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P70429 (EVL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ena/VASP-like protein
Alternative name(s):
Ena/vasodilator-stimulated phosphoprotein-like
Gene names
Name:Evl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.3

Subunit structure

Homotetramer By similarity. Binds to the SH3 domains of ABL1, LYN and SRC. Also binds to profilin, with preference for isoform IIaof PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A. Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich domain of ZYX By similarity. Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA. Ref.2 Ref.3 Ref.5 Ref.6

Subcellular location

Cytoplasmcytoskeleton. Cell projectionlamellipodium. Note: Targeted to the leading edge of lamellipodia and the dital 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. Ref.2

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. Ref.2 Ref.4

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). Ref.4

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.

Post-translational modification

Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC. Ref.2

Miscellaneous

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

Sequence similarities

Belongs to the Ena/VASP family.

Contains 1 WH1 domain.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainSH3-binding
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament-based movement

Non-traceable author statement Ref.2. Source: UniProtKB

actin nucleation

Non-traceable author statement Ref.2. Source: UniProtKB

actin polymerization or depolymerization

Inferred from direct assay Ref.2. Source: UniProtKB

axon guidance

Non-traceable author statement Ref.2. Source: UniProtKB

barbed-end actin filament capping

Non-traceable author statement Ref.2. Source: UniProtKB

platelet activation

Non-traceable author statement Ref.2. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from direct assay PubMed 23153535. Source: UniProt

protein homotetramerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from direct assay Ref.2. Source: UniProtKB

lamellipodium

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionSH3 domain binding

Inferred from direct assay Ref.2. Source: UniProtKB

profilin binding

Inferred from direct assay Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P70429-1)

Also known as: EVL-I;

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.
Isoform 1 (identifier: P70429-2)

The sequence of this isoform differs from the canonical sequence as follows:
     339-359: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Ena/VASP-like protein
PRO_0000087105

Regions

Domain1 – 112112WH1
Region220 – 411192EVH2
Region220 – 24021EVH2 block A
Region263 – 28018EVH2 block B
Region377 – 41135EVH2 block C
Motif229 – 2324KLKR
Compositional bias160 – 20445Pro-rich

Amino acid modifications

Modified residue2441Phosphoserine By similarity
Modified residue3021Phosphoserine By similarity
Modified residue3041Phosphoserine By similarity
Modified residue3271Phosphoserine By similarity
Modified residue3291Phosphoserine By similarity
Modified residue3391Phosphoserine By similarity
Modified residue3471Phosphoserine By similarity
Modified residue3521Phosphoserine By similarity
Modified residue3671Phosphoserine Ref.7

Natural variations

Alternative sequence339 – 35921Missing in isoform 1.
VSP_004045

Secondary structure

..................... 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (EVL-I) [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: 146A018BCD6CA370

FASTA41444,337
        10         20         30         40         50         60 
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASSTFRVV GVKLQDQQVV 

        70         80         90        100        110        120 
INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQEGGPS 

       130        140        150        160        170        180 
TQRQVQNGPS PEEMDIQRRQ VMEQQHRQES LERRISATGP ILPPGHPSSA ASTTLSCSGP 

       190        200        210        220        230        240 
PPPPPPPVPP PPTGSTPPPP PPLPAGGAQG TNHDESSASG LAAALAGAKL RRVQRPEDAS 

       250        260        270        280        290        300 
GGSSPSGTSK SDANRASSGG GGGGLMEEMN KLLAKRRKAA SQTDKPADRK EDESQTEDPS 

       310        320        330        340        350        360 
TSPSPGTRAT SQPPNSSEAG RKPWERSNSV EKPVSSLLSR TPSVAKSPEA KSPLQSQPHS 

       370        380        390        400        410 
RVKPAGSVND VGLDALDLDR MKQEILEEVV RELHKVKEEI IDAIRQELSG ISTT 

« Hide

Isoform 1 [UniParc].

Checksum: BBD63FB013ADBE00
Show »

FASTA39342,123

References

« Hide 'large scale' references
[1]"Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics."
Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.
Cell 87:227-239(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains."
Lambrechts A., Kwiatkowski A.V., Lanier L.M., Bear J.E., Vandekerckhove J., Ampe C., Gertler F.B.
J. Biol. Chem. 275:36143-36151(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PFN2; LYN; APBB1; ABL1 AND SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION BY PKA.
Strain: C57BL/6J.
[3]"Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes."
Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L., Jockusch B.M., Wehland J., Gertler F.B., Carlier M.-F.
J. Cell Biol. 144:1245-1258(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN L.MONOCYTOGENES MOBILITY, MISCELLANEOUS, INTERACTION WITH L.MONOCYTOGENES ACTA.
[4]"Mena is required for neurulation and commissure formation."
Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M., Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B.
Neuron 22:313-325(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[5]"The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like protein (EVL) via a novel carboxyl-terminal zyxin-like domain."
Klostermann A., Lutz B., Gertler F., Behl C.
J. Biol. Chem. 275:39647-39653(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEMA6A.
[6]"Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton."
Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.
J. Biol. Chem. 278:49031-49043(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNMBP.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function."
Fedorov A.A., Fedorov E., Gertler F., Almo S.C.
Nat. Struct. Biol. 6:661-665(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-130 IN COMPLEX WITH A SYNTHETIC PRO-RICH PEPTIDE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72519 mRNA. Translation: AAC52862.1.
AF279662 mRNA. Translation: AAG23653.1.
CCDSCCDS26161.1. [P70429-2]
CCDS49167.1. [P70429-1]
RefSeqNP_001156866.1. NM_001163394.1. [P70429-1]
NP_031991.3. NM_007965.3. [P70429-2]
UniGeneMm.238841.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QC6X-ray2.60A/B1-130[»]
ProteinModelPortalP70429.
SMRP70429. Positions 1-113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199547. 1 interaction.
MINTMINT-142769.

PTM databases

PhosphoSiteP70429.

Proteomic databases

MaxQBP70429.
PaxDbP70429.
PRIDEP70429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021689; ENSMUSP00000021689; ENSMUSG00000021262. [P70429-1]
ENSMUST00000077735; ENSMUSP00000076916; ENSMUSG00000021262. [P70429-2]
GeneID14026.
KEGGmmu:14026.
UCSCuc007ozv.1. mouse. [P70429-2]
uc007ozw.1. mouse. [P70429-1]

Organism-specific databases

CTD51466.
MGIMGI:1194884. Evl.

Phylogenomic databases

eggNOGNOG265043.
GeneTreeENSGT00730000110272.
HOGENOMHOG000013015.
HOVERGENHBG006655.
InParanoidP70429.
OMAQHRQESL.
OrthoDBEOG72JWGQ.
PhylomeDBP70429.
TreeFamTF321411.

Gene expression databases

ArrayExpressP70429.
BgeeP70429.
CleanExMM_EVL.
GenevestigatorP70429.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTSM00461. WH1. 1 hit.
[Graphical view]
PROSITEPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP70429.
NextBio284948.
PROP70429.
SOURCESearch...

Entry information

Entry nameEVL_MOUSE
AccessionPrimary (citable) accession number: P70429
Secondary accession number(s): Q9ERU8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot