Calmodulin-3 (CALM3)
The protein contains 149 amino acids for an estimated molecular weight of 16838 Da.
Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Is a regulator of voltage-dependent L-type calcium channels (PubMed:31454269). Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. (updated: Oct. 7, 2020)
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.
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No binding partner found
Biological Process
Activation of adenylate cyclase activity
Calcium-mediated signaling
Detection of calcium ion
Establishment of protein localization to mitochondrial membrane
G protein-coupled receptor signaling pathway
G2/M transition of mitotic cell cycle
Microtubule cytoskeleton organization
Negative regulation of high voltage-gated calcium channel activity
Negative regulation of peptidyl-threonine phosphorylation
Negative regulation of ryanodine-sensitive calcium-release channel activity
Obsolete positive regulation by host of symbiont cAMP-mediated signal transduction
Positive regulation of cyclic-nucleotide phosphodiesterase activity
Positive regulation of DNA binding
Positive regulation of nitric-oxide synthase activity
Positive regulation of peptidyl-threonine phosphorylation
Positive regulation of phosphoprotein phosphatase activity
Positive regulation of protein autophosphorylation
Positive regulation of protein dephosphorylation
Positive regulation of protein serine/threonine kinase activity
Positive regulation of ryanodine-sensitive calcium-release channel activity
Regulation of cardiac muscle cell action potential
Regulation of cardiac muscle contraction
Regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
Regulation of cell communication by electrical coupling involved in cardiac conduction
Regulation of cytokinesis
Regulation of heart rate
Regulation of high voltage-gated calcium channel activity
Regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
Regulation of synaptic vesicle endocytosis
Regulation of synaptic vesicle exocytosis
Response to amphetamine
Response to calcium ion
Response to corticosterone
Substantia nigra development
Cellular Component
Calcium channel complex
Catalytic complex
Centrosome
Cytoplasm
Growth cone
Mitochondrial membrane
Myelin sheath
Nucleus
Obsolete cell
Plasma membrane
Protein-containing complex
Sarcomere
Spindle microtubule
Spindle pole
Synaptic vesicle membrane
Vesicle
Voltage-gated potassium channel complex
Molecular Function
Adenylate cyclase activator activity
Adenylate cyclase binding
Calcium ion binding
Calcium-dependent protein binding
Disordered domain specific binding
Enzyme regulator activity
Ion channel binding
N-terminal myristoylation domain binding
Nitric-oxide synthase binding
Nitric-oxide synthase regulator activity
Phosphatidylinositol 3-kinase binding
Protein domain specific binding
Protein kinase binding
Protein phosphatase activator activity
Protein serine/threonine kinase activator activity
Titin binding
Type 3 metabotropic glutamate receptor binding
The reference OMIM entry for this protein is 114183
Calmodulin 3; calm3
Phkd3
CLONING
Fischer et al. (1988) cloned CALM3 from human brain and teratoma cDNA libraries. CALM3 is identical in amino acid sequence to CALM1 (114180) and CALM2 (114182), but within the coding regions, CALM3 shares only 82% and 81% nucleotide identity with CALM1 and CALM2, respectively. The untranslated regions contain no significant homologies. Using an N-terminal sequence to probe a Northern blot, Fischer et al. (1988) detected 0.8- and 2.3-kb transcripts in fibroblast, erythroleukemia, and teratoma cell lines. Only the 2.3-kb transcript was revealed with a C-terminal probe, suggesting use of an alternate polyadenylation signal. Toutenhoofd et al. (1998) measured the mRNA abundance and transcriptional activity of the 3 CALM genes in proliferating human teratoma cells. All 5 possible mRNA transcripts were detected in these cells, with highest abundance of CALM3. CALM3 was 5-fold more actively transcribed than CALM1 and CALM2.GENE STRUCTURE
Fischer et al. (1988) determined that the CALM3 gene contains 6 exons. Koller and Strehler (1993) determined that the 5-prime flanking region of CALM3 is GC rich and contains a canonical CAAT box but no TATA box. There are several clustered SP1 (189906)-binding sites and 7 AGGA elements, which are found in genes encoding Ca(2+)-binding proteins. Using a promoter-reporter construct transfected into several cell lines, Koller and Strehler (1993) found that CALM3 promoter activity was neither cell type nor species specific.MAPPING
McPherson et al. (1991) assigned the CALM3 gene to chromosome 19 by study of somatic cell hybrids. By PCR-based amplification of CALM3-specific sequences using DNA from human/hamster cell hybrids as template, Berchtold et al. (1993) confirmed the assignment to chromosome 19 and regionalized the gene to 19q13.2-q13.3 by in situ hybridization. ... More on the omim web site
Oct. 20, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 114183 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).