Protein enabled homolog (Protein name
), ENAH_MOUSE from NCBI database.
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General Annotation
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Antigen Annotation
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3D
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Predicted Eptitope
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Vaild Sequence
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Gene name:
Enah(Mena;Ndpp1);
Protein name:
Protein enabled homolog;
Alternative:
NPC-derived proline-rich protein 1(NDPP-1);
Organism:
Mouse (Mus musculus).
General Annotation
Sub Unit:
Homotetramer (By similarity). Interacts with APBB1IP, APBB1, PFN1 and ROBO4. Isoforms, containing the polyproline-rich regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms, containing the PPSY motif, bind, in vitro, to the WW2 and WW3 domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3 domain of BAIAP2-alpha but only after the autoinhibitory region of BAIAP2-alpha has been blocked by interaction with CDC42. Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from VCL, ZYX and Listeria monocytogenes actA and with TES (via LIM domain). The TES LIM domain and the Pro-rich domains from VCL or ZYX compete for the same binding site. Interaction with ZYX is important for targeting ENAH to focal adhesions and enhances production of actin-rich structures at the apical surface of cells. Interacts, through the Pro-rich region, with the C-terminal SH3 domain of DNMPB. Binds GPHN. Heterotrimer with TES and ACTL7A (By similarity). Interacts with FAT1 (via EVH1 domains).
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. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation. Required for actin-based mobility of Listeria monocytogenes.
Subcellular Location:
Cytoplasm
Cytoplasm
cytoskeleton
Cell projection
lamellipodium
Cell projection
filopodium
Cell junction
synapse
Cell junction
focal adhesion
Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);TISSUE SPECIFICITY
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5);FUNCTION;TISSUE SPECIFICITY;SUBCELLULAR LOCATION;ROLE IN L.MONOCYTOGENES MOBILITY;MISCELLANEOUS;INTERACTION WITH PFN1
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: FUNCTION;SUBCELLULAR LOCATION;TISSUE SPECIFICITY;DEVELOPMENTAL STAGE;DISRUPTION PHENOTYPE
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Cited for: FUNCTION;SUBCELLULAR LOCATION;MUTAGENESIS OF SER-255 AND SER-637
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Cited for: ALTERNATIVE SPLICING (ISOFORM 6);PHOSPHORYLATION AT TYR-557;INTERACTION WITH ABI1
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112 IN COMPLEX WITH PRO-RICH PEPTIDE OF L.MONOCYTOGENES ACTA
Vaild Sequence:
