Septin-11 (SEPT11)
The protein contains 429 amino acids for an estimated molecular weight of 49398 Da.
Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy. (updated: Jan. 23, 2007)
Protein identification was indicated in the following studies:
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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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Biological Process
Cellular protein localization
Cilium assembly
Cytoskeleton-dependent cytokinesis
Mitotic cytokinesis
Protein heterooligomerization
Regulation of synapse organization
Septin ring assembly
The reference OMIM entry for this protein is 612887
Septin 11; sept11
DESCRIPTION
SEPT11 belongs to the conserved septin family of filament-forming cytoskeletal GTPases that are involved in a variety of cellular functions including cytokinesis and vesicle trafficking (Hanai et al., 2004; Nagata et al., 2004).CLONING
By PCR of a human brain cDNA library, Hanai et al. (2004) cloned SEPT11. The deduced 429-amino acid protein has a unique N-terminal region followed by a conserved GTPase domain and a C-terminal domain. Northern blot analysis detected SEPT11 expression in all tissues examined except leukocytes, with transcripts of 6.5, 3.0, and 2.0 kb expressed in a tissue-specific manner. Western blot analysis detected SEPT11 at an apparent molecular mass of 48 kD in rat brain and in several mammalian cell lines, including human. Endogenous SEPT11 localized to short filaments in HeLa and COS-7 cells, and SEPT11 colocalized with microtubule or actin cytoskeletal elements in other cell lines in a cell type-dependent manner.GENE FUNCTION
By mutating a critical glycine (gly48) within the G1 box of SEPT11 GTPase domain, Hanai et al. (2004) showed that GTPase activity was required for filament formation by SEPT11. SEPT11 with this mutation was able to bind GTP, but lost GTP hydrolysis activity. Nagata et al. (2004) stated that the C-terminal domain of most septins, including SEPT11, is a coiled-coil domain involved in protein-protein interaction. Nagata et al. (2004) coprecipitated Sept11 with a septin complex that included Sept2 (601506), Sept7 (603151), 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.MAPPING
Hartz (2009) mapped the SEPT11 gene to chromosome 4q21.1 based on an alignment of the SEPT11 sequence (GenBank GENBANK AL110300) with the genomic sequence (build 36.1). ... More on the omim web site
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 612887 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).