VIGGDECNIN EHRFLVAVYE GTNWTFICGG VLIHPEWVIT AEHCARRRMN LVFGMHRKSE 

        70         80         90        100        110        120 
KFDDEQERYP KKRYFIRCNK TRTSWDEDIM LIRLNKPVNN SEHIAPLSLP SNPPIVGSDC 

       130        140        150        160        170        180 
RVMGWGSINR RIDVLSDEPR CANINLHNFT MCHGLFRKMP KKGRVLCAGD LRGRRDSCNS 

       190        200        210        220        230 
DSGGPLICNE ELHGIVARGP NPCAQPNKPA LYTSIYDYRD WVNNVIAGNA TCSP

P26324 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