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P70429

- EVL_MOUSE

UniProt

P70429 - EVL_MOUSE

Protein

Ena/VASP-like protein

Gene

Evl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (15 Nov 2002)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. 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. platelet activation Source: UniProtKB
    7. positive regulation of actin filament polymerization Source: UniProt
    8. protein homotetramerization Source: InterPro

    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-SubCell
    3. focal adhesion Source: UniProtKB
    4. lamellipodium Source: UniProtKB

    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 – 3671Phosphoserine2 Publications

    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

    ArrayExpressiP70429.
    BgeeiP70429.
    CleanExiMM_EVL.
    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 – 1714
    Turni18 – 214
    Beta strandi22 – 254
    Beta strandi34 – 418
    Turni42 – 454
    Beta strandi46 – 527
    Turni54 – 563
    Beta strandi59 – 646
    Beta strandi70 – 756
    Beta strandi78 – 825
    Beta strandi87 – 937
    Helixi95 – 11117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASSTFRVV    50
    GVKLQDQQVV INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT 100
    FSNAMLFALN IMNSQEGGPS TQRQVQNGPS PEEMDIQRRQ VMEQQHRQES 150
    LERRISATGP ILPPGHPSSA ASTTLSCSGP PPPPPPPVPP PPTGSTPPPP 200
    PPLPAGGAQG TNHDESSASG LAAALAGAKL RRVQRPEDAS GGSSPSGTSK 250
    SDANRASSGG GGGGLMEEMN KLLAKRRKAA SQTDKPADRK EDESQTEDPS 300
    TSPSPGTRAT SQPPNSSEAG RKPWERSNSV EKPVSSLLSR TPSVAKSPEA 350
    KSPLQSQPHS RVKPAGSVND VGLDALDLDR MKQEILEEVV RELHKVKEEI 400
    IDAIRQELSG ISTT 414
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    ArrayExpressi P70429.
    Bgeei P70429.
    CleanExi MM_EVL.
    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

    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: October 1, 2014
    This is version 121 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