Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vasodilator-stimulated phosphoprotein

Gene

VASP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-BTA-376176. Signaling by Robo receptor.
R-BTA-446353. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Vasodilator-stimulated phosphoprotein
Short name:
VASP
Gene namesi
Name:VASP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 383382Vasodilator-stimulated phosphoproteinPRO_0000227759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei39 – 391PhosphotyrosineBy similarity
Modified residuei160 – 1601Phosphoserine; by PKA, PKG/PRKG1, PKC and ROCK1By similarity
Modified residuei242 – 2421Phosphoserine; by PKA and PKG/PRKG1By similarity
Modified residuei281 – 2811Phosphothreonine; by PKA, PKG/PRKG1 and AMPKBy similarity
Modified residuei286 – 2861N6-acetyllysineBy similarity
Modified residuei319 – 3191PhosphothreonineBy similarity
Modified residuei325 – 3251Phosphoserine; by AMPKBy similarity
Modified residuei326 – 3261PhosphoserineBy similarity
Modified residuei328 – 3281PhosphoserineBy similarity

Post-translational modificationi

Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-160, the preferred site for PKG/PRKG1, Ser-242. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-160 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-281 requires prior phosphorylation on Ser-160 and Ser-242. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-281 by AMPK does not require prior phosphorylation at Ser-160 or Ser-242. Phosphorylation at Ser-160 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-325 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-160, while nitric oxide (NO) promotes phosphorylation at Ser-160, but also at Ser-242 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ2TA49.
PRIDEiQ2TA49.

Interactioni

Subunit structurei

Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of DNMBP. Interacts weakly with MEFV (By similarity).By similarity

Protein-protein interaction databases

IntActiQ2TA49. 1 interaction.
STRINGi9913.ENSBTAP00000026119.

Structurei

3D structure databases

ProteinModelPortaliQ2TA49.
SMRiQ2TA49. Positions 1-115, 206-242, 341-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 113112WH1PROSITE-ProRule annotationAdd
BLAST
Repeati347 – 361151Add
BLAST
Repeati362 – 376152Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni228 – 380153EVH2Add
BLAST
Regioni228 – 24821EVH2 block AAdd
BLAST
Regioni262 – 28120EVH2 block BAdd
BLAST
Regioni346 – 38035EVH2 block CAdd
BLAST
Regioni347 – 361152 X 15 AA tandem repeats of L-[EQ]-[KR] [MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-EAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili343 – 37634Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi237 – 2404KLKR

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi118 – 219102Pro-richAdd
BLAST
Compositional biasi325 – 3284Poly-Ser

Domaini

The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.
The WH1 domain mediates interaction with XIRP1.By similarity

Sequence similaritiesi

Belongs to the Ena/VASP family.Curated
Contains 1 WH1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3-binding

Phylogenomic databases

eggNOGiKOG4590. Eukaryota.
ENOG41101TS. LUCA.
GeneTreeiENSGT00730000110272.
HOGENOMiHOG000013015.
HOVERGENiHBG006655.
InParanoidiQ2TA49.
KOiK06274.
OMAiIRGVKYN.
OrthoDBiEOG72JWGQ.
TreeFamiTF321411.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
[Graphical view]
PANTHERiPTHR11202:SF12. PTHR11202:SF12. 1 hit.
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q2TA49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETVVCTSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV
60 70 80 90 100
GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAT
110 120 130 140 150
QFANGMASAL EALEGGGPLP PPPPTAPPTW SAQNGPSPEE MEQQKRQQQS
160 170 180 190 200
ELMERERRAS NAGGPPAASA GAPPPPPGPP PPPGPPPPPG LSSSGVSAAT
210 220 230 240 250
QGAGGGPPPA PPLPTAQGPS GGGTGAPSLA SAIAGAKLRK VSKQEEASAG
260 270 280 290 300
PVAPKAESSR STGGGLMEEM NAMLARRRKA TQVGEKPAKD ESANQEESDA
310 320 330 340 350
RVPAHSESVR RPWEKNSTTL PRMKSSSSVT TSEAHPATPS SSDESDLERV
360 370 380
KQELLEEVRK ELQKVKEEII EAFVQELRKR GAP
Length:383
Mass (Da):40,463
Last modified:January 23, 2007 - v3
Checksum:i991EF24796BAACE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC111116 mRNA. Translation: AAI11117.1.
RefSeqiNP_001033199.1. NM_001038110.2.
UniGeneiBt.56013.

Genome annotation databases

EnsembliENSBTAT00000026119; ENSBTAP00000026119; ENSBTAG00000019604.
GeneIDi514902.
KEGGibta:514902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC111116 mRNA. Translation: AAI11117.1.
RefSeqiNP_001033199.1. NM_001038110.2.
UniGeneiBt.56013.

3D structure databases

ProteinModelPortaliQ2TA49.
SMRiQ2TA49. Positions 1-115, 206-242, 341-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ2TA49. 1 interaction.
STRINGi9913.ENSBTAP00000026119.

Proteomic databases

PaxDbiQ2TA49.
PRIDEiQ2TA49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000026119; ENSBTAP00000026119; ENSBTAG00000019604.
GeneIDi514902.
KEGGibta:514902.

Organism-specific databases

CTDi7408.

Phylogenomic databases

eggNOGiKOG4590. Eukaryota.
ENOG41101TS. LUCA.
GeneTreeiENSGT00730000110272.
HOGENOMiHOG000013015.
HOVERGENiHBG006655.
InParanoidiQ2TA49.
KOiK06274.
OMAiIRGVKYN.
OrthoDBiEOG72JWGQ.
TreeFamiTF321411.

Enzyme and pathway databases

ReactomeiR-BTA-376176. Signaling by Robo receptor.
R-BTA-446353. Cell-extracellular matrix interactions.

Miscellaneous databases

NextBioi20871563.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
[Graphical view]
PANTHERiPTHR11202:SF12. PTHR11202:SF12. 1 hit.
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiVASP_BOVIN
AccessioniPrimary (citable) accession number: Q2TA49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.