|SMART accession number:||SM01015|
|Description:||Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.|
|Interpro abstract (IPR010504):|
The arfaptin homology (AH) domain is a protein domain found in a range of proteins, including arfaptins, protein kinase C-binding protein PICK1 [(PUBMED:10623590)] and mammalian 69 kDa islet cell autoantigen (ICA69) [(PUBMED:12682071)]. The AH domain of arfaptin has been shown to dimerise and to bind Arf and Rho family GTPases [(PUBMED:11346801), (PUBMED:11696355)], including ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules.
The AH domain consists of three alpha-helices arranged as an extended antiparallel alpha-helical bundle. Two arfaptin AH domains associate to form a highly elongated, crescent-shaped dimer [(PUBMED:11346801), (PUBMED:11696355)].
|GO function:||protein domain specific binding (GO:0019904)|
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- Evolution (species in which this domain is found)
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- Structure (3D structures containing this domain)
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