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

Ena/VASP-like protein

Gene

Evl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

ReactomeiR-RNO-376176. Signaling by ROBO receptors.
R-RNO-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Ena/VASP-like protein
Alternative name(s):
Ena/vasodilator-stimulated phosphoprotein-like
Gene namesi
Name:EvlImported
Synonyms:Rnb6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621150. Evl.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000871061 – 420Ena/VASP-like proteinAdd BLAST420

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei136PhosphoserineCombined sources1
Modified residuei250PhosphoserineBy similarity1
Modified residuei263PhosphoserineCombined sources1
Modified residuei308PhosphoserineCombined sources1
Modified residuei310PhosphoserineBy similarity1
Modified residuei333PhosphoserineBy similarity1
Modified residuei335PhosphoserineCombined sources1
Modified residuei345PhosphoserineBy similarity1
Modified residuei353PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei373PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO08719.
PRIDEiO08719.

PTM databases

CarbonylDBiO08719.
iPTMnetiO08719.
PhosphoSitePlusiO08719.

Expressioni

Gene expression databases

BgeeiENSRNOG00000014476.

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 Listeria monocytogenes actA (By similarity). Binds, via the EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1. Interacts with ZDHHC17 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiO08719. 2 interactors.
MINTiO08719.
STRINGi10116.ENSRNOP00000019584.

Structurei

3D structure databases

ProteinModelPortaliO08719.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 118WH1PROSITE-ProRule annotationAdd BLAST118

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni226 – 417EVH2Add BLAST192
Regioni226 – 246EVH2 block AAdd BLAST21
Regioni269 – 286EVH2 block BAdd BLAST18
Regioni346 – 366Required for interaction with ZDHHC17By similarityAdd BLAST21
Regioni383 – 417EVH2 block CAdd BLAST35

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili138 – 164Sequence analysisAdd BLAST27
Coiled coili386 – 412Sequence analysisAdd BLAST27

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi235 – 238KLKR4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi166 – 210Pro-richAdd BLAST45
Compositional biasi265 – 270Poly-Gly6

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

Keywords - Domaini

Coiled coil, SH3-binding

Phylogenomic databases

eggNOGiENOG410KD2J. Eukaryota.
ENOG410YM7V. LUCA.
GeneTreeiENSGT00730000110272.
HOGENOMiHOG000013015.
HOVERGENiHBG006655.
InParanoidiO08719.
OMAiSTQRQVQ.
PhylomeDBiO08719.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiView protein in InterPro
IPR034319. ENA/VASP-like_protein.
IPR011993. PH-like_dom_sf.
IPR017354. VASP/EVL.
IPR038023. VASP_sf.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
PANTHERiPTHR11202:SF4. PTHR11202:SF4. 1 hit.
PfamiView protein in Pfam
PF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiView protein in SMART
SM00461. WH1. 1 hit.
SUPFAMiSSF118370. SSF118370. 1 hit.
PROSITEiView protein in PROSITE
PS50229. WH1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O08719-1) [UniParc]FASTAAdd to basket

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
MFAFEEFSEQ SICQARASVM VYDDTSKKWV PIKPGQQGFS RINIYHNTAS
60 70 80 90 100
NTFRVVGVKL QDQQVVINYS IVKGLKYNQA TPTFHQWRDA RQVYGLNFAS
110 120 130 140 150
KEEATTFSNA MLFALNIMNS QEGGPSTQRQ VQNGPSPEEM DIQRRQVMEQ
160 170 180 190 200
QHRQESLERR ISATGPILPP GHPSSAASAT FSCSGPPPPP PPPVPPPPTG
210 220 230 240 250
STPPPPPPLP AGGAQGTNHD ESSASGLAAA LAGAKLRRVQ RPEDASGGSS
260 270 280 290 300
PSGTSKSDAN RASSGGGGGG LMEEMNKLLA KRRKAASQTD KPADRKEDEN
310 320 330 340 350
QTEDPSTSPS PGSRATSQPP NSSEAGRKPW ERSNSVEKPV SSLLSRTPSV
360 370 380 390 400
AKSPEAKSPL QSQPHSRVKP AGSVNDVGLD ALDLDRMKQE ILEEVVRELH
410 420
KVKEEIIDAI RQELSGISTT
Length:420
Mass (Da):45,152
Last modified:November 22, 2017 - v2
Checksum:iFEEE5E87F4784989
GO
Isoform 2 (identifier: O08719-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MFAFEEF → M
     344-365: LSRTPSVAKSPEAKSPLQSQPH → L

Show »
Length:393
Mass (Da):42,167
Checksum:iF99379994A917272
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti102E → G in AAC53322 (PubMed:9268706).1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0592201 – 7MFAFEEF → M in isoform 2. 7
Alternative sequenceiVSP_059221344 – 365LSRTP…QSQPH → L in isoform 2. Add BLAST22

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70211 mRNA. Translation: AAC53322.1.
AABR07065505 Genomic DNA. No translation available.
PIRiJC5614.
RefSeqiNP_077061.1. NM_024147.1.
XP_008763073.1. XM_008764851.2. [O08719-1]
XP_008763074.1. XM_008764852.2. [O08719-1]
UniGeneiRn.28912.

Genome annotation databases

EnsembliENSRNOT00000080230; ENSRNOP00000072070; ENSRNOG00000014476. [O08719-1]
GeneIDi79115.
KEGGirno:79115.
UCSCiRGD:621150. rat. [O08719-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiEVL_RAT
AccessioniPrimary (citable) accession number: O08719
Secondary accession number(s): A0A0G2K217
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 22, 2017
Last modified: March 28, 2018
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome