Protein Domain : Arf GTPase activating protein 3, BAR domain IPR028775

Type	Domain
Description	The Arf GAPs (GTPase-activating proteins) are a family of multidomain proteins with the common function of accelerating the hydrolysis of GTP bound to Arf proteins. ASAP proteins are a subtype of Arf GAPs. ASAP3 (Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3, also known as ACAP4, DDEFL1 (Development and Differentiation Enhancing Factor-Like 1), or centaurin beta-6), is a focal adhesion-associated Arf GAP that functions in cell migration and invasion of cancers [ , ]. It is an Arf6-specific GTPase activating protein (GAP) and is co-localized with Arf6 in ruffling membranes upon EGF stimulation []. ASAP3 promotes cell proliferation [], being implicated in the pathogenesis of hepatocellular carcinoma and plays a role in regulating cell migration and invasion [].ASAP3 (Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3) contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain and ankyrin (ANK) repeats. Unlike ASAP1 and ASAP2, ASAP3 do not have an SH3 domain at the C-terminal. This entry represents the N-terminal BAR domain, domains that form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions [, , . The BAR domain of the related protein ASAP1 mediates membrane bending, is essential for function, and auto inhibits GAP activity by interacting with the PH and/or Arf GAP domains.
Short Name	BAR_ASAP3