Unconventional myosin-Id (MYO1D)

The protein contains 1006 amino acids for an estimated molecular weight of 116202 Da.

 

Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity). Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity). Required for normal planar cell polarity in ciliated tracheal cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement in the trachea. Required for normal, polarized cilia organization in brain ependymal epithelial cells (By similarity). (updated: Feb. 13, 2019)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology.


Interpro domains
Total structural coverage: 100%
Model score: 36

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VariantDescription
dbSNP:rs7209106
dbSNP:rs7215958

The reference OMIM entry for this protein is 606539

Myosin id; myo1d
Kiaa0727

Myosins are molecular motors that, upon interaction with actin filaments, utilize energy from ATP hydrolysis to generate mechanical force. For further background information on myosins, see MYO1A (601478).

CLONING

By screening for cDNAs with the potential to encode large proteins expressed in brain, Nagase et al. (1998) identified a cDNA encoding MYO1D, which they called KIAA0727. The deduced 674-amino acid protein is 98% identical to rat Myr4. RT-PCR analysis detected expression of KIAA0727 in all tissues tested, with highest levels in brain, followed by lung and ovary; expression was lowest in spleen.

MAPPING

By radiation hybrid analysis, Nagase et al. (1998) mapped the MYO1D gene to chromosome 17. Hasson et al. (1996) mapped the mouse gene to chromosome 11 by interspecific backcross analysis and predicted a localization of 17q11-q12 in human.

ANIMAL MODEL

Hozumi et al. (2006) found that handedness of the embryonic gut and the adult gut and testes is reversed (not randomized) in viable and fertile homozygous Myo31DF Drosophila mutants. Myo31DF encodes an unconventional myosin, Drosophila MyoIA (also referred to as MYO1D in mammals), and is the first actin-based motor protein to be implicated in left-right patterning. Hozumi et al. (2006) found that Myo31DF is required in the hindgut epithelium for normal embryonic handedness. Disruption of actin filaments in hindgut epithelium randomizes the handedness of the embryonic gut, suggesting that Myo31DF function requires the actin cytoskeleton. Consistent with this, Hozumi et al. (2006) found that Myo31DF colocalizes with the cytoskeleton. Overexpression of Myo61F, another myosin I, reversed the handedness of the embryonic gut, and its knockdown also caused a left-right patterning defect. Hozumi et al. (2006) suggested that these 2 unconventional myosin I proteins may have antagonistic functions in left-right patterning. They suggested that the actin cytoskeleton and myosin I proteins may be crucial for generating left-right asymmetry in invertebrates. Speder et al. (2006) identified the conserved Myo31DF gene in Drosophila as a unique situs inversus locus. Myo31DF mutations reversed the dextral looping of genitalia, a prominent left-right marker in adult flies. Genetic mosaic analysis pinpointed the A8 segment of the genital disc as a left-right organizer and revealed an anterior-posterior compartmentalization of Myo31DF function that directs dextral development and represses a sinistral default state. As expected of a determinant, Myo31DF has a trigger-like function and is expressed symmetrically in the organizer, and its symmetrical overexpression does not impair left-right asymmetry. Thus, Speder et al. (2006) concluded that Myo31DF is a dextral gene with actin-based motor activity controlling situs choice. Like mouse inversin, Myo31DF interacts and colocalizes with beta-catenin, suggesting that situs inversus genes can direct left-right development through the adherens junction. ... More on the omim web site

Subscribe to this protein entry history

Feb. 22, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606539 was added.