Septin-7 (SEPT7)
The protein contains 437 amino acids for an estimated molecular weight of 50680 Da.
Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (PubMed:25588830). (updated: July 3, 2019)
Protein identification was indicated in the following studies:
- 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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No binding partner found
Biological Process
Cell differentiation
Cellular protein localization
Cilium assembly
Cytoskeleton-dependent cytokinesis
Positive regulation of non-motile cilium assembly
Regulation of embryonic cell shape
Spermatogenesis
The reference OMIM entry for this protein is 603151
Septin 7; sept7
Cell division cycle 10; cdc10
CLONING
The Saccharomyces cerevisiae CDC10 protein is a structural component of the 10-nm filament which lies inside the cytoplasmic membrane and is essential for budding. Nakatsuru et al. (1994) cloned a novel human gene whose predicted 418-amino acid product shared 39% and 54% sequence identity with yeast CDC10 and mouse H5 proteins, respectively. The human CDC10 protein contains a conserved GTP-binding domain. Northern blot analysis revealed a 2.4-kb mRNA that was expressed in all human tissues tested.GENE FUNCTION
Low and Macara (2006) noted that specific combinations of septins can heterooligomerize and form filaments in vitro and in vivo. Using fluorescence resonance energy transfer, size exclusion chromatography, and multiangle light scattering analyses, they characterized the complex formed by SEPT2 (601506), SEPT6 (300683), and SEPT7. SEPT6 and SEPT7 interacted through a parallel coiled-coil domain, and SEPT2 interacted with SEPT6 through its C-terminal coiled-coil domain. Kremer et al. (2007) showed that knockdown of SEPT2, SEPT6, and SEPT7 in HeLa cells caused actin stress fibers to disintegrate and cells to lose polarity. They found that these septins acted through SOCS7 (608788) to restrict nuclear accumulation of NCK (NCK1; 600508). In the absence of septin filaments, SOCS7 recruited NCK into the nucleus. Moreover, depletion of NCK from the cytoplasm triggered dissolution of actin stress fibers and loss of cell polarity. Kremer et al. (2007) also showed that the association between septins, SOCS7, and NCK played a role in the DNA damage checkpoint response. NCK entered the nucleus following DNA damage and was required for ultraviolet (UV)-induced cell cycle arrest. Furthermore, nuclear NCK was essential for activation of p53 (TP53; 191170) in response to UV-induced DNA damage. Kremer et al. (2007) concluded that septins, SOCS7, and NCK are part of a signaling pathway that couples regulation of the DNA damage response to the cytoskeleton. Nagata et al. (2004) coprecipitated Sept11 (612887) with a septin complex that included Sept2, Sept7, Sept8 (608418), and Sept9b (see SEPT9, 604061) from a rat fibroblast cell line, and examined the interaction of Sept11 with Sept7 and Sept9b. They found that the C-terminal coiled-coil regions of Sept7 and Sept11 interact with each other, and that these coiled-coil regions interact with the N-terminal variable region of Sept9b. Sept7, Sept9b, and Sept11 formed thin filaments when expressed alone in COS-7 cells. Coexpression of Sept11 with Sept7 disrupted the filaments formed by each component alone, although Sept7 and Sept11 colocalized despite filament disruption. Conversely, coexpression of Sept11 and Sept9b increased filament bundling compared with filaments formed by each component alone. Nagata et al. (2004) concluded that the filaments formed by individual septins are affected by other septins in the filament complex. Kim et al. (2010) identified control of septin localization by the planar cell polarity (PCP) protein Fritz (613580) as a crucial control point for both collective cell movement and ciliogenesis in Xenopus embryos. Sept2 and Sept7 were expressed strongly in cells during convergent extension, and morpholino-mediated knockdown of either resulted in defective gastrulation. Cells in septin morphants displayed reduced cell elongation but normal polarization, similar to Fritz morphants. Data suggested that septins and Fritz collaborate during PCP-mediat ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 603151 was added.
July 4, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).