Reviewed, UniProtKB/Swiss-Prot P81661 (VSPA_BOTJA)

Names and origin

Protein names	Recommended name:     Thrombin-like enzyme bothrombin     EC=3.4.21.74 Alternative name(s):     Reptilase
Organism	Bothrops jararaca (Jararaca)
Taxonomic identifier	8724 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length	232 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. Aggregates platelets in the presence of exogenous fibrinogen, possibly through interaction with glycoprotein 1b. Activates blood coagulation factor VIII.
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.
Enzyme regulation	Inhibited by diisopropyl fluorophosphate, but not by hirudin.
Subunit structure	Monomer.
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
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 – 232

232

Thrombin-like enzyme bothrombin

PRO_0000088731

Regions

Domain

1 – 223

223

Peptidase S1

Sites

Active site

41

1

Charge relay system By similarity

Active site

86

1

Charge relay system By similarity

Active site

178

1

Charge relay system By similarity

Amino acid modifications

Glycosylation

98

1

N-linked (GlcNAc...) Probable

Glycosylation

146

1

N-linked (GlcNAc...) Probable

Glycosylation

225

1

N-linked (GlcNAc...) Probable

Disulfide bond

7 ↔ 139

By similarity

Disulfide bond

26 ↔ 42

By similarity

Disulfide bond

74 ↔ 230

By similarity

Disulfide bond

118 ↔ 184

By similarity

Disulfide bond

150 ↔ 163

By similarity

Disulfide bond

174 ↔ 199

By similarity

Secondary structure

1

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232

Helix Strand Turn

Details...

Turn

9 – 11

3

Beta strand

16 – 19

4

Beta strand

21 – 23

3

Beta strand

27 – 38

12

Beta strand

48 – 52

5

Beta strand

56 – 58

3

Beta strand

64 – 66

3

Beta strand

68 – 71

4

Beta strand

79 – 81

3

Beta strand

88 – 94

7

Beta strand

99 – 101

3

Beta strand

117 – 122

6

Beta strand

126 – 129

4

Beta strand

138 – 144

7

Helix

147 – 153

7

Beta strand

155 – 157

3

Beta strand

167 – 172

6

Beta strand

181 – 184

4

Beta strand

187 – 192

6

Beta strand

196 – 201

6

Beta strand

208 – 210

3

Turn

211 – 214

4

Helix

215 – 222

8

Sequences

	Sequence		Length	Mass (Da)
	P81661-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: BFCD46A729D3E8AA	FASTA	232	25,584
	10 20 30 40 50 60 VIGGDECDIN EHPFLAFMYY SPQYFCGMTL INQEWVLTAA HCDKTYMRIY LGIHTRSVAN 70 80 90 100 110 120 DDEVIRYPKE KFICPNKKKN VITDKDIMLI RLNRPVKNST HIAPISLPSN PPSVGSVCRI 130 140 150 160 170 180 MGWGAITTSE DTYPDVPHCA NINLFNNTVC REAYNGLPAK TLCAGVLQGG IDTCGGDSGG 190 200 210 220 230 PLICNGQFQG ILSWGSDPCA EPRKPAFYTK VFDYLPWIQS IIAGNKTATC PP

References

[1]

"Purification and characterization of bothrombin, a fibrinogen-clotting serine protease from the venom of Bothrops jararaca." Nishida S., Fujimura Y., Miura S., Ozaki Y., Usami Y., Suzuki M., Titani K., Yoshida E., Sugimoto M., Yoshioka A., Fukui H. Biochemistry 33:1843-1849(1994) [PubMed: 8110787] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

Sequence databases

PIR

A54361.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CXM	model	-	A	1-232	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P81661.

Enzyme and pathway databases

BRENDA

3.4.21.74. 19086.

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. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

VSPA_BOTJA

Accession

Primary (citable) accession number: P81661

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)