Actin-related protein 2/3 complex subunit 1A (ARPC1A)
The protein contains 370 amino acids for an estimated molecular weight of 41569 Da.
Probably functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
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Biological Process
Actin cytoskeleton organization
Arp2/3 complex-mediated actin nucleation
Ephrin receptor signaling pathway
Fc-gamma receptor signaling pathway involved in phagocytosis
Membrane organization
The reference OMIM entry for this protein is 604220
Actin-related protein 2/3 complex, subunit 1a; arpc1a
Sop2-like; sop2l
DESCRIPTION
The ARP2/3 protein complex (604221) is involved in the control of actin polymerization in cells. The human complex consists of 7 subunits, including the actin-related proteins ARP2 (ACTR2; 604221) and ARP3 (ACTR3; 604222). ARPC1A and ARPC1B (604223) are thought to encode alternate p41 regulatory subunits of the ARP2/3 complex (Welch et al., 1997).CLONING
The S. pombe Sop2 (suppressor of profilin-2) gene product is essential for cell viability. By searching DNA databases for sequences that encode proteins with sequence similarity to S. pombe Sop2, Balasubramanian et al. (1996) identified Sop2-like human ESTs. Using 1 of these ESTs, they isolated a full-length HeLa cell cDNA encoding ARPC1A, a Sop2-like protein, which they named SOP2HS. The deduced 370-amino acid ARPC1A protein contains beta-transducin repeats.GENE FUNCTION
Sop2-null S. pombe mutants display defects that suggest a role for the Sop2 protein in multiple cortical actin-dependent processes. The S. pombe Sop2 protein is present in a complex that also contains Arp3. Balasubramanian et al. (1996) found that human ARPC1A functionally complemented an S. pombe Sop2 mutation. Laurila et al. (2009) identified ARPC1A and ARPC1B within a region of chromosome 7q21-q22 that was amplified in about 25% of pancreatic cancer cell lines and primary pancreatic tumors examined. RT-PCR showed that amplification resulted in increased expression of ARPC1A and ARPC1B. Silencing of ARPC1A by small interfering RNA reduced cell proliferation, migration, and invasion in a pancreatic cancer cell line with a high level of amplification. Silencing of ARPC1B decreased cell migration, but it had no effect on cell proliferation and invasion.MAPPING
By genomic sequence analysis, Laurila et al. (2009) mapped the ARPC1A gene to chromosome 7q21-q22. ... More on the omim web site
June 7, 2019: Protein entry updated
Automatic update: OMIM entry 604220 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).