Reviewed, UniProtKB/Swiss-Prot P09872 (VSP1_AGKCO)

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 contortrix contortrix (Southern copperhead)
Taxonomic identifier	8713 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Agkistrodon

Protein attributes

Sequence length	231 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. Activates protein C.
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 Potential.
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
Biological process	Blood coagulation
Cellular component	Secreted
Molecular function	Hydrolase Protease Serine protease Toxin
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW 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 – 231

231

Ancrod

PRO_0000088726

Regions

Domain

1 – 222

222

Peptidase S1

Sites

Active site

40

1

Charge relay system Ref.3

Active site

85

1

Charge relay system Ref.3

Active site

177

1

Charge relay system Ref.3

Amino acid modifications

Glycosylation

21

1

N-linked (GlcNAc...) Ref.3 Ref.1

Glycosylation

78

1

N-linked (GlcNAc...) Ref.3 Ref.1

Glycosylation

129

1

N-linked (GlcNAc...) Ref.3 Ref.1

Disulfide bond

7 ↔ 138

Ref.3

Disulfide bond

25 ↔ 41

Ref.3

Disulfide bond

73 ↔ 229

Ref.3

Disulfide bond

117 ↔ 183

Ref.3

Disulfide bond

149 ↔ 162

Ref.3

Disulfide bond

173 ↔ 198

Ref.3

Secondary structure

1

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231

Helix Strand Turn

Details...

Beta strand

15 – 20

6

Beta strand

23 – 31

9

Beta strand

34 – 37

4

Helix

39 – 41

3

Beta strand

47 – 51

5

Beta strand

63 – 65

3

Beta strand

67 – 72

6

Beta strand

78 – 80

3

Turn

81 – 84

4

Beta strand

87 – 93

7

Beta strand

116 – 123

8

Beta strand

125 – 129

5

Beta strand

137 – 144

8

Helix

146 – 152

7

Beta strand

158 – 164

7

Beta strand

180 – 183

4

Beta strand

186 – 194

9

Beta strand

205 – 209

5

Helix

210 – 213

4

Helix

214 – 222

9

Sequences

	Sequence		Length	Mass (Da)
	P09872-1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: DC3D7CBE601EC52B	FASTA	231	25,106
	10 20 30 40 50 60 VIGGDECNIN EHRFLALVYA NGSLCGGTLI NQEWVLTARH CDRGNMRIYL GMHNLKVLNK 70 80 90 100 110 120 DALRRFPKEK YFCLNTRNDT IWDKDIMLIR LNRPVRNSAH IAPLSLPSNP PSVGSVCRIM 130 140 150 160 170 180 GWGTITSPNA TLPDVPHCAN INILDYAVCQ AAYKGLAATT LCAGILEGGK DTCKGDSGGP 190 200 210 220 230 LICNGQFQGI LSVGGNPCAQ PRKPGIYTKV FDYTDWIQSI ISGNTDATCP P

References

[1]	"Primary structure of a protein C activator from Agkistrodon contortrix contortrix venom." McMullen B.A., Fujikawa K., Kisiel W. Biochemistry 28:674-679(1989) [PubMed: 2653426] [Abstract] Cited for: PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129. Tissue: Venom.
[2]	"Characterization of a protein C activator from Agkistrodon contortrix contortrix venom." Kisiel W., Kondo S., Smith K.J., McMullen B.A., Smith L.F. J. Biol. Chem. 262:12607-12613(1987) [PubMed: 3624272] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-63. Tissue: Venom.
[3]	"Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator." Murakami M.T., Arni R.K. J. Biol. Chem. 280:39309-39315(2005) [PubMed: 16162508] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129.

Cross-references

Sequence databases

PIR

A60468.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AIP	X-ray	1.65	A	1-231	[»]
2AIQ	X-ray	1.54	A	1-231	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S01.466.

Phylogenomic databases

HOVERGEN

P09872.

Enzyme and pathway databases

BRENDA

3.4.21.74. 19148.

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. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

VSP1_AGKCO

Accession

Primary (citable) accession number: P09872

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)