MYO1A

Myosin-Ia is a protein that in humans is encoded by the MYO1A gene.[5][6][7]

MYO1A
Identifiers
Aliases	MYO1A, BBMI, DFNA48, MIHC, MYHL, myosin IA
External IDs	OMIM: 601478 MGI: 107732 HomoloGene: 21113 GeneCards: MYO1A
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.3 Start 57,028,517 bp[1] End 57,051,198 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 D3|10 74.62 cM Start 127,705,170 bp[2] End 127,720,940 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • actin binding • actin filament binding • cellular motor activity • calmodulin binding • ATP binding • microtubule motor activity • microtubule binding Cellular component • filamentous actin • brush border • cytoplasm • cortical actin cytoskeleton • microvilli • apical plasma membrane • basal plasma membrane • plasma membrane raft • myosin complex • basolateral plasma membrane • lateral plasma membrane Biological process • sensory perception of sound • microvillus assembly • cell projection organization • vesicle localization • microtubule-based movement Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4640	432516
Ensembl	ENSG00000166866	ENSMUSG00000025401
UniProt	Q9UBC5	O88329
RefSeq (mRNA)	NM_001256041 NM_005379	NM_001081219
RefSeq (protein)	NP_001242970 NP_005370	NP_001074688
Location (UCSC)	Chr 12: 57.03 – 57.05 Mb	Chr 10: 127.71 – 127.72 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene belongs to the myosin superfamily. Myosins are molecular motors that, upon interaction with actin filaments, utilize energy from ATP hydrolysis to generate mechanical force. Each myosin has a conserved N-terminal motor domain that contains both ATP-binding and actin-binding sequences. Following the motor domain is a light-chain-binding 'neck' region containing 1-6 copies of a repeat element, the IQ motif, that serves as a binding site for calmodulin or other members of the EF-hand superfamily of calcium-binding proteins. At the C-terminus, each myosin class has a distinct tail domain that serves in dimerization, membrane binding, protein binding, and/or enzymatic activities and targets each myosin to its particular subcellular location. The myosin-1a protein is expressed by enterocytes, the epithelial cells that line the luminal surface of the small intestine. In these cells the myosin-1a protein localizes specifically to the brush border. Experiments indicate that the brush border population of the encoded protein turns over rapidly, while its head and tail domains interact transiently with the core actin and plasma membrane, respectively. A rapidly exchanging pool of the myosin-1a protein binds to the actin core bundle, which turns over on a much slower timescale.[8]