Recombinant Mouse Transmembrane Protein 111 (TMEM111) is a protein belonging to the family of transmembrane proteins, which are integral components of cellular membranes. These proteins play crucial roles in various cellular processes, including signaling, transport, and cell-cell interactions. Despite its importance, detailed structural and functional information about TMEM111 is limited compared to other transmembrane proteins.
Transmembrane proteins are embedded within the lipid bilayer of cell membranes and can span the membrane once or multiple times. They are involved in a wide range of biological functions, such as ion transport, cell signaling, and the recognition of extracellular ligands. The study of recombinant forms of these proteins allows researchers to explore their functions in a controlled manner.
Given the lack of detailed information on TMEM111, future research should focus on:
Structural Analysis: Determining the three-dimensional structure of TMEM111 could provide insights into its function and potential binding sites.
Functional Studies: Investigating the protein's role in cell signaling or transport processes could reveal its biological significance.
Expression Patterns: Analyzing TMEM111 expression across different tissues and conditions may help identify its physiological relevance.
| Probe ID | Gene Symbol | Entrez Gene Name | Expression Change | Statistical Significance | Heritability |
|---|---|---|---|---|---|
| 1812325 | TMEM111 | Transmembrane protein 111 | CV↓ | 9.48E−13 | 0.75 |
- Identification of brain transcriptional variation reproduced in ... (2009)
- Variably expressed networks: Topics by Science.gov
Transmembrane protein 111 (TMEM111) is a component of the endoplasmic reticulum membrane protein complex (EMC). It facilitates the energy-independent insertion of newly synthesized membrane proteins into the endoplasmic reticulum (ER) membrane. TMEM111 preferentially accommodates proteins with weakly hydrophobic transmembrane domains or those containing destabilizing features such as charged and aromatic residues. It is involved in the co-translational insertion of multi-pass membrane proteins, where stop-transfer membrane-anchor sequences become ER membrane-spanning helices. Additionally, it's essential for the post-translational insertion of tail-anchored (TA) proteins into ER membranes. By mediating the correct co-translational insertion of N-terminal transmembrane domains in an N-exo topology (with a translocated N-terminus in the ER lumen), TMEM111 regulates the topology of multi-pass membrane proteins, such as G protein-coupled receptors. Through its role in regulating protein membrane insertion, it indirectly influences various cellular processes.