Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein- like) (EVL RNB6)

Function: - enhances actin nucleation & polymerization - required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes - binds to the SH3 domains of ABL1, LYN & SRC - binds to profilin, with preference for isoform IIa of PFN2, & 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 - phosphorylated by PKA, phosphorylation abolishes binding to SH3 domains of ABL & SRC Structure: - homotetramer - belongs to the Ena/VASP family - contains 1 WH1 domain - 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 & for actin polymerization - block B is required for F-actin binding & subcellular location - block C is required for tetramerization Compartment: - cytoplasm, cytoskeleton - cell projection, lamellipodium - targeted to the leading edge of lamellipodia & the dital tip of stress fibers - in activated T-cells, localizes to the F-actin collar & the distal tip of microspikes (putative) Alternative splicing: named isoforms=2

General

Ena/VASPfamily phosphoprotein

Properties

SIZE: MW = 45 kD entity length = 416 aa COMPARTMENT: cytoplasm MOTIF: WH1 {1-112} proline-rich region SITE: 162-206 MOTIF: proline residue (SEVERAL) EVH2 block A {222-242} MOTIF: KLKR {231-234} EVH2 block B {265-282} MOTIF: Ser phosphorylation site {S329} Ser phosphorylation site {S331} Ser phosphorylation site {S349} EVH2 block C {379-413}

Database Correlations

UniProt Q9UI08 PFAM correlations

References

UniProt :accession Q9UI08