Signal recognition particle subunit SRP72 (SRP72)
The protein contains 671 amino acids for an estimated molecular weight of 74606 Da.
Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- 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 |
|---|---|
| BMFS1 |
Cellular Component
Cytosol
Endoplasmic reticulum
Signal recognition particle
Signal recognition particle, endoplasmic reticulum targeting
Molecular Function
7S RNA binding
RNA binding
Signal recognition particle binding
TPR domain binding
The reference OMIM entry for this protein is 602122
Signal recognition particle, 72-kd; srp72
DESCRIPTION
The SRP72 gene encodes the 72-kD subunit of the signal recognition particle (SRP), 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 (600707), SRP14 (600708), SRP19 (182175), SRP54 (604857), SRP68 (604858), and SRP72. 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 Lutcke et al., 1993).CLONING
By screening a canine kidney cell line with anti-SRP72, Lutcke et al. (1993) isolated an SPR72 cDNA encoding a 671-amino acid protein. The C-terminal portion of the protein gives it an overall basic character. By screening autoimmune patient sera for the ability to precipitate phosphoproteins from apoptotic Jurkat cell lysates, Utz et al. (1998) serendipitously identified sera that precipitated SRP72 in untreated but not in apoptotic cells. The human SRP72 gene also encodes a 671-amino acid protein. SDS-PAGE and Western blot analyses showed that the 6-kD C terminus is cleaved during apoptosis by caspases and is selectively phosphorylated on serine residues. For information on a signal recognition particle database, see Larsen et al. (1998).BIOCHEMICAL FEATURES
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, Breen and Ashcroft (1997) mapped the SRP72 gene to chromosome 18. However, Gross (2012) mapped the SRP72 gene to chromosome 4q12 based on an alignment of the SRP72 sequence (GenBank GENBANK AF038851) with the genomic sequence (GRCh37).OTHER FEATURES
Breen and Ashcroft (1997) cloned and sequenced a cDNA consisting of 5-prime sequence from the human gamma calcium/calmodulin-dependent protein kinase II (CAMKG; 602123) joined to the 3-prime end of the human signal recognition particle-72 (SRP72). The 3-prime end of this novel cDNA contains 804 basepairs of human SRP72 sequence that encode the last 6 codons and 3-prime untranslated portion of the clone. Since SRP72 and CAMKG map to different chromosomes, the authors suggest that this may represent the first example of trans-splicing producing a potentially functional protein in normal adult tissue.MOLECULAR GENETICS
By whole-exome sequencing, Kirwan et al. (2012) identified a heterozygous truncating mutation in the SRP72 gene (602122.0001) in 4 affected members of a family with autosomal dominant bone marrow failure syndrome (BMFS1; 614675). The mother had myelodysplasia, and 3 children, aged 11 to 14 years, had aplastic anemia or pancytopenia. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 602122 was added.
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).