From Wikipedia, the free encyclopedia
Jump to: navigation, search
Myosin VA (heavy chain 12, myoxin)
Protein MYO5A PDB 1oe9.png
PDB rendering based on 1oe9.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols MYO5A ; GS1; MYH12; MYO5; MYR12
External IDs OMIM160777 MGI105976 HomoloGene20100 GeneCards: MYO5A Gene
RNA expression pattern
PBB GE MYO5A 204527 at tn.png
More reference expression data
Species Human Mouse
Entrez 4644 17918
Ensembl ENSG00000197535 ENSMUSG00000034593
UniProt Q9Y4I1 Q99104
RefSeq (mRNA) NM_000259 NM_010864
RefSeq (protein) NP_000250 NP_034994
Location (UCSC) Chr 15:
52.6 – 52.82 Mb
Chr 9:
75.07 – 75.22 Mb
PubMed search [1] [2]

Myosin-Va is a protein that in humans is encoded by the MYO5A gene.[1][2][3]

Model organisms[edit]

Model organisms have been used in the study of MYO5A function. A conditional knockout mouse line, called Myo5atm1e(KOMP)Wtsi[9][10] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[11][12][13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[7][14] Twenty five tests were carried out on mutant mice and three significant abnormalities were observed.[7] Male homozygous mutants had abnormal hair cycles, coat colouration and an increased susceptibility to bacterial infection.[7]


MYO5A has been shown to interact with DYNLL1,[15] RAB27A[16][17] and DYNLL2.[15][18]

Clinical significance[edit]

Defects are associated with Griscelli syndrome type 1, also known as Elejalde syndrome.

See also[edit]


  1. ^ Engle LJ, Kennett RH (June 1994). "Cloning, analysis, and chromosomal localization of myoxin (MYH12), the human homologue to the mouse dilute gene". Genomics 19 (3): 407–16. doi:10.1006/geno.1994.1088. PMID 8188282. 
  2. ^ Bement WM, Hasson T, Wirth JA, Cheney RE, Mooseker MS (August 1994). "Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types". Proc Natl Acad Sci U S A 91 (14): 6549–53. doi:10.1073/pnas.91.14.6549. PMC 44240. PMID 8022818. 
  3. ^ "Entrez Gene: MYO5A myosin VA (heavy chain 12, myoxin)". 
  4. ^ "Dysmorphology data for Myo5a". Wellcome Trust Sanger Institute. 
  5. ^ "Salmonella infection data for Myo5a". Wellcome Trust Sanger Institute. 
  6. ^ "Citrobacter infection data for Myo5a". Wellcome Trust Sanger Institute. 
  7. ^ a b c d Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  8. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  9. ^ "International Knockout Mouse Consortium". 
  10. ^ "Mouse Genome Informatics". 
  11. ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.  edit
  12. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  13. ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  14. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. 
  15. ^ a b Naisbitt, S; Valtschanoff J; Allison D W; Sala C; Kim E; Craig A M; Weinberg R J; Sheng M (June 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". J. Neurosci. (UNITED STATES) 20 (12): 4524–34. ISSN 0270-6474. PMID 10844022. 
  16. ^ Wu, Xufeng; Wang Fei; Rao Kang; Sellers James R; Hammer John A (May 2002). "Rab27a is an essential component of melanosome receptor for myosin Va". Mol. Biol. Cell (United States) 13 (5): 1735–49. doi:10.1091/mbc.01-12-0595. ISSN 1059-1524. PMC 111140. PMID 12006666. 
  17. ^ Nagashima, Kazuaki; Torii Seiji; Yi Zhaohong; Igarashi Michihiro; Okamoto Koichi; Takeuchi Toshiyuki; Izumi Tetsuro (April 2002). "Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions". FEBS Lett. (Netherlands) 517 (1–3): 233–8. doi:10.1016/S0014-5793(02)02634-0. ISSN 0014-5793. PMID 12062444. 
  18. ^ Puthalakath, H; Villunger A; O'Reilly L A; Beaumont J G; Coultas L; Cheney R E; Huang D C; Strasser A (September 2001). "Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis". Science (United States) 293 (5536): 1829–32. doi:10.1126/science.1062257. ISSN 0036-8075. PMID 11546872. 

Further reading[edit]