Protein S100-A6 (S100A6)
The protein contains 90 amino acids for an estimated molecular weight of 10180 Da.
May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- 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.
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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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| Variant | Description |
|---|---|
| dbSNP:rs11974 | |
| dbSNP:rs1802581 | |
| dbSNP:rs1802582 | |
| dbSNP:rs2228293 |
The reference OMIM entry for this protein is 114110
S100 calcium-binding protein a6; s100a6
Calcyclin; cacy
DESCRIPTION
S100 proteins, such as S100A6, are small, acidic Ca(2+)-binding proteins that transduce Ca(2+)-signals via interaction with intracellular target proteins (Mandinova et al., 1998).CLONING
Ferrari et al. (1987) noted that S100A6, which they called calcyclin, was originally defined as a cDNA clone (2A9) whose cognate RNA was found to be growth-regulated and whose sequence showed strong similarities to that of the S100 protein (see S100A1; 176940) and to a subunit of the major cellular substrate for tyrosine kinase. Using Northern blot analysis, Engelkamp et al. (1992) found ubiquitous expression of a CACY transcript of about 550 bp. Highest expression was detected in kidney, lung, and thymus. Using immunofluorescence analysis and confocal laser scanning microscopy, Mandinova et al. (1998) showed that S100A1, S100A2 (176993), S100A4 (114210), and S100A6 localized to distinct intracellular compartments in cultured human vascular and intestinal smooth muscle cells. S100A6 localized predominantly with the sarcoplasmic reticulum.GENE FUNCTION
Mandinova et al. (1998) showed that elevated cytosolic Ca(2+) led to relocalization of S100A1, S100A4, and S100A6 from sarcoplasmic reticulum to vesicle-like structures around the nucleus in human vascular smooth muscle cells.GENE STRUCTURE
Using a full-length cDNA, Ferrari et al. (1987) isolated the entire calcyclin gene plus extensive flanking sequences. They found that the calcyclin gene is present in single copy and has 3 exons. The 5-prime flanking sequence contains a TATA box, GC boxes, and a sequence with a strong homology to the enhancer core of the SV40 promoter. Other enhancer-like elements are scattered in both the 5-prime and 3-prime flanking regions.MAPPING
By in situ hybridization, Ferrari et al. (1987) determined that the CACY gene maps to chromosome 1q21-q25. Using cDNA probes for CACY, van Heyningen et al. (1989) and Dorin et al. (1990) showed that the CACY gene cosegregates with CAGA (S100A8; 123885) and CAGB (S100A9; 123886), which are located on chromosome 1q12-q21. In the course of constructing a physical map of human 1q21-q23, Oakey et al. (1992) determined that the CACY gene is located at the centromeric end of that segment, proximal to SPTA1 (182860). Schafer et al. (1995) isolated a YAC from chromosome 1q21 on which 9 different genes coding for S100 calcium-binding proteins could be localized. The clustered organization of S100 genes allowed introduction of a new logical nomenclature based on their physical arrangement on the chromosome with S100A1 being closest to the telomere and S100A9 being closest to the centromere. In the new nomenclature, CACY became S100A6. By linkage studies of interspecific backcrosses of Mus spretus and Mus musculus domesticus, Seldin (1989) demonstrated that the Cacy gene is located on mouse chromosome 3. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 114110 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed