ACTN3 (gene)

Actinin, alpha 3
PDB rendering based on 1tjt.
Available structures: 1tjt, 1wku
Identifiers
Symbol(s)	ACTN3; MGC117002; MGC117005
External IDs	OMIM: 102574 MGI: 99678 Homologene: 862
Gene ontology Molecular Function: • actin binding • integrin binding • calcium ion binding • protein binding • structural constituent of muscle • protein homodimerization activity Cellular Component: • actin filament • focal adhesion • pseudopodium Biological Process: • muscle contraction • regulation of apoptosis • focal adhesion formation
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	89	11474
Ensembl	ENSG00000204633	ENSMUSG00000006457
Uniprot	Q08043	Q14DS8
Refseq	NM_001104 (mRNA) NP_001095 (protein)	NM_013456 (mRNA) NP_038484 (protein)
Location	Chr 11: 66.07 - 66.09 Mb	Chr 19: 4.86 - 4.88 Mb
Pubmed search	[1]	[2]

Actinin, alpha 3, also known as ACTN3, is a human gene.

Alpha-actinin is an actin-binding protein with multiple roles in different cell types. This gene expression is limited to skeletal muscle. It is localized to the Z-disc and analogous dense bodies, where it helps to anchor the myofibrillar actin filaments

Further reading

• MacArthur DG, North KN (2004). "A gene for speed? The evolution and function of alpha-actinin-3.". Bioessays 26 (7): 786-95. doi:10.1002/bies.20061. PMID 15221860.
• Beggs AH, Byers TJ, Knoll JH, et al. (1992). "Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11.". J. Biol. Chem. 267 (13): 9281-8. PMID 1339456.
• Yürüker B, Niggli V (1992). "Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network.". J. Cell. Sci. 101 ( Pt 2): 403-14. PMID 1629252.
• Pavalko FM, LaRoche SM (1993). "Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin.". J. Immunol. 151 (7): 3795-807. PMID 8104223.
• Chan Y, Tong HQ, Beggs AH, Kunkel LM (1998). "Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo.". Biochem. Biophys. Res. Commun. 248 (1): 134-9. PMID 9675099.
• North KN, Yang N, Wattanasirichaigoon D, et al. (1999). "A common nonsense mutation results in alpha-actinin-3 deficiency in the general population.". Nat. Genet. 21 (4): 353-4. doi:10.1038/7675. PMID 10192379.
• Nikolopoulos SN, Spengler BA, Kisselbach K, et al. (2000). "The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells.". Oncogene 19 (3): 380-6. doi:10.1038/sj.onc.1203310. PMID 10656685.
• Takada F, Vander Woude DL, Tong HQ, et al. (2001). "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines.". Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1595-600. doi:10.1073/pnas.041609698. PMID 11171996.
• Bang ML, Mudry RE, McElhinny AS, et al. (2001). "Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies.". J. Cell Biol. 153 (2): 413-27. PMID 11309420.
• Mills M, Yang N, Weinberger R, et al. (2001). "Differential expression of the actin-binding proteins, alpha-actinin-2 and -3, in different species: implications for the evolution of functional redundancy.". Hum. Mol. Genet. 10 (13): 1335-46. PMID 11440986.
• 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.
• Burgueño J, Blake DJ, Benson MA, et al. (2003). "The adenosine A2A receptor interacts with the actin-binding protein alpha-actinin.". J. Biol. Chem. 278 (39): 37545-52. doi:10.1074/jbc.M302809200. PMID 12837758.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
• Clarkson PM, Devaney JM, Gordish-Dressman H, et al. (2005). "ACTN3 genotype is associated with increases in muscle strength in response to resistance training in women.". J. Appl. Physiol. 99 (1): 154-63. doi:10.1152/japplphysiol.01139.2004. PMID 15718405.
• Franzot G, Sjöblom B, Gautel M, Djinović Carugo K (2005). "The crystal structure of the actin binding domain from alpha-actinin in its closed conformation: structural insight into phospholipid regulation of alpha-actinin.". J. Mol. Biol. 348 (1): 151-65. doi:10.1016/j.jmb.2005.01.002. PMID 15808860.
• Clarkson PM, Hoffman EP, Zambraski E, et al. (2005). "ACTN3 and MLCK genotype associations with exertional muscle damage.". J. Appl. Physiol. 99 (2): 564-9. doi:10.1152/japplphysiol.00130.2005. PMID 15817725.
• Asanuma K, Kim K, Oh J, et al. (2005). "Synaptopodin regulates the actin-bundling activity of alpha-actinin in an isoform-specific manner.". J. Clin. Invest. 115 (5): 1188-98. doi:10.1172/JCI200523371. PMID 15841212.
• Niemi AK, Majamaa K (2005). "Mitochondrial DNA and ACTN3 genotypes in Finnish elite endurance and sprint athletes.". Eur. J. Hum. Genet. 13 (8): 965-9. doi:10.1038/sj.ejhg.5201438. PMID 15886711.
• Triplett JW, Pavalko FM (2006). "Disruption of alpha-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosis.". Am. J. Physiol., Cell Physiol. 291 (5): C909-21. doi:10.1152/ajpcell.00113.2006. PMID 16807302.