Actin, alpha cardiac muscle 1 (ACTC1)
The protein contains 377 amino acids for an estimated molecular weight of 42019 Da.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- 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.
- 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.
Biological Process
Actin filament organization
Actin filament-based movement
Actin-myosin filament sliding
Actomyosin structure organization
Cardiac muscle contraction
Cardiac muscle tissue morphogenesis
Cardiac myofibril assembly
Heart contraction
Mesenchyme migration
Muscle filament sliding
Negative regulation of apoptotic process
Positive regulation of gene expression
Response to drug
Response to ethanol
Skeletal muscle thin filament assembly
The reference OMIM entry for this protein is 102540
Actin, alpha, cardiac muscle; actc1
Actc
Smooth muscle actin
Actin, alpha
CLONING
Because actin is a highly conserved protein, Engel et al. (1981) could use cloned actin genes from Drosophila and from chicken to isolate 12 actin gene fragments from a human DNA library. Restriction endonuclease studies of each indicated that they are not allelic and are from nonoverlapping regions of the genome. In all, 25 to 30 EcoRI fragments homologous to actin genes were found in the human genome and no restriction site polymorphism was found indicating evolutionary conservatism. Humphries et al. (1981) used probes from the mouse to detect actin genes in human DNA and concluded that there are about 20 actin genes in the human genome. Three lines of evidence supported this number: the rate of hybridization of the mouse probe with human DNA; the fact that the probe hybridizes to 17-20 bands in Southern blots of restriction enzyme digests of total human DNA; restriction enzyme mapping of individual human actin genes indicating at least 9 different genes, judged on probability grounds to have been picked from a pool of at least 20. Hamada et al. (1982) isolated and characterized the human cardiac actin gene. The cardiac and skeletal actin genes showed close similarity, suggesting a relatively recent derivation from a common ancestral gene. Nucleotide sequences of all exon/intron boundaries agreed with the GT/AG rule (GT at the 5-prime and AG at the 3-prime termini of each intron). Gunning et al. (1984) noted that the cardiac actin gene and the skeletal actin gene (102610) on chromosome 1 are coexpressed in both skeletal and heart muscle.MAPPING
Using a cDNA fragment from an exon of the human cardiac actin gene in somatic hybrid cell studies, Shows et al. (1984) showed that the gene is coded by the segment 15q11-qter. Crosby et al. (1989) showed that in the mouse the cardiac actin gene (Actc-1) is not on chromosome 17 as previously reported (Czosnek et al., 1983) but is located on chromosome 2. It is closely linked to beta-2-microglobulin as indicated by mapping studies using restriction fragment variants in recombinant inbred strains. Using a highly polymorphic CA repeat microsatellite within intron 4 of the ACTC gene, Kramer et al. (1992) did family linkage studies with multiple markers on 15q, thus permitting the gene to be placed on the chromosome linkage map. They demonstrated that it lies about 0.06 cM proximal to D15S49, which is about 0.05 cM proximal to D15S25, which in turn is about 0.07 cM proximal to D15S1; D15S1 is tightly linked to the Marfan syndrome and to fibrillin. Thus ACTC may be about 0.18 cM proximal to the fibrillin locus and no more distal than 15q21.1. By fluorescence in situ hybridization, Ueyama et al. (1995) assigned the ACTC1 gene to chromosome 15q14.GENE FUNCTION
Actin has been identified in many kinds of cells including muscle, where it is a major constituent of the thin filament, and platelets. Muscle actins from sources as diverse as rabbits and fish are very similar in amino acid sequence. Elzinga et al. (1976) examined whether actin in different tissues of the same organism are products of the same gene. They found that human platelet and human cardiac actins differ by one amino acid, viz., threonine and valine, respectively, at position 129. Thus they must be determined by different genes. Actins can be separated by isoelectric focusing into 3 main groups which show more than 90% homology of amino acid sequence. Firtel (1981) referred to the actin of smooth ... More on the omim web site
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 102540 was added.