CENTD3

From Wikipedia, the free encyclopedia

Centaurin, delta 3

Identifiers

CENTD3; ARAP3; DRAG1; FLJ21065

External IDs

OMIM: 606647 MGI: 2147274 HomoloGene: 11199

Gene ontology
Molecular Function:	• phosphatidylinositol-3,4,5-triphosphate binding • ARF GTPase activator activity • zinc ion binding • Rac GTPase activator activity • phosphatidylinositol-3,4-bisphosphate binding • metal ion binding
Cellular Component:	• ruffle • intracellular • cytoplasm • lamellipodium
Biological Process:	• cytoskeleton organization and biogenesis • signal transduction • regulation of cell shape • vesicle-mediated transport • negative regulation of cell migration • negative regulation of Rac protein signal transduction • negative regulation of Rho protein signal transduction • regulation of GTPase activity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_022481 (mRNA)
NP_071926 (protein)

NM_139206 (mRNA)
NP_631945 (protein)

Location

Chr 5: 141.01 - 141.04 Mb

Chr 18: 38.1 - 38.12 Mb

Pubmed search

[1]

[2]

Centaurin, delta 3, also known as CENTD3, is a human gene.^[1]

This gene encodes a phosphoinositide binding protein containing ARF-GAP, RHO-GAP, RAS-associating, and pleckstrin homology domains. The ARF-GAP and RHO-GAP domains cooperate in mediating rearrangements in the cell cytoskeleton and cell shape. It is a specific PtdIns(3,4,5)P3/PtdIns(3,4)P2-stimulated Arf6-GAP protein. An alternatively spliced transcript has been found for this gene, but its full-length nature has not been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: CENTD3 centaurin, delta 3.

[edit] Further reading

Raaijmakers JH, Deneubourg L, Rehmann H, et al. (2007). "The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner.". Cell. Signal. 19 (6): 1249-57. doi:10.1016/j.cellsig.2006.12.015. PMID 17314030.
Lu Q, Wei W, Kowalski PE, et al. (2005). "EST-based genome-wide gene inactivation identifies ARAP3 as a host protein affecting cellular susceptibility to anthrax toxin.". Proc. Natl. Acad. Sci. U.S.A. 101 (49): 17246-51. doi:10.1073/pnas.0407794101. PMID 15569923.
I ST, Nie Z, Stewart A, et al. (2005). "ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner.". J. Cell. Sci. 117 (Pt 25): 6071-84. doi:10.1242/jcs.01526. PMID 15546919.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
Reinhard C, Schweikert M, Wieland FT, Nickel W (2003). "Functional reconstitution of COPI coat assembly and disassembly using chemically defined components.". Proc. Natl. Acad. Sci. U.S.A. 100 (14): 8253-7. doi:10.1073/pnas.1432391100. PMID 12832619.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Santy LC, Casanova JE (2002). "GTPase signaling: bridging the GAP between ARF and Rho.". Curr. Biol. 12 (10): R360-2. PMID 12015138.
Krugmann S, Anderson KE, Ridley SH, et al. (2002). "Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices.". Mol. Cell 9 (1): 95-108. PMID 11804589.