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PROSITE documentation PDOC50870
Arfaptin homology (AH) domain profile


Description

The arfaptin homology domain (AH) is an about 210-residue region of homology, which has been identified between PICK1 and arfaptins [1]. The AH domain can be found alone or in association with other domains such as PDZ (see <PDOC50106>) [1]. The AH domain of arfaptin has been shown to dimerize and to bind Arf and Rho family GTPases [2,3].

The resolution of arfaptin has shown that the AH domain consists of three α-helices arranged as an extended antiparallel α-helical bundle. Two arfaptin AH domains associate to form a highly elongated, crescent-shaped dimer (see <PDB:1I49>) [2,3].

Some proteins known to contain an AH domain are listed below:

  • Animal protein kinase C-binding protein PICK1.
  • Animal arfaptin 1 and 2. Arfaptins are effectors of two G proteins, Rac and Arf (ADP-ribosylation factor).
  • Mammalian 69 kDa islet cell autoantigen (ICA69) [4]. It is likely to play a role in membrane trafficking at the Golgi complex and immature secretory granules in neurosecretory cells.

The profile we developed covers the entire AH domain.

Last update:

November 2003 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

AH, PS50870; Arfaptin homology (AH) domain profile  (MATRIX)


References

1AuthorsTakeya R. Takeshige K. Sumimoto H.
TitleInteraction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors.
SourceBiochem. Biophys. Res. Commun. 267:149-155(2000).
PubMed ID10623590
DOI10.1006/bbrc.1999.1932

2AuthorsTarricone C. Xiao B. Justin N. Walker P.A. Rittinger K. Gamblin S.J. Smerdon S.J.
TitleThe structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways.
SourceNature 411:215-219(2001).
PubMed ID11346801
DOI10.1038/35075620

3AuthorsCherfils J.
TitleStructural mimicry of DH domains by Arfaptin suggests a model for the recognition of Rac-GDP by its guanine nucleotide exchange factors.
SourceFEBS Lett. 507:280-284(2001).
PubMed ID11696355

4AuthorsSpitzenberger F. Pietropaolo S. Verkade P. Habermann B. Lacas-Gervais S. Mziaut H. Pietropaolo M. Solimena M.
TitleIslet cell autoantigen of 69 kDa is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells.
SourceJ. Biol. Chem. 278:26166-26173(2003).
PubMed ID12682071
DOI10.1074/jbc.M213222200



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