Septin-8 (SEPT8)
The protein contains 483 amino acids for an estimated molecular weight of 55756 Da.
Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion (PubMed:15116257). Seems to participate in the process of SNARE complex formation in synaptic vesicles (By similarity).', 'Stabilizes BACE1 protein levels and promotes the sorting and accumulation of BACE1 to the recycling or endosomal compartments, modulating the beta-amyloidogenic processing of APP. (updated: Dec. 11, 2019)
Protein identification was indicated in the following studies:
- 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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Biological Process
Cell cycle
Cellular protein localization
Cilium assembly
Cytoskeleton-dependent cytokinesis
Mitotic cytokinesis
Regulation of intracellular protein transport
Regulation of protein stability
Regulation of SNARE complex assembly
Septin ring assembly
The reference OMIM entry for this protein is 608418
Septin 8; sept8
Kiaa0202
DESCRIPTION
SEPT8 is a member of the highly conserved septin family. Septins are 40- to 60-kD GTPases that assemble as filamentous scaffolds. They are involved in the organization of submembranous structures, in neuronal polarity, and in vesicle trafficking (Blaser et al., 2003).CLONING
By sequencing clones obtained from an immature myeloid cell line cDNA library, Nagase et al. (1996) cloned SEPT8, which they designated KIAA0202. The deduced 508-amino acid protein contains an ATP/GTP-binding site motif A (P loop). Northern blot analysis detected expression in all tissues and cell lines examined except peripheral blood leukocytes. Highest expression was in kidney. Using CDCREL1 (602724) as bait in a yeast 2-hybrid screen, Blaser et al. (2002) cloned SEPT8 from fetal brain and adult heart cDNA libraries. Northern blot analysis detected transcripts of 4.4, 2.8, and 2.2 kb. Blaser et al. (2003) characterized 4 SEPT8 transcripts obtained by screening an acute megakaryoblastic leukemia cell cDNA library, an endothelial cell cDNA library, and a fetal brain cDNA library. Three transcripts (variants 1 through 3) arise by alternative splicing, while the fourth transcript utilizes an alternative polyadenylation signal but has an open reading frame identical to that of variant 1. Variant 1 encodes a deduced 508-amino acid protein, variant 2 encodes a deduced 562-amino acid protein, and variant 3 encodes a deduced 453-amino acid protein. A conserved region found in all 3 variants contains the GTP-binding motif and is encoded by exons 3 through 10. Northern blot analysis detected expression of most SEPT8 variants in all brain and cardiovascular regions tested, as well as in prostate, testis, and ovary. Expression was highest in brain and aorta, and expression of each variant was tissue specific. Western blot analysis detected variant 1 at an apparent molecular mass of 58 kD in prostate, testis, and ovary.GENE FUNCTION
Using several protein interaction assays, Blaser et al. (2002) confirmed that CDCREL1 interacted with SEPT8 in cells expressing both proteins. They also observed a strong correlation between the presence of CDCREL1 and SEPT8 transcripts and proteins in brain, heart, and platelets.GENE STRUCTURE
Wenderfer et al. (2000) determined that the SEPT8 gene, which they called SEPL, contains 10 exons and spans at least 21 kb. The mouse Sept8 gene also contains 10 exons. Blaser et al. (2003) determined that the SEPT8 gene contains 12 exons and spans more than 27 kb.MAPPING
By genomic sequence analysis, Wenderfer et al. (2000) mapped the SEPT8 gene to chromosome 5q31-q33. They mapped the mouse Sept8 gene to a region of chromosome 11 that shows homology of synteny to human chromosome 5q31-q33. ... More on the omim web site
Jan. 22, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Dec. 9, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for SEPT8
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 608418 was added.