Alpha-centractin (ACTR1A)

The protein contains 376 amino acids for an estimated molecular weight of 42614 Da.

 

Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome. (updated: April 1, 2015)

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. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. 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.
  4. 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.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. 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.

Interpro domains
Total structural coverage: 99%
Model score: 22

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The reference OMIM entry for this protein is 605143

Actin-related protein 1a; actr1a
Arp1
Centractin, alpha

DESCRIPTION

ACTR1A is an essential subunit of the 20S dynactin complex, which is involved in microtubule-dependent vesicular transport, spindle assembly, and cell division. Polymers of 8 to 13 ACTR1 molecules make up the central 37-nm filament that forms the base of the dynactin complex (summary by Karki et al., 2000).

CLONING

By randomly sequencing a brain cDNA library, Adams et al. (1991) identified a cDNA (EST00370) encoding a 37-amino acid peptide with 76% similarity to actin. Using oligonucleotide probes derived from clone EST00370 to screen a teratocarcinoma library, Lees-Miller et al. (1992) obtained a cDNA encoding ACTR1A, which they called actin-RPV (vertebrate actin-related protein). Sequence analysis predicted that the 376-amino acid ACTR1A protein shares only 69% amino acid similarity with vertebrate actins; most of the nonconservative substitutions occur in the surface loops of ACTR1A rather than the core structure. Two-dimensional immunoblot analysis of the dynactin complex, an activator of dynein-driven vesicle movement (see 601143), determined that ACTR1A is the most abundant molecule in the complex and is expressed as a 45-kD protein with a pI of 6.8. By screening a testis cDNA library with a canine alpha-centractin probe, Clark et al. (1994) isolated cDNAs encoding ACTR1A, which they called alpha-centractin. Northern blot analysis detected variable levels of a 3.0-kb ACTR1A transcript in all tissues tested. The same probe also detected a 1.3-kb transcript representing a putative truncated isoform, which the authors called centractin-gamma. Two-dimensional immunoblot analysis determined that ACTR1A is expressed in the cytosol as part of the dynactin complex as a 43-kD protein with a pI of 6.6; levels of ACTR1A were at least 15-fold greater than those of ACTR1B (605144).

GENE FUNCTION

Eaton et al. (2002) disrupted the dynactin complex in Drosophila, using 3 separate perturbations: dsRNA interference with arp1, mutation in p150/Glued (homolog of DCTN1; 601143), and a dominant-negative Glued transgene. In all 3 cases, the disruption resulted in an increase in the frequency and extent of synaptic retraction events at the neuromuscular junction. Eaton et al. (2002) concluded that dynactin functions locally within the presynaptic arbor to promote synapse stability at the neuromuscular junction. Karki et al. (2000) noted that one end of the ARP1 filament is likely capped by the alpha (see 601580) and beta (CAPZB; 601572) subunits of capping protein. They found that the other end of ARP1 was bound by p62 dynactin (DCTN4; 614758).

MAPPING

Gross (2012) mapped the ACTR1A gene to chromosome 10q24.32 based on an alignment of the ACTR1A sequence (GenBank GENBANK AK302072) with the genomic sequence (GRCh37). ... More on the omim web site

Subscribe to this protein entry history

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

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

Nov. 23, 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 605143 was added.