Actin, alpha skeletal muscle

Details

Name
Actin, alpha skeletal muscle
Synonyms
  • ACTA
  • Alpha-actin-1
Gene Name
ACTA1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016680|Actin, alpha skeletal muscle
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF
Number of residues
377
Molecular Weight
42050.67
Theoretical pI
5.05
GO Classification
Functions
ADP binding / ATP binding / myosin binding / structural constituent of cytoskeleton
Processes
cell growth / mesenchyme migration / muscle contraction / muscle filament sliding / positive regulation of gene expression / response to extracellular stimulus / response to lithium ion / response to mechanical stimulus / response to steroid hormone / skeletal muscle fiber adaptation / skeletal muscle fiber development / skeletal muscle thin filament assembly
Components
actin cytoskeleton / actin filament / blood microparticle / cell body / cytosol / extracellular exosome / extracellular space / filopodium / lamellipodium / sarcomere / stress fiber / striated muscle thin filament
General Function
Structural constituent of cytoskeleton
Specific Function
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016681|Actin, alpha skeletal muscle (ACTA1)
ATGTGCGACGAAGACGAGACCACCGCCCTCGTGTGCGACAATGGCTCCGGCCTGGTGAAA
GCCGGCTTCGCCGGGGATGACGCCCCTAGGGCCGTGTTCCCGTCCATCGTGGGCCGCCCC
CGACACCAGGGCGTCATGGTCGGTATGGGTCAGAAAGATTCCTACGTGGGCGACGAGGCT
CAGAGCAAGAGAGGTATCCTGACCCTGAAGTACCCTATCGAGCACGGCATCATCACCAAC
TGGGATGACATGGAGAAGATCTGGCACCACACCTTCTACAACGAGCTTCGCGTGGCTCCC
GAGGAGCACCCCACCCTGCTCACCGAGGCCCCCCTCAATCCCAAGGCCAACCGCGAGAAG
ATGACCCAGATCATGTTTGAGACCTTCAACGTGCCCGCCATGTACGTGGCCATCCAGGCC
GTGCTGTCCCTCTACGCCTCCGGCAGGACCACCGGCATCGTGCTGGACTCCGGCGACGGC
GTCACCCACAACGTGCCCATTTATGAGGGCTACGCGCTGCCGCACGCCATCATGCGCCTG
GACCTGGCGGGCCGCGATCTCACCGACTACCTGATGAAGATCCTCACTGAGCGTGGCTAC
TCCTTCGTGACCACAGCTGAGCGCGAGATCGTGCGCGACATCAAGGAGAAGCTGTGCTAC
GTGGCCCTGGACTTCGAGAACGAGATGGCGACGGCCGCCTCCTCCTCCTCCCTGGAAAAG
AGCTACGAGCTGCCAGACGGGCAGGTCATCACCATCGGCAACGAGCGCTTCCGCTGCCCG
GAGACGCTCTTCCAGCCCTCCTTCATCGGTATGGAGTCGGCGGGCATTCACGAGACCACC
TACAACAGCATCATGAAGTGTGACATCGACATCAGGAAGGACCTGTATGCCAACAACGTC
ATGTCGGGGGGCACCACGATGTACCCTGGGATCGCTGACCGCATGCAGAAAGAGATCACC
GCGCTGGCACCCAGCACCATGAAGATCAAGATCATCGCCCCGCCGGAGCGCAAATACTCG
GTGTGGATCGGCGGCTCCATCCTGGCCTCGCTGTCCACCTTCCAGCAGATGTGGATCACC
AAGCAGGAGTACGACGAGGCCGGCCCTTCCATCGTCCACCGCAAATGCTTCTAG
Chromosome Location
1
Locus
1q42.13-q42.2
External Identifiers
ResourceLink
UniProtKB IDP68133
UniProtKB Entry NameACTS_HUMAN
GenBank Protein ID178029
GenBank Gene IDJ00068
GenAtlas IDACTA1
HGNC IDHGNC:129
General References
  1. Hanauer A, Levin M, Heilig R, Daegelen D, Kahn A, Mandel JL: Isolation and characterization of cDNA clones for human skeletal muscle alpha actin. Nucleic Acids Res. 1983 Jun 11;11(11):3503-16. [Article]
  2. Taylor A, Erba HP, Muscat GE, Kedes L: Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains. Genomics. 1988 Nov;3(4):323-36. [Article]
  3. Nowak KJ, Wattanasirichaigoon D, Goebel HH, Wilce M, Pelin K, Donner K, Jacob RL, Hubner C, Oexle K, Anderson JR, Verity CM, North KN, Iannaccone ST, Muller CR, Nurnberg P, Muntoni F, Sewry C, Hughes I, Sutphen R, Lacson AG, Swoboda KJ, Vigneron J, Wallgren-Pettersson C, Beggs AH, Laing NG: Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy. Nat Genet. 1999 Oct;23(2):208-12. [Article]
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  6. Hauser MA, Horrigan SK, Salmikangas P, Torian UM, Viles KD, Dancel R, Tim RW, Taivainen A, Bartoloni L, Gilchrist JM, Stajich JM, Gaskell PC, Gilbert JR, Vance JM, Pericak-Vance MA, Carpen O, Westbrook CA, Speer MC: Myotilin is mutated in limb girdle muscular dystrophy 1A. Hum Mol Genet. 2000 Sep 1;9(14):2141-7. [Article]
  7. Bosch-Comas A, Lindsten K, Gonzalez-Duarte R, Masucci MG, Marfany G: The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins. Cell Mol Life Sci. 2006 Mar;63(6):723-34. [Article]
  8. Kudryashov DS, Durer ZA, Ytterberg AJ, Sawaya MR, Pashkov I, Prochazkova K, Yeates TO, Loo RR, Loo JA, Satchell KJ, Reisler E: Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18537-42. doi: 10.1073/pnas.0808082105. Epub 2008 Nov 17. [Article]
  9. Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y: The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. doi: 10.1074/mcp.M111.012658. Epub 2011 Sep 9. [Article]
  10. Li MM, Nilsen A, Shi Y, Fusser M, Ding YH, Fu Y, Liu B, Niu Y, Wu YS, Huang CM, Olofsson M, Jin KX, Lv Y, Xu XZ, He C, Dong MQ, Rendtlew Danielsen JM, Klungland A, Yang YG: ALKBH4-dependent demethylation of actin regulates actomyosin dynamics. Nat Commun. 2013;4:1832. doi: 10.1038/ncomms2863. [Article]
  11. Heisler DB, Kudryashova E, Grinevich DO, Suarez C, Winkelman JD, Birukov KG, Kotha SR, Parinandi NL, Vavylonis D, Kovar DR, Kudryashov DS: ACTIN-DIRECTED TOXIN. ACD toxin-produced actin oligomers poison formin-controlled actin polymerization. Science. 2015 Jul 31;349(6247):535-9. doi: 10.1126/science.aab4090. [Article]
  12. Ilkovski B, Cooper ST, Nowak K, Ryan MM, Yang N, Schnell C, Durling HJ, Roddick LG, Wilkinson I, Kornberg AJ, Collins KJ, Wallace G, Gunning P, Hardeman EC, Laing NG, North KN: Nemaline myopathy caused by mutations in the muscle alpha-skeletal-actin gene. Am J Hum Genet. 2001 Jun;68(6):1333-43. Epub 2001 Apr 27. [Article]
  13. Sparrow JC, Nowak KJ, Durling HJ, Beggs AH, Wallgren-Pettersson C, Romero N, Nonaka I, Laing NG: Muscle disease caused by mutations in the skeletal muscle alpha-actin gene (ACTA1). Neuromuscul Disord. 2003 Sep;13(7-8):519-31. [Article]
  14. Jungbluth H, Sewry CA, Brown SC, Nowak KJ, Laing NG, Wallgren-Pettersson C, Pelin K, Manzur AY, Mercuri E, Dubowitz V, Muntoni F: Mild phenotype of nemaline myopathy with sleep hypoventilation due to a mutation in the skeletal muscle alpha-actin (ACTA1) gene. Neuromuscul Disord. 2001 Jan;11(1):35-40. [Article]
  15. Agrawal PB, Strickland CD, Midgett C, Morales A, Newburger DE, Poulos MA, Tomczak KK, Ryan MM, Iannaccone ST, Crawford TO, Laing NG, Beggs AH: Heterogeneity of nemaline myopathy cases with skeletal muscle alpha-actin gene mutations. Ann Neurol. 2004 Jul;56(1):86-96. [Article]
  16. Laing NG, Clarke NF, Dye DE, Liyanage K, Walker KR, Kobayashi Y, Shimakawa S, Hagiwara T, Ouvrier R, Sparrow JC, Nishino I, North KN, Nonaka I: Actin mutations are one cause of congenital fibre type disproportion. Ann Neurol. 2004 Nov;56(5):689-94. [Article]
  17. Ilkovski B, Nowak KJ, Domazetovska A, Maxwell AL, Clement S, Davies KE, Laing NG, North KN, Cooper ST: Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms. Hum Mol Genet. 2004 Aug 15;13(16):1727-43. Epub 2004 Jun 15. [Article]
  18. Kaindl AM, Ruschendorf F, Krause S, Goebel HH, Koehler K, Becker C, Pongratz D, Muller-Hocker J, Nurnberg P, Stoltenburg-Didinger G, Lochmuller H, Huebner A: Missense mutations of ACTA1 cause dominant congenital myopathy with cores. J Med Genet. 2004 Nov;41(11):842-8. [Article]
  19. Ohlsson M, Tajsharghi H, Darin N, Kyllerman M, Oldfors A: Follow-up of nemaline myopathy in two patients with novel mutations in the skeletal muscle alpha-actin gene (ACTA1). Neuromuscul Disord. 2004 Sep;14(8-9):471-5. [Article]
  20. Hutchinson DO, Charlton A, Laing NG, Ilkovski B, North KN: Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: clinical and pathological variability within a kindred. Neuromuscul Disord. 2006 Feb;16(2):113-21. Epub 2006 Jan 19. [Article]
  21. D'Amico A, Graziano C, Pacileo G, Petrini S, Nowak KJ, Boldrini R, Jacques A, Feng JJ, Porfirio B, Sewry CA, Santorelli FM, Limongelli G, Bertini E, Laing N, Marston SB: Fatal hypertrophic cardiomyopathy and nemaline myopathy associated with ACTA1 K336E mutation. Neuromuscul Disord. 2006 Oct;16(9-10):548-52. Epub 2006 Sep 1. [Article]
  22. Clarke NF, Ilkovski B, Cooper S, Valova VA, Robinson PJ, Nonaka I, Feng JJ, Marston S, North K: The pathogenesis of ACTA1-related congenital fiber type disproportion. Ann Neurol. 2007 Jun;61(6):552-61. [Article]
  23. Domazetovska A, Ilkovski B, Kumar V, Valova VA, Vandebrouck A, Hutchinson DO, Robinson PJ, Cooper ST, Sparrow JC, Peckham M, North KN: Intranuclear rod myopathy: molecular pathogenesis and mechanisms of weakness. Ann Neurol. 2007 Dec;62(6):597-608. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02772Sucroseapproved, experimental, investigationalunknownDetails
DB03021Ulapualide AexperimentalunknownDetails
DB03616Kabiramide CexperimentalunknownDetails
DB03850Jaspisamide AexperimentalunknownDetails
DB03903TmrexperimentalunknownDetails
DB041511-MethylhistidineexperimentalunknownDetails
DB04395Phosphoaminophosphonic Acid-Adenylate EsterexperimentalunknownDetails
DB04629Aplyronine AexperimentalunknownDetails
DB04774Reidispongiolide AexperimentalunknownDetails
DB04775Reidispongiolide CexperimentalunknownDetails
DB04783Sphinxolide BexperimentalunknownDetails
DB08080Latrunculin BexperimentalunknownDetails
DB02621Latrunculin AexperimentalunknowninhibitorDetails