Summary: Arfaptin-like domain
This is the Wikipedia entry entitled "Arfaptin". More...
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Arfaptin Edit Wikipedia article
|crystal structure analysis of rac1-gdp complexed with arfaptin (p21)|
In molecular biology, the arfaptin domain is a protein domain which 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.
- ^ Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ (May 2001). "The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways". Nature 411 (6834): 2159. doi:10.1038/35075620. PMID 11346801.
- ^ Spitzenberger F, Pietropaolo S, Verkade P, Habermann B, Lacas-Gervais S, Mziaut H, Pietropaolo M, Solimena M (July 2003). "Islet cell autoantigen of 69 kDa is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells". J. Biol. Chem. 278 (28): 2616673. doi:10.1074/jbc.M213222200. PMID 12682071.
Arfaptin-like domain Provide feedback
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 .
Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ; , Nature 2001;411:215-219.: The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. PUBMED:11346801 EPMC:11346801
Spitzenberger F, Pietropaolo S, Verkade P, Habermann B, Lacas-Gervais S, Mziaut H, Pietropaolo M, Solimena M; , J Biol Chem 2003;278:26166-26173.: Islet Cell Autoantigen of 69 kDa Is an Arfaptin-related Protein Associated with the Golgi Complex of Insulinoma INS-1 Cells. PUBMED:12682071 EPMC:12682071
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||protein domain specific binding (GO:0019904)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Seed source:||Pfam-B_5314 (release 7.5)|
|Number in seed:||11|
|Number in full:||535|
|Average length of the domain:||209.60 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||55.43 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Arfaptin domain has been found. There are 10 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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