Coronin-7 (CORO7)
The protein contains 925 amino acids for an estimated molecular weight of 100605 Da.
F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post-Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology. (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.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs17137007 | |
| dbSNP:rs3747579 | |
| dbSNP:rs35357594 | |
| dbSNP:rs9928967 |
Biological Process
Actin filament organization
Actin filament polymerization
Golgi to endosome transport
Protein transport
The reference OMIM entry for this protein is 611668
Coronin 7; coro7
Polarity-osmotic defective 1, drosophila, homolog of; pod1
Crn7
DESCRIPTION
Coronins, such as CORO7, constitute an evolutionarily conserved family of WD-repeat actin-binding proteins. CORO7 plays a role in Golgi complex morphology and function (Rybakin et al., 2004, 2006).CLONING
By EST database analysis, followed by RT-PCR of human liver carcinoma cDNA, Rybakin et al. (2004) cloned CORO7, which they called CRN7. The deduced 924-amino acid protein has a calculated molecular mass of 100.5 kD, which was confirmed experimentally. CORO7 contains 2 coronin WD repeat-containing domains with a proline-, serine-, and threonine-enriched region (PST motif) preceding the second WD-repeat. CORO7 shares 30% and 29% amino acid identity with Drosophila Pod1 and C. elegans Pod1, respectively. Northern blot analysis detected expression in mouse embryos as early as day 5 postcoitum and expression increased through day 15. Coro7 expression was detected in most mouse tissues examined with high levels in brain, thymus, and kidney and low levels in heart, liver, testis, and muscle. Western blot analysis of mouse tissues showed a similar distribution of Coro7 with low expression in skeletal and heart muscle. Immunofluorescence studies detected developmental expression of mouse Coro7 in embryonic brain, thymus, intestine, skin, and eye. Indirect immunofluorescence studies detected Coro7 in vesicle-like structures and in a Golgi-like perinuclear compartment in mouse fibroblasts. Sucrose gradient centrifugation and immunoprecipitation studies demonstrated that Coro7 localized to cytosolic vesicles and to the cis-Golgi region. The membrane-associated form of Coro7 was tyrosine-phosphorylated, whereas the cytosolic form was not.GENE FUNCTION
By electron microscopy, Rybakin et al. (2006) showed that siRNA knockdown of CORO7 in HeLa cells caused loss of Golgi integrity and membrane scattering. CORO7 knockdown caused a defect in Golgi export of vesicular stomatitis virus glycoprotein (VSVG) but did not alter protein import into the trans-Golgi network. Golgi cargo glycosylation was not affected. Using in vitro binding, coimmunoprecipitation, and colocalization studies, the authors demonstrated that CORO7 interacted with clathrin adaptor AP1 (see 600157) and that this interaction takes place at Golgi membranes. Rybakin et al. (2006) showed that CORO7 was not required for AP1 targeting to Golgi membranes and suggested that CORO7 acts downstream of AP1 recruitment.MAPPING
Gross (2015) mapped the CORO7 gene to chromosome 16p13.3 based on an alignment of the CORO7 sequence (GenBank GENBANK BC117289) with the genomic sequence (GRCh38). ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 611668 was added.