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P70429

- EVL_MOUSE

UniProt

P70429 - EVL_MOUSE

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Protein

Ena/VASP-like protein

Gene

Evl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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 and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.2 Publications

GO - Molecular functioni

  1. profilin binding Source: UniProtKB
  2. SH3 domain binding Source: UniProtKB

GO - Biological processi

  1. actin filament-based movement Source: UniProtKB
  2. actin nucleation Source: UniProtKB
  3. actin polymerization or depolymerization Source: UniProtKB
  4. axon guidance Source: UniProtKB
  5. barbed-end actin filament capping Source: UniProtKB
  6. negative regulation of epithelial cell migration Source: Ensembl
  7. negative regulation of ruffle assembly Source: Ensembl
  8. platelet activation Source: UniProtKB
  9. positive regulation of actin filament polymerization Source: UniProt
  10. positive regulation of stress fiber assembly Source: Ensembl
  11. protein homotetramerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_221567. Signaling by Robo receptor.
REACT_225768. Generation of second messenger molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Ena/VASP-like protein
Alternative name(s):
Ena/vasodilator-stimulated phosphoprotein-like
Gene namesi
Name:Evl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1194884. Evl.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cell projectionlamellipodium 1 Publication
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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. focal adhesion Source: UniProtKB
  4. lamellipodium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Ena/VASP-like proteinPRO_0000087105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei302 – 3021PhosphoserineBy similarity
Modified residuei304 – 3041PhosphoserineBy similarity
Modified residuei327 – 3271PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei339 – 3391PhosphoserineBy similarity
Modified residuei347 – 3471PhosphoserineBy similarity
Modified residuei352 – 3521PhosphoserineBy similarity
Modified residuei367 – 3671Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP70429.
PaxDbiP70429.
PRIDEiP70429.

PTM databases

PhosphoSiteiP70429.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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).1 Publication

Gene expression databases

BgeeiP70429.
CleanExiMM_EVL.
ExpressionAtlasiP70429. baseline and differential.
GenevestigatoriP70429.

Interactioni

Subunit structurei

Homotetramer (By similarity). Binds to the SH3 domains of ABL1, LYN and SRC. Also binds to profilin, with preference for isoform IIa of 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.By similarity5 Publications

Protein-protein interaction databases

BioGridi199547. 1 interaction.
IntActiP70429. 1 interaction.
MINTiMINT-142769.

Structurei

Secondary structure

1
414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1714Combined sources
Turni18 – 214Combined sources
Beta strandi22 – 254Combined sources
Beta strandi34 – 418Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 527Combined sources
Turni54 – 563Combined sources
Beta strandi59 – 646Combined sources
Beta strandi70 – 756Combined sources
Beta strandi78 – 825Combined sources
Beta strandi87 – 937Combined sources
Helixi95 – 11117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QC6X-ray2.60A/B1-130[»]
ProteinModelPortaliP70429.
SMRiP70429. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70429.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 112112WH1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni220 – 411192EVH2Add
BLAST
Regioni220 – 24021EVH2 block AAdd
BLAST
Regioni263 – 28018EVH2 block BAdd
BLAST
Regioni377 – 41135EVH2 block CAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi229 – 2324KLKR

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi160 – 20445Pro-richAdd
BLAST

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.

Sequence similaritiesi

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

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiNOG265043.
GeneTreeiENSGT00730000110272.
HOGENOMiHOG000013015.
HOVERGENiHBG006655.
InParanoidiP70429.
OMAiQHRQESL.
OrthoDBiEOG72JWGQ.
PhylomeDBiP70429.
TreeFamiTF321411.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: P70429-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASSTFRVV
60 70 80 90 100
GVKLQDQQVV INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT
110 120 130 140 150
FSNAMLFALN IMNSQEGGPS TQRQVQNGPS PEEMDIQRRQ VMEQQHRQES
160 170 180 190 200
LERRISATGP ILPPGHPSSA ASTTLSCSGP PPPPPPPVPP PPTGSTPPPP
210 220 230 240 250
PPLPAGGAQG TNHDESSASG LAAALAGAKL RRVQRPEDAS GGSSPSGTSK
260 270 280 290 300
SDANRASSGG GGGGLMEEMN KLLAKRRKAA SQTDKPADRK EDESQTEDPS
310 320 330 340 350
TSPSPGTRAT SQPPNSSEAG RKPWERSNSV EKPVSSLLSR TPSVAKSPEA
360 370 380 390 400
KSPLQSQPHS RVKPAGSVND VGLDALDLDR MKQEILEEVV RELHKVKEEI
410
IDAIRQELSG ISTT
Length:414
Mass (Da):44,337
Last modified:November 15, 2002 - v2
Checksum:i146A018BCD6CA370
GO
Isoform 1 (identifier: P70429-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:393
Mass (Da):42,123
Checksum:iBBD63FB013ADBE00
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei339 – 35921Missing in isoform 1. 1 PublicationVSP_004045Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72519 mRNA. Translation: AAC52862.1.
AF279662 mRNA. Translation: AAG23653.1.
CCDSiCCDS26161.1. [P70429-2]
CCDS49167.1. [P70429-1]
RefSeqiNP_001156866.1. NM_001163394.1. [P70429-1]
NP_031991.3. NM_007965.3. [P70429-2]
UniGeneiMm.238841.

Genome annotation databases

EnsembliENSMUST00000021689; ENSMUSP00000021689; ENSMUSG00000021262. [P70429-1]
ENSMUST00000077735; ENSMUSP00000076916; ENSMUSG00000021262. [P70429-2]
GeneIDi14026.
KEGGimmu:14026.
UCSCiuc007ozv.1. mouse. [P70429-2]
uc007ozw.1. mouse. [P70429-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72519 mRNA. Translation: AAC52862.1 .
AF279662 mRNA. Translation: AAG23653.1 .
CCDSi CCDS26161.1. [P70429-2 ]
CCDS49167.1. [P70429-1 ]
RefSeqi NP_001156866.1. NM_001163394.1. [P70429-1 ]
NP_031991.3. NM_007965.3. [P70429-2 ]
UniGenei Mm.238841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QC6 X-ray 2.60 A/B 1-130 [» ]
ProteinModelPortali P70429.
SMRi P70429. Positions 1-113.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199547. 1 interaction.
IntActi P70429. 1 interaction.
MINTi MINT-142769.

PTM databases

PhosphoSitei P70429.

Proteomic databases

MaxQBi P70429.
PaxDbi P70429.
PRIDEi P70429.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021689 ; ENSMUSP00000021689 ; ENSMUSG00000021262 . [P70429-1 ]
ENSMUST00000077735 ; ENSMUSP00000076916 ; ENSMUSG00000021262 . [P70429-2 ]
GeneIDi 14026.
KEGGi mmu:14026.
UCSCi uc007ozv.1. mouse. [P70429-2 ]
uc007ozw.1. mouse. [P70429-1 ]

Organism-specific databases

CTDi 51466.
MGIi MGI:1194884. Evl.

Phylogenomic databases

eggNOGi NOG265043.
GeneTreei ENSGT00730000110272.
HOGENOMi HOG000013015.
HOVERGENi HBG006655.
InParanoidi P70429.
OMAi QHRQESL.
OrthoDBi EOG72JWGQ.
PhylomeDBi P70429.
TreeFami TF321411.

Enzyme and pathway databases

Reactomei REACT_221567. Signaling by Robo receptor.
REACT_225768. Generation of second messenger molecules.

Miscellaneous databases

EvolutionaryTracei P70429.
NextBioi 284948.
PROi P70429.
SOURCEi Search...

Gene expression databases

Bgeei P70429.
CleanExi MM_EVL.
ExpressionAtlasi P70429. baseline and differential.
Genevestigatori P70429.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view ]
Pfami PF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view ]
PIRSFi PIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTi SM00461. WH1. 1 hit.
[Graphical view ]
PROSITEi PS50229. WH1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiEVL_MOUSE
AccessioniPrimary (citable) accession number: P70429
Secondary accession number(s): Q9ERU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: November 26, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3