Reviewed, UniProtKB/Swiss-Prot P26324 (VSP1_AGKRH)

Names and origin

Protein names	Recommended name:     Ancrod     EC=3.4.21.74 Alternative name(s):     Venombin-A     Protein C activator     ACC-C
Organism	Agkistrodon rhodostoma (Malayan pit viper) (Calloselasma rhodostoma)
Taxonomic identifier	8717 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Calloselasma

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 use	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).
Sequence similarities	Belongs to the peptidase S1 family. Snake venom subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Hydrolase Protease Serine protease Toxin
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 234	234	Ancrod		PRO_0000088730
Regions
	Domain	1 – 227	227	Peptidase S1
Sites
	Active site	43	1	Charge relay system By similarity
	Active site	88	1	Charge relay system By similarity
	Active site	182	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	23	1	N-linked (GlcNAc...) Ref.1
	Glycosylation	79	1	N-linked (GlcNAc...) Ref.1
	Glycosylation	99	1	N-linked (GlcNAc...) Ref.1
	Glycosylation	148	1	N-linked (GlcNAc...) Ref.1
	Glycosylation	229	1	N-linked (GlcNAc...) Ref.1
	Disulfide bond	7 ↔ 141		By similarity
	Disulfide bond	28 ↔ 44		By similarity
	Disulfide bond	78 ↔ 232		By similarity
	Disulfide bond	120 ↔ 188		By similarity
	Disulfide bond	152 ↔ 167		By similarity
	Disulfide bond	178 ↔ 203		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26324-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 3C55F0276B65E5CF	FASTA	234	26,570
	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

References

[1]	"Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Akistrodon rhodostoma." Burkhart W., Simth G.F.H., Su J.-L., Parikh I., Levine H. III FEBS Lett. 297:297-301(1992) [PubMed: 1544412] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

Sequence databases
PIR	S20407.
3D structure databases
HSSP	HSSP built from PDB template 1BQY based on UniProtKB Q91516.
ModBase	Search...
Protein family/group databases
MEROPS	S01.178.
PTM databases
GlycoSuiteDB	P26324.
Phylogenomic databases
HOVERGEN	P26324.
Enzyme and pathway databases
BRENDA	3.4.21.74. 18614.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. False negative. PS00135. TRYPSIN_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

VSP1_AGKRH

Accession

Primary (citable) accession number: P26324

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)