Immediate early response 3-interacting protein 1 (IER3IP1)
The protein contains 82 amino acids for an estimated molecular weight of 8969 Da.
Regulator of endoplasmic reticulum secretion that acts as a key determinant of brain size (PubMed:33122427). Required for secretion of extracellular matrix proteins (PubMed:33122427). Required for correct brain development by depositing sufficient extracellular matrix proteins for tissue integrity and the proliferation of neural progenitors (PubMed:33122427). Acts as a regulator of the unfolded protein response (UPR) (By similarity). (updated: April 7, 2021)
Protein identification was indicated in the following studies:
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
This protein is predicted to be membranous by TOPCONS.
Biological Process
Brain development
Endoplasmic reticulum to Golgi vesicle-mediated transport
Organ growth
Positive regulation of extracellular matrix constituent secretion
Positive regulation of protein secretion
Protein transport
Regulation of fibroblast apoptotic process
Cellular Component
COPII-coated ER to Golgi transport vesicle
Endoplasmic reticulum
Endoplasmic reticulum membrane
Golgi apparatus
Integral component of Golgi membrane
Membrane
Molecular Function
The reference OMIM entry for this protein is 609382
Immediate-early response 3-interacting protein 1; ier3ip1
CLONING
By large-scale partial sequencing of a human liver cDNA library and EST database searching, Yiu et al. (2004) identified a novel cDNA encoding a deduced 82-amino acid protein, which they designated immediate-early response-3-interacting protein-1 (IER3IP1). IER3IP1 contains a putative G-patch domain and 2 transmembrane domains. Northern blot analysis revealed a single 1.5-kb transcript expressed at high levels in heart, skeletal muscle, and kidney, moderate levels in liver and brain, and low levels in placenta, lung, and peripheral blood leukocytes. Yiu et al. (2004) found that the IER3IP1 protein localizes to the endoplasmic reticulum through its C-terminal transmembrane domain.GENE STRUCTURE
Yiu et al. (2004) demonstrated that the IER3IP1 gene contains 3 exons.MAPPING
By somatic cell hybrid analysis, Yiu et al. (2004) mapped the IER3IP1 gene to chromosome 18. They refined the mapping to 18q12 by radiation hybrid analysis.GENE FUNCTION
In cultured fibroblasts, Poulton et al. (2011) demonstrated that expression of IER3IP1 was increased approximately 1.5-fold by TNF-alpha (191160).MOLECULAR GENETICS
By homozygosity mapping followed by candidate gene sequencing in 2 consanguineous families with microcephaly, epilepsy, and diabetes syndrome (MEDS; 614231), Poulton et al. (2011) identified different homozygous mutations in the IER3IP1 gene: V21G (609382.0001) and L78P (609382.0002). Poulton et al. (2011) concluded that the disorder was due to abnormally increased apoptosis. In 4 patients from 2 unrelated consanguineous Egyptian families with MEDS, Abdel-Salam et al. (2012) identified homozygosity for the L78P mutation in the IER3IP1 gene. The mutation, which was found by whole-exome sequencing, segregated with the disorder in the families. Functional studies of the variant were not performed. In a boy with MEDS, Shalev et al. (2014) identified compound heterozygous mutations in the IER3IP1 gene: V21G and c.79delT (609382.0003). The mutations, which were found by whole-exome sequencing, segregated with the disorder in the family. The V21G mutation was inherited from the unaffected father, who was of mixed Libyan-Tangier origin, whereas the c.79delT mutation was inherited from the unaffected mother, who was of mixed Ashkenazi Jewish/Spanish/French origin. Functional studies of the variants were not performed. ... More on the omim web site
April 10, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 609382 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).