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Protein

Factor V activator RVV-V gamma

Gene
N/A
Organism
Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671Charge relay system1 Publication
Active sitei112 – 1121Charge relay system1 Publication
Active sitei206 – 2061Charge relay system1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Protease, Serine protease, Toxin

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiDaboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Taxonomic identifieri343250 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 2461 PublicationPRO_0000432323
Chaini25 – 260236Factor V activator RVV-V gammaPRO_0000088739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 165PROSITE-ProRule annotation1 Publication
Disulfide bondi52 ↔ 68PROSITE-ProRule annotation1 Publication
Disulfide bondi100 ↔ 258PROSITE-ProRule annotation1 Publication
Disulfide bondi144 ↔ 212PROSITE-ProRule annotation1 Publication
Disulfide bondi176 ↔ 191PROSITE-ProRule annotation1 Publication
Disulfide bondi202 ↔ 227PROSITE-ProRule annotation1 Publication
Glycosylationi253 – 2531N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446Combined sources
Beta strandi47 – 5812Combined sources
Beta strandi61 – 644Combined sources
Helixi66 – 683Combined sources
Beta strandi73 – 786Combined sources
Beta strandi80 – 845Combined sources
Beta strandi90 – 923Combined sources
Beta strandi94 – 985Combined sources
Helixi109 – 1113Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi143 – 1508Combined sources
Beta strandi152 – 1554Combined sources
Beta strandi164 – 1718Combined sources
Helixi173 – 1753Combined sources
Turni176 – 1794Combined sources
Beta strandi187 – 1937Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi215 – 2228Combined sources
Beta strandi234 – 2385Combined sources
Helixi239 – 2424Combined sources
Helixi243 – 2519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S9AX-ray1.90A25-260[»]
3S9BX-ray1.90A25-260[»]
3S9CX-ray1.80A25-260[»]
3SBKX-ray2.55A25-260[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18965.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 251227Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLIKVLANL LVLQLSYAQK SSELVVGGDE CNINEHPFLV ALYTSASSTI
60 70 80 90 100
HCAGALINRE WVLTAAHCDR RNIRIKLGMH SKNIRNEDEQ IRVPRGKYFC
110 120 130 140 150
LNTKFPNGLD KDIMLIRLRR PVTYSTHIAP VSLPSRSRGV GSRCRIMGWG
160 170 180 190 200
KISTTEDTYP DVPHCTNIFI VKHKWCEPLY PWVPADSRTL CAGILKGGRD
210 220 230 240 250
TCHGDSGGPL ICNGEMHGIV AGGSEPCGQH LKPAVYTKVF DYNNWIQSII
260
AGNRTVTCPP
Length:260
Mass (Da):28,823
Last modified:March 4, 2015 - v2
Checksum:iCDFC23F40C0EC8F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031H → K in ADP88558 (PubMed:21640745).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ270463 mRNA. Translation: ADP88558.1.
PIRiB32121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ270463 mRNA. Translation: ADP88558.1.
PIRiB32121.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S9AX-ray1.90A25-260[»]
3S9BX-ray1.90A25-260[»]
3S9CX-ray1.80A25-260[»]
3SBKX-ray2.55A25-260[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG013304.

Miscellaneous databases

EvolutionaryTraceiP18965.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVSPG_DABSI
AccessioniPrimary (citable) accession number: P18965
Secondary accession number(s): E5L0E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 4, 2015
Last modified: September 7, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.