Transmembrane emp24 domain-containing protein 10 (TMED10)
The protein contains 219 amino acids for an estimated molecular weight of 24976 Da.
Cargo receptor involved in protein vesicular trafficking and quality control in the endoplasmic reticulum (ER) and Golgi (PubMed:10052452, PubMed:11726511, PubMed:16641999, PubMed:17288597, PubMed:19296914, PubMed:20427317, PubMed:21219331, PubMed:27569046). The p24 protein family is a group of transmembrane proteins that bind coat protein complex I/COPI and coat protein complex II/COPII involved in vesicular trafficking between the membranes (PubMed:10052452). Acts at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and involved in vesicle coat formation at the cytoplasmic side (PubMed:20427317, PubMed:27569046). Mainly functions in the early secretory pathway and cycles between the ER, ER-Golgi intermediate compartment (ERGIC) and Golgi, mediating cargo transport through COPI and COPII-coated vesicles (PubMed:10052452, PubMed:10852829, PubMed:12237308). In COPII vesicle-mediated anterograde transport, involved in the transport of GPI-anchored proteins by acting together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER (PubMed:20427317, PubMed:27569046). Recognizes GPI anchors structural remodeled in the ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase MPPE1/PGAP5 (By similarity). In COPI vesicle-mediated retrograde transport, involved in the biogenesis of COPI vesicles and vesicle coat recruitment (PubMed:11 (updated: Oct. 7, 2020)
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.
- 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.
- 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 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 |
|---|---|
| dbSNP:rs4929 | |
| dbSNP:rs17103066 |
Biological Process
COPI coating of Golgi vesicle
COPI-coated vesicle budding
COPII vesicle coating
Cytosol to endoplasmic reticulum transport
Cytosol to ERGIC protein transport
Endoplasmic reticulum to Golgi vesicle-mediated transport
Golgi organization
Interleukin-1 production
Intracellular protein transport
Kidney development
Negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process
Positive regulation of interleukin-1 production
Positive regulation of protein secretion
Protein complex oligomerization
Protein localization to ERGIC
Regulated exocytosis
Regulation of amyloid-beta formation
Response to alkaloid
Retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
Vesicle cargo loading
Vesicle targeting, to, from or within Golgi
Cellular Component
Cis-Golgi network
COPI-coated vesicle
COPII-coated ER to Golgi transport vesicle
Endoplasmic reticulum
Endoplasmic reticulum membrane
Endoplasmic reticulum-Golgi intermediate compartment
Endoplasmic reticulum-Golgi intermediate compartment membrane
ER to Golgi transport vesicle membrane
Extracellular exosome
Gamma-secretase complex
Golgi apparatus
Golgi membrane
Integral component of membrane
Melanosome
Obsolete cell
Plasma membrane
Secretory granule membrane
Trans-Golgi network transport vesicle
Transport vesicle
Transport vesicle membrane
Zymogen granule membrane
The reference OMIM entry for this protein is 605406
Transmembrane emp24 transport domain-containing protein 10; tmed10
Transmembrane trafficking protein, 21-kd; tmp21
CLONING
Blum et al. (1996) identified a 21-kD rat pancreatic microsomal membrane protein that they designated Tmp21. By probing a human brain cDNA library with a fragment of the rat sequence, they isolated a cDNA encoding human TMP21. The deduced 219-amino acid type I intracellular transmembrane protein contains a signal sequence and is predicted to be located in the lumen of the endoplasmic reticulum. Northern blot analysis detected a 1.4-kb TMP21 transcript. Immunoblot analysis showed that the rat Tmp21 protein is expressed predominantly in the microsomal fraction of pancreatic acinar cells. Horer et al. (1999) determined that a putative TMP21 isoform, TMP21-II, is a neutral pseudogene.MAPPING
By linkage analysis, Sherrington et al. (1995) mapped the TMP21 gene to 14q24.3.GENE FUNCTION
Chen et al. (2006) identified TMP21 as a component of presenilin complexes and differentially regulates gamma-secretase cleavage without affecting epsilon-secretase activity (see 104311). ... More on the omim web site
Oct. 20, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 605406 was added.