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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC50870
Arfaptin homology (AH) domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC50870

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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