Signal recognition particle 14 kDa protein (SRP14)
The protein contains 136 amino acids for an estimated molecular weight of 14570 Da.
Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding. (updated: March 4, 2015)
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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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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| Variant | Description |
|---|---|
| dbSNP:rs1802601 | |
| dbSNP:rs1802600 | |
| dbSNP:rs7535 | |
| dbSNP:rs200831083 | |
| dbSNP:rs16924521 | |
| dbSNP:rs4814 |
Biological Process
Cellular protein metabolic process
Cotranslational protein targeting to membrane
Gene expression
Neutrophil degranulation
Protein targeting to ER
Response to drug
SRP-dependent cotranslational protein targeting to membrane
Translation
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Extracellular region
Ficolin-1-rich granule lumen
Intercellular bridge
Nucleolus
Nucleus
Secretory granule lumen
Signal recognition particle, endoplasmic reticulum targeting
Molecular Function
7S RNA binding
Endoplasmic reticulum signal peptide binding
Poly(A) RNA binding
RNA binding
The reference OMIM entry for this protein is 600708
Signal recognition particle, 14-kd; srp14
Alu rna-binding protein, 14-kd subunit; alurbp
CLONING
Together with SRP9 (600707), SRP14 forms a complex that recognizes Alu RNA and the related 7SL RNA. Chang et al. (1994) cloned the SRP14 cDNA by PCR with primers based on partial protein sequences obtained from tryptic peptides and the previously identified mouse nucleotide sequence. The predicted amino acid sequence was found to be approximately 90% similar to the mouse homolog. The human sequence is longer at the C terminus and the predicted protein is 18 kD rather than 14 kD.GENE FAMILY
The signal recognition particle (SRP) is a ribonucleoprotein complex that mediates the targeting of proteins to the endoplasmic reticulum (ER). The complex consists of a 7S (or 7SL) RNA and 6 different proteins, SRP9, SRP14, SRP19 (182175), SRP54 (604857), SRP68 (604858), and SRP72 (602122). The proteins are bound to the 7S RNA as monomers (SRP19 and SRP54) or heterodimers (SRP9/SRP14 and SRP68/SRP72). SRP9 and SRP14 constitute the Alu domain of 7S, whereas the other 4 proteins belong to the S domain. SRP has at least 3 distinct functions that can be associated with the protein subunits: signal recognition, translational arrest, and ER membrane targeting by interaction with the docking protein (summary by Lingelbach et al., 1988). For information on a signal recognition particle database, see Larsen et al. (1998).BIOCHEMICAL FEATURES
- Crystal Structure Weichenrieder et al. (2000) reported 2 crystal structures of the heterodimer SRP9/14 bound either to the 5-prime domain or to a construct containing both 5-prime and 3-prime domains of the SRP RNA. - Cryoelectron Microscopy Halic et al. (2004) presented the structure of a targeting complex consisting of mammalian SRP bound to an active 80S ribosome carrying a signal sequence. This structure, determined to 12-angstrom resolution by cryoelectron microscopy, enabled Halic et al. (2004) to generate a molecular model of SRP in its functional conformation. The model showed how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation factor-binding site of the ribosome, explaining its elongation arrest activity.MAPPING
By somatic cell hybrid analysis, Chang et al. (1994) mapped the SRP14 gene to human chromosome 15q22. ... More on the omim web site
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 600708 was added.