Reviewed, UniProtKB/Swiss-Prot P47797 (VSP2_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	258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Sequence similarities	Belongs to the peptidase S1 family. Snake venom subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease Toxin
PTM	Disulfide bond Glycoprotein Zymogen
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
	Signal peptide	1 – 18	18	By similarity
	Propeptide	19 – 24	6	By similarity		PRO_0000028377
	Chain	25 – 258	234	Ancrod		PRO_0000028378
Regions
	Domain	25 – 251	227	Peptidase S1
Sites
	Active site	67	1	Charge relay system By similarity
	Active site	112	1	Charge relay system By similarity
	Active site	206	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	123	1	N-linked (GlcNAc...) Potential
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Glycosylation	253	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 165		By similarity
	Disulfide bond	52 ↔ 68		By similarity
	Disulfide bond	102 ↔ 256		By similarity
	Disulfide bond	144 ↔ 212		By similarity
	Disulfide bond	176 ↔ 191		By similarity
	Disulfide bond	202 ↔ 227		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47797-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 9181C7D1F2D689F4	FASTA	258	29,145
	10 20 30 40 50 60 MVLIRVLANL VILQLSYAQK SSELVIGGDE CNINEHRFLV ALYDSTTRNF LCGGVLIHPE 70 80 90 100 110 120 WVITAKHCNK KSMVLYLGKH KQSVKFDDEQ ERFPKEKHFI RCNKPRTRWG EDIMLIRLNK 130 140 150 160 170 180 PVNNSEHIAP LSLPSNPPIV GSVCRVMGWG SINKYIDVLP DEPRCANINL YNYTVCRGVF 190 200 210 220 230 240 PRIPKKSKIL CAGDLQGRLD SCHCDSGGPL ICSEEFHGIV YRGPNPCAQP DKPALYTNIF 250 DHLHWILSIM AGNATCYP

References

[1]

"Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma." Au L.-C., Lin S.-B., Chou J.-S., Teh G.-W., Chang K.-J., Shih C.-M. Biochem. J. 294:387-390(1993) [PubMed: 8373353] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L07308 mRNA. Translation: AAA49195.1.
PIR	S36783.
3D structure databases
HSSP	HSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBase	Search...
Protein family/group databases
MEROPS	S01.178.
Phylogenomic databases
HOVERGEN	P47797.
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

VSP2_AGKRH

Accession

Primary (citable) accession number: P47797

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)