Reticulon-1 (RTN1)
The protein contains 776 amino acids for an estimated molecular weight of 83618 Da.
Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity. (updated: Feb. 10, 2021)
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.
- 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.
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.
This protein is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs35645652 | |
| dbSNP:rs35707243 |
Cellular Component
Endoplasmic reticulum
Endoplasmic reticulum membrane
Golgi membrane
Integral component of endoplasmic reticulum membrane
Molecular Function
The reference OMIM entry for this protein is 600865
Reticulon 1; rtn1
Neuroendocrine-specific protein; nsp
CLONING
Roebroek et al. (1993) described the cloning of a gene, which they designated NSP, that encodes several neuroendocrine-specific proteins. The original cDNA was identified by screening an expression library of the small-cell lung cancer (SCLC) NCI-H82 cell line with antibodies to the previously identified proteins. The gene can produce 3 different transcripts (3.4, 2.3, and 1.8 kb), which are identical at their 3-prime ends but have unique amino termini. The common carboxyl-terminal region contains 2 large hydrophobic domains. The largest cDNA (NSP-A) produces a 135-kD (776-amino acid) protein which is rich in proline and serine residues and contains multiple potential phosphorylation sites. NSP-B and NSP-C have predicted reading frames of 356 and 208 amino acids, respectively. The B transcript was found only in the NCI-H82 cell line. NSP-specific antibodies showed that the proteins are localized to membranes of the endoplasmic reticulum (Senden et al., 1994), leading to their proposed designation as 'reticulons.' Immunohistochemical studies in the rat (van de Velde et al., 1994) showed the presence of NSP-A protein in many regions of the brain. NSP-A or -C transcripts were found in 18 different SCLC lines but not in any of 11 nonendocrine non-SCLCs (van de Velde et al., 1994).GENE STRUCTURE
Roebroek et al. (1996) found that the NSP exons are dispersed over a genomic region of about 275 kb. The genomic organization explained the generation of NSP mRNA variants encoding NSP protein isoforms. Multiple promoters rather than alternative splicing of internal exons seemed to be involved in this diversity. Comparison of NSP genomic and cDNA sequences with databank nucleotide sequences resulted in the discovery of other human members of this novel family of reticulon encoding genes. Mannan et al. (2006) noted that RTN1 has 9 exons spanning approximately 295 kb.MAPPING
Kools et al. (1994) mapped the human NSP gene to chromosome 14q21-q22 by fluorescence in situ hybridization. Mannan et al. (2006) stated that the RTN1 gene maps to chromosome 14q23.1.GENE FUNCTION
By yeast 2-hybrid analysis and coimmunoprecipitation studies in mouse fibroblast cells (NIH3T3) and HeLa cells, Mannan et al. (2006) demonstrated that reticulon-1 interacts with spastin (SPAST; 604277), which is mutated in hereditary spastic paraplegia-4 (SPG4; 182601). The interaction is mediated through the spastin N-terminal region, which contains a microtubule-interacting and trafficking domain. Intracellular distribution studies showed colocalization of the 2 proteins in discrete cytoplasmic vesicles. The findings strengthened the hypothesis that disruption of intracellular vesicular transport processes may underlie spastic paraplegia. Mannan et al. (2006) failed to identify mutations in the coding or flanking intronic sequences of the RTN1 gene in 2 index patients from families with SPG15 (270700), which had been mapped to chromosome 14q. ... More on the omim web site
Feb. 16, 2021: 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 16, 2016: Protein entry updated
Automatic update: OMIM entry 600865 was added.