P70429 · EVL_MOUSE
- ProteinEna/VASP-like protein
- GeneEvl
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids414 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Miscellaneous
Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | focal adhesion | |
Cellular Component | lamellipodium | |
Cellular Component | phagocytic vesicle | |
Cellular Component | stress fiber | |
Molecular Function | actin binding | |
Molecular Function | profilin binding | |
Molecular Function | SH3 domain binding | |
Biological Process | actin filament-based movement | |
Biological Process | actin nucleation | |
Biological Process | actin polymerization or depolymerization | |
Biological Process | axon guidance | |
Biological Process | barbed-end actin filament capping | |
Biological Process | cellular response to type II interferon | |
Biological Process | platelet activation | |
Biological Process | positive regulation of actin filament polymerization | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEna/VASP-like protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP70429
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Targeted to the leading edge of lamellipodia and the distal 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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000087105 | 1-414 | Ena/VASP-like protein | |||
Sequence: MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASSTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASTTLSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVNDVGLDALDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT | ||||||
Modified residue | 130 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 244 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 257 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 302 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 304 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 327 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 329 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 339 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 347 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 352 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 367 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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.
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).
Gene expression databases
Interaction
Subunit
Homotetramer (By similarity).
Binds to the SH3 domains of ABL1, LYN and SRC (PubMed:10945997).
Also binds to profilin, with preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65 (PubMed:10945997).
Binds to SEMA6A (PubMed:10993894).
Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP (PubMed:14506234).
Interacts with RAPH1 (By similarity).
Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA (PubMed:10087267).
Binds, via the EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1. Interacts with ZDHHC17 (By similarity).
Binds to the SH3 domains of ABL1, LYN and SRC (PubMed:10945997).
Also binds to profilin, with preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65 (PubMed:10945997).
Binds to SEMA6A (PubMed:10993894).
Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP (PubMed:14506234).
Interacts with RAPH1 (By similarity).
Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA (PubMed:10087267).
Binds, via the EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1. Interacts with ZDHHC17 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-112 | WH1 | ||||
Sequence: MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASSTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIM | ||||||
Region | 157-369 | Disordered | ||||
Sequence: ATGPILPPGHPSSAASTTLSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVN | ||||||
Compositional bias | 177-206 | Pro residues | ||||
Sequence: CSGPPPPPPPPVPPPPTGSTPPPPPPLPAG | ||||||
Region | 220-240 | EVH2 block A | ||||
Sequence: GLAAALAGAKLRRVQRPEDAS | ||||||
Region | 220-411 | EVH2 | ||||
Sequence: GLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVNDVGLDALDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGI | ||||||
Motif | 229-232 | KLKR | ||||
Sequence: KLRR | ||||||
Compositional bias | 239-256 | Polar residues | ||||
Sequence: ASGGSSPSGTSKSDANRA | ||||||
Region | 263-280 | EVH2 block B | ||||
Sequence: GGLMEEMNKLLAKRRKAA | ||||||
Compositional bias | 270-297 | Basic and acidic residues | ||||
Sequence: NKLLAKRRKAASQTDKPADRKEDESQTE | ||||||
Compositional bias | 298-363 | Polar residues | ||||
Sequence: DPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVK | ||||||
Region | 340-360 | Required for interaction with ZDHHC17 | ||||
Sequence: RTPSVAKSPEAKSPLQSQPHS | ||||||
Region | 377-411 | EVH2 block C | ||||
Sequence: DLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGI |
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.
Sequence similarities
Belongs to the Ena/VASP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P70429-1
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.
- Name2
- SynonymsEVL-I
- Length414
- Mass (Da)44,337
- Last updated2002-11-15 v2
- Checksum146A018BCD6CA370
P70429-2
- Name1
- Differences from canonical
- 339-359: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1Y7VNI5 | A0A1Y7VNI5_MOUSE | Evl | 39 | ||
E9PVP4 | E9PVP4_MOUSE | Evl | 401 | ||
A0A1Y7VJA2 | A0A1Y7VJA2_MOUSE | Evl | 426 | ||
F8WJB9 | F8WJB9_MOUSE | Evl | 399 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 177-206 | Pro residues | ||||
Sequence: CSGPPPPPPPPVPPPPTGSTPPPPPPLPAG | ||||||
Compositional bias | 239-256 | Polar residues | ||||
Sequence: ASGGSSPSGTSKSDANRA | ||||||
Compositional bias | 270-297 | Basic and acidic residues | ||||
Sequence: NKLLAKRRKAASQTDKPADRKEDESQTE | ||||||
Compositional bias | 298-363 | Polar residues | ||||
Sequence: DPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVK | ||||||
Alternative sequence | VSP_004045 | 339-359 | in isoform 1 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U72519 EMBL· GenBank· DDBJ | AAC52862.1 EMBL· GenBank· DDBJ | mRNA | ||
AF279662 EMBL· GenBank· DDBJ | AAG23653.1 EMBL· GenBank· DDBJ | mRNA |