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P18965 (VSPG_DABSI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Factor V activator RVV-V gamma

EC=3.4.21.95
Alternative name(s):
Russel's viper venom FV activator gamma
Short name=RVV-V gamma
Snake venom serine protease
Short name=SVSP
OrganismDaboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Taxonomic identifier343250 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeViperinaeDaboia

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma. Ref.1

Catalytic activity

Fully activates human clotting factor V by a single cleavage at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

There are three isoproteins of RVV-V, designated RVV-V alpha, V-beta, and V-gamma.

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Factor V activator RVV-V gamma
PRO_0000088739

Regions

Domain1 – 227227Peptidase S1

Sites

Active site431Charge relay system Ref.3
Active site881Charge relay system Ref.3
Active site1821Charge relay system Ref.3

Amino acid modifications

Glycosylation2291N-linked (GlcNAc...) Ref.1
Disulfide bond7 ↔ 141 Ref.3
Disulfide bond28 ↔ 44 Ref.3
Disulfide bond76 ↔ 234 Ref.3
Disulfide bond120 ↔ 188 Ref.3
Disulfide bond152 ↔ 167 Ref.3
Disulfide bond178 ↔ 203 Ref.3

Secondary structure

........................................ 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18965 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: ED7C01F17DB8F7C5

FASTA23626,167
        10         20         30         40         50         60 
VVGGDECNIN EHPFLVALYT SASSTIHCAG ALINREWVLT AAHCDRRNIR IKLGMHSKNI 

        70         80         90        100        110        120 
RNEDEQIRVP RGKYFCLNTK FPNGLDKDIM LIRLRRPVTY STHIAPVSLP SRSRGVGSRC 

       130        140        150        160        170        180 
RIMGWGKIST TEDTYPDVPH CTNIFIVKHK WCEPLYPWVP ADSRTLCAGI LKGGRDTCHG 

       190        200        210        220        230 
DSGGPLICNG EMHGIVAGGS EPCGQHLKPA VYTKVFDYNN WIQSIIAGNR TVTCPP 

« Hide

References

[1]"The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences."
Tokunaga F., Nagasawa K., Tamura S., Miyata T., Iwanaga S., Kisiel W.
J. Biol. Chem. 263:17471-17481(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, GLYCOSYLATION AT ASN-229.
Tissue: Venom.
[2]"Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom."
Nakayama D., Ben Ammar Y., Takeda S.
Acta Crystallogr. F 65:1306-1308(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[3]"Structural basis of coagulation factor V recognition for cleavage by RVV-V."
Nakayama D., Ben Ammar Y., Miyata T., Takeda S.
FEBS Lett. 585:3020-3025(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), ACTIVE SITE, DISULFIDE BONDS.

Cross-references

Sequence databases

PIRB32121.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S9AX-ray1.90A1-236[»]
3S9BX-ray1.90A1-236[»]
3S9CX-ray1.80A1-236[»]
3SBKX-ray2.55A1-236[»]
ProteinModelPortalP18965.
SMRP18965. Positions 1-236.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18965.

Entry information

Entry nameVSPG_DABSI
AccessionPrimary (citable) accession number: P18965
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families