Signal peptidase complex subunit 1 (SPCS1)
The protein contains 102 amino acids for an estimated molecular weight of 11805 Da.
Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum.', '(Microbial infection) Required for the post-translational processing of proteins involved in virion assembly and secretion from flaviviruses such as West Nile virus (WNV), Japanese encephalitis virus (JEV), Dengue virus type 2 (DENV-2), Yellow Fever virus (YFV), Zika virus (ZIKV) and hepatitis C virus (HCV) (PubMed:24009510, PubMed:27383988, PubMed:29593046). Plays a key role in the post-translational processing of flaviviral structural proteins prM, E, and NS1 (PubMed:27383988, PubMed:29593046). In HCV, it is involved in virion assembly where it promotes the interaction between HCV virus proteins NS2 and E2 (PubMed:24009510). (updated: Oct. 16, 2019)
Protein identification was indicated in the following studies:
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.
(right-click above to access to more options from the contextual menu)
No binding partner found
Biological Process
Protein targeting to ER
Proteolysis
Signal peptide processing
Viral protein processing
Virion assembly
The reference OMIM entry for this protein is 610358
Signal peptidase complex, subunit 1, s. cerevisiae, homolog of; spcs1
Signal peptidase, 12-kd subunit; spc12
CLONING
By RT-PCR of a human fetal brain cDNA library using degenerate oligonucleotides based on canine Spcs1, Kailes and Hartmann (1996) cloned human SPCS1. The 102-amino acid protein has a predicted molecular mass of 11.8 kD. SPCS1 shows no sequence similarity to any of the other signal peptidase complex subunits. SPCS1 contains 2 predicted transmembrane domains, and immunoblot analysis of protease-digested canine microsomes showed that both the N- and C-terminal domains of Spcs1 and Spcs2 are cytoplasmic.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SPCS1 gene to chromosome 3 (TMAP RH102956). ... More on the omim web site
Oct. 27, 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. 20, 2018: Protein entry updated
Automatic update: OMIM entry 610358 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).