Destrin (DSTN)
The protein contains 165 amino acids for an estimated molecular weight of 18506 Da.
Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner. (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.
- 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.
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| Variant | Description |
|---|---|
| a colorectal cancer sample; somatic mutation |
The reference OMIM entry for this protein is 609114
Destrin; dstn
Actin depolymerizing factor; adf
DESCRIPTION
Destrin is an essential actin regulatory protein belonging to the actin-depolymerizing factor (ADF)/cofilin family (see 601442). This family of proteins is responsible for enhancing the turnover rate of actin in vivo.CLONING
ADF was first isolated from chick embryo brains as a protein that promoted the disassembly of actin filaments (Bamburg et al., 1980). Hawkins et al. (1993) cloned human ADF from an embryonic brain cDNA library. They found that the deduced 165-amino acid protein is 100% and 95% identical to porcine destrin (Moriyama et al., 1990) chick ADF, respectively.GENE FUNCTION
Hawkins et al. (1993) showed that human destrin expressed in E. coli behaved like native destrin from porcine brain. It bound to G-actin at pH 8, thereby sequestering monomers and preventing polymerization. It did not cosediment with F-actin at this pH, but severed actin filaments in a calcium-insensitive manner. By contrast, at pH values below 7, destrin bound to actin filaments in a highly cooperative manner and at a 1:1 ratio to filament subunits. When the pH was raised to 8.0, the decorated filaments were rapidly severed and depolymerized.MAPPING
Deloukas et al. (2001) assembled a physical map of human chromosome 20 and annotated 727 genes, one of which was destrin.ANIMAL MODEL
Corneal disease-1 (corn1) and corn1(2J) are spontaneous mouse mutants that develop irregular thickening of the corneal epithelium, similar to that observed in human corneal surface disease. These autosomal recessive mutations cause an increase in the rate of proliferation of the corneal epithelial cells. Ikeda et al. (2003) reported that the phenotypes in both mutants are caused by mutations in the destrin gene. By positional cloning, they identified a deletion encompassing the entire coding sequence of the destrin gene in corn1 mice and a point mutation, pro106 to ser (P106S), in corn1(2J) mice. In situ analysis showed that destrin was highly expressed in the corneal epithelium. The corn1 mutations increased the content of filamentous actin in corneal epithelial cells. Ikeda et al. (2003) suggested that there is an in vivo connection between remodeling of the actin cytoskeleton and the control of cell proliferation, at least in the corneal epithelium. ... 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
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 609114 was added.