Endoplasmic reticulum resident protein 29 (ERP29)
The protein contains 261 amino acids for an estimated molecular weight of 28993 Da.
Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. (updated: April 1, 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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
- 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
Activation of MAPK activity
Intracellular protein transport
Negative regulation of gene expression
Negative regulation of protein secretion
Positive regulation of gene expression
Positive regulation of protein phosphorylation
Protein folding
Protein phosphopantetheinylation
Protein secretion
Protein unfolding
Regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
The reference OMIM entry for this protein is 602287
Endoplasmic reticulum protein, 29-kd; erp29
Chromosome 12 open reading frame 8; c12orf8
Erp29
Erp28
CLONING
Reticuloplasmins are proteins found in the lumen of the endoplasmic reticulum (ER). Demmer et al. (1997) cloned ERp29, a 29-kD reticuloplasmin, from rat enamel cells by microsequencing of the purified protein followed by RT-PCR. ERp29 has the N-terminal hydrophobic signal sequence and C-terminal endoplasmic reticulum retention motif (KEEL) characteristic of reticuloplasmins, but lacks calcium-binding motifs. Northern blot analysis showed that ERp29 is widely expressed in rat tissues. A homologous transcript was expressed in human hepatoma cells. Ferrari et al. (1998) cloned ERP29, which they designated ERP28, from a human liver cDNA library. The deduced 229-amino acid protein has a calculated molecular mass of 24.8 kD and contains the KEEL ER retention signal. The purified protein migrates as a dimer under nondenaturing conditions and as a 28-kD monomer by SDS-PAGE. The same apparent masses are seen with recombinant protein and protein purified from human hepatocellular carcinoma cells or from bovine liver, indicating lack of glycosylation. Ferrari et al. (1998) found that ERP29 shares 92% sequence identity with the rat homolog. It shows low but significant similarity with members of the protein disulfide isomerase family (see 176790), but does not contain a reactive thioredoxin-box motif. Immunofluorescence and subcellular fractionation studies showed colocalization of ERP29 with calreticulin (109091) in the ER.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ERP29 gene to chromosome 12 (TMAP SGC31784). ... 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
Nov. 23, 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 602287 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed