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Protein

Ena/VASP-like protein

Gene

Evl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • actin polymerization or depolymerization Source: UniProtKB
  • axon guidance Source: UniProtKB
  • central nervous system development Source: UniProtKB
  • movement of cell or subcellular component Source: UniProtKB
  • protein homotetramerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

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

Organism-specific databases

RGDi621150. Evl.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Cell projectionlamellipodium By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000871061 – 393Ena/VASP-like proteinAdd BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei130PhosphoserineCombined sources1
Modified residuei244PhosphoserineBy similarity1
Modified residuei257PhosphoserineCombined sources1
Modified residuei302PhosphoserineCombined sources1
Modified residuei304PhosphoserineBy similarity1
Modified residuei327PhosphoserineBy similarity1
Modified residuei329PhosphoserineCombined sources1
Modified residuei339PhosphoserineBy similarity1
Modified residuei346PhosphoserineCombined 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

iPTMnetiO08719.
PhosphoSitePlusiO08719.

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 and of Listeria monocytogenes actA (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiO08719. 2 interactors.
MINTiMINT-7211630.
STRINGi10116.ENSRNOP00000019584.

Structurei

3D structure databases

ProteinModelPortaliO08719.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 112WH1PROSITE-ProRule annotationAdd BLAST112

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni220 – 390EVH2Add BLAST171
Regioni220 – 240EVH2 block AAdd BLAST21
Regioni263 – 280EVH2 block BAdd BLAST18
Regioni356 – 390EVH2 block CAdd BLAST35

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili132 – 158Sequence analysisAdd BLAST27
Coiled coili359 – 385Sequence analysisAdd BLAST27

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi229 – 232KLKR4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi160 – 204Pro-richAdd BLAST45
Compositional biasi259 – 264Poly-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
Contains 1 WH1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3-binding

Phylogenomic databases

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

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
[Graphical view]
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08719-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASNTFRVV
60 70 80 90 100
GVKLQDQQVV INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKGEATT
110 120 130 140 150
FSNAMLFALN IMNSQEGGPS TQRQVQNGPS PEEMDIQRRQ VMEQQHRQES
160 170 180 190 200
LERRISATGP ILPPGHPSSA ASATFSCSGP PPPPPPPVPP PPTGSTPPPP
210 220 230 240 250
PPLPAGGAQG TNHDESSASG LAAALAGAKL RRVQRPEDAS GGSSPSGTSK
260 270 280 290 300
SDANRASSGG GGGGLMEEMN KLLAKRRKAA SQTDKPADRK EDENQTEDPS
310 320 330 340 350
TSPSPGSRAT SQPPNSSEAG RKPWERSNSV EKPVSSLLSR VKPAGSVNDV
360 370 380 390
GLDALDLDRM KQEILEEVVR ELHKVKEEII DAIRQELSGI STT
Length:393
Mass (Da):42,095
Last modified:July 1, 1997 - v1
Checksum:i6371D91362925D4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70211 mRNA. Translation: AAC53322.1.
PIRiJC5614.
RefSeqiNP_077061.1. NM_024147.1.
UniGeneiRn.28912.

Genome annotation databases

GeneIDi79115.
KEGGirno:79115.
UCSCiRGD:621150. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70211 mRNA. Translation: AAC53322.1.
PIRiJC5614.
RefSeqiNP_077061.1. NM_024147.1.
UniGeneiRn.28912.

3D structure databases

ProteinModelPortaliO08719.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08719. 2 interactors.
MINTiMINT-7211630.
STRINGi10116.ENSRNOP00000019584.

PTM databases

iPTMnetiO08719.
PhosphoSitePlusiO08719.

Proteomic databases

PaxDbiO08719.
PRIDEiO08719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi79115.
KEGGirno:79115.
UCSCiRGD:621150. rat.

Organism-specific databases

CTDi51466.
RGDi621150. Evl.

Phylogenomic databases

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

Miscellaneous databases

PROiO08719.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
[Graphical view]
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEVL_RAT
AccessioniPrimary (citable) accession number: O08719
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.