Transmembrane emp24 domain-containing protein 1 (TMED1)
The protein contains 227 amino acids for an estimated molecular weight of 25206 Da.
Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side. (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.
- 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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| a breast cancer sample; somatic mutation |
No binding partner found
Biological Process
Cell-cell signaling
Endoplasmic reticulum to Golgi vesicle-mediated transport
Golgi organization
Intracellular protein transport
Protein transport
Signal transduction
Cellular Component
COPII-coated ER to Golgi transport vesicle
Endoplasmic reticulum
Endoplasmic reticulum membrane
Endoplasmic reticulum-Golgi intermediate compartment
Endoplasmic reticulum-Golgi intermediate compartment membrane
Golgi apparatus
Integral component of membrane
Intracellular membrane-bounded organelle
Plasma membrane
The reference OMIM entry for this protein is 605395
Transmembrane emp24 transport domain-containing protein 1; tmed1
Interleukin 1 receptor-like 1 ligand; il1rl1lg
Il1rl1-binding protein
CLONING
The T1/ST2 receptor, also called IL1RL1 (601203), is a member of the interleukin-1 receptor family. Gayle et al. (1996) determined that none of the 3 interleukin-1 species (IL1A (147760), IL1B (147720), or IL1RA (IL1RN; 147679)) binds to IL1RL1. By flow cytometry, they found that several cell lines bind specifically to IL1RL1. Using expression cloning, Gayle et al. (1996) isolated a cDNA encoding IL1RL1 ligand, or IL1RL1LG. Sequence analysis predicted that the 227-amino acid, type I transmembrane protein, which lacks any similarity to any of the IL1 types, contains a 170-amino acid extracellular region between the signal peptide and the transmembrane domain as well as a 12-amino acid cytoplasmic tail. Northern blot analysis detected wide expression of a 1.5-kb transcript. Functional analysis failed to show that the interaction of IL1RL1LG and IL1RL1 leads to the activation of DNA binding by nuclear factor kappa-B (NFKB; 164011) or transcription from the IL8 (146930) promoter. The authors concluded that other proteins must interact with IL1RL1 in order for these functions to occur.MAPPING
Using FISH, Gayle et al. (1996) mapped the IL1RL1LG gene to 19p13.2. ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605395 was added.