P70429 · EVL_MOUSE

  • Protein
    Ena/VASP-like protein
  • Gene
    Evl
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.

Miscellaneous

Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentfocal adhesion
Cellular Componentlamellipodium
Cellular Componentphagocytic vesicle
Cellular Componentstress fiber
Molecular Functionactin binding
Molecular Functionprofilin binding
Molecular FunctionSH3 domain binding
Biological Processactin filament-based movement
Biological Processactin nucleation
Biological Processactin polymerization or depolymerization
Biological Processaxon guidance
Biological Processbarbed-end actin filament capping
Biological Processcellular response to type II interferon
Biological Processplatelet activation
Biological Processpositive regulation of actin filament polymerization
Biological Processprotein homotetramerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ena/VASP-like protein
  • Alternative names
    • Ena/vasodilator-stimulated phosphoprotein-like

Gene names

    • Name
      Evl

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P70429
  • Secondary accessions
    • Q9ERU8

Proteomes

Organism-specific databases

Subcellular Location

Note: Targeted to the leading edge of lamellipodia and the distal tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000871051-414Ena/VASP-like protein
Modified residue130Phosphoserine
Modified residue244Phosphoserine
Modified residue257Phosphoserine
Modified residue302Phosphoserine
Modified residue304Phosphoserine
Modified residue327Phosphoserine
Modified residue329Phosphoserine
Modified residue339Phosphoserine
Modified residue347Phosphoserine
Modified residue352Phosphoserine
Modified residue367Phosphoserine

Post-translational modification

Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highest expression in thymus and spleen (at protein level). Low levels in placenta, ovary, testis, fat and lung (at protein level). Isoform 1 and isoform 2 are expressed in cortical neurons and glial cells.

Developmental stage

At an early stage, highly expressed in the branchial and pharyngeal arches, but not in the brain. Expression in the brain starts at 15 dpc (at protein level).

Gene expression databases

Interaction

Subunit

Homotetramer (By similarity).
Binds to the SH3 domains of ABL1, LYN and SRC (PubMed:10945997).
Also binds to profilin, with preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65 (PubMed:10945997).
Binds to SEMA6A (PubMed:10993894).
Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP (PubMed:14506234).
Interacts with RAPH1 (By similarity).
Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA (PubMed:10087267).
Binds, via the EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1. Interacts with ZDHHC17 (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias, motif.

TypeIDPosition(s)Description
Domain1-112WH1
Region157-369Disordered
Compositional bias177-206Pro residues
Region220-240EVH2 block A
Region220-411EVH2
Motif229-232KLKR
Compositional bias239-256Polar residues
Region263-280EVH2 block B
Compositional bias270-297Basic and acidic residues
Compositional bias298-363Polar residues
Region340-360Required for interaction with ZDHHC17
Region377-411EVH2 block C

Domain

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.

Sequence similarities

Belongs to the Ena/VASP family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P70429-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    2
  • Synonyms
    EVL-I
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    414
  • Mass (Da)
    44,337
  • Last updated
    2002-11-15 v2
  • Checksum
    146A018BCD6CA370
MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASSTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASTTLSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVNDVGLDALDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT

P70429-2

  • Name
    1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1Y7VNI5A0A1Y7VNI5_MOUSEEvl39
E9PVP4E9PVP4_MOUSEEvl401
A0A1Y7VJA2A0A1Y7VJA2_MOUSEEvl426
F8WJB9F8WJB9_MOUSEEvl399

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias177-206Pro residues
Compositional bias239-256Polar residues
Compositional bias270-297Basic and acidic residues
Compositional bias298-363Polar residues
Alternative sequenceVSP_004045339-359in isoform 1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U72519
EMBL· GenBank· DDBJ
AAC52862.1
EMBL· GenBank· DDBJ
mRNA
AF279662
EMBL· GenBank· DDBJ
AAG23653.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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