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HighlightsTransmembrane BAX inhibitor motif containing 1 (TMBIM1, also known as RECS1, LFG3) is a 34.6 kDa protein predicted to contain seven transmembrane domains located in endosomal/lysosomal membranes. It is ubiquitously distributed in different tissues, with high expression in the heart, skeletal muscle, and brain, but is not expressed in the thymus, spleen or testis. Like other members of TMBIM family, TMBIM1 protein possesses the di-aspartyl pH sensor responsible for pH sensing. Studies of this protein have primarily been achieved in animal models.
| Basic Information of TMBIM1 | |
| Protein Name | Transmembrane BAX inhibitor motif containing 1 |
| Gene Name | TMBIM1 |
| Aliases | Protein RECS1 homolog, Transmembrane BAX inhibitor motif-containing protein 1 |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q969X1 |
| Transmembrane Times | 7 |
| Length (aa) | 311 |
| Sequence | MSNPSAPPPYEDRNPLYPGPPPPGGYGQPSVLPGGYPAYPGYPQPGYGHPAGYPQPMPPTHPMPMNYGPGHGYDGEERAVSDSFGPGEWDDRKVRHTFIRKVYSIISVQLLITVAIIAIFTFVEPVSAFVRRNVAVYYVSYAVFVVTYLILACCQGPRRRFPWNIILLTLFTFAMGFMTGTISSMYQTKAVIIAMIITAVVSISVTIFCFQTKVDFTSCTGLFCVLGIVLLVTGIVTSIVLYFQYVYWLHMLYAALGAICFTLFLAYDTQLVLGNRKHTISPEDYITGALQIYTDIIYIFTFVLQLMGDRN |
TMBIM1 is an essential protein that is involved in a variety of biological processes. It protects against Fas-mediated apoptosis by reducing Fas expression on the cell surface, negatively regulate aortic matrix metalloproteinase-9 (MMP9) production and play a protective role in vascular remodeling. Like other TMBIM members, it also maintains cellular Ca2+ homeostasis. In addition, TMBIM has been also involved in the progression of some diseases. It is reported that TMBIM is a critical regulator of NASH by targeting the lysosomal degradation of TLR4. TMBIM has been also identified as an important regulator of cardiac hypertrophy promoting the lysosome-mediated degradation of activated TLR4. These studies have indicated that TMBIM1 could be a potential drug target for related diseases.
Fig. 1 Schematic illustration of human TMBIM1.
This study investigated the role of TMBIM1 in cardiac hypertrophy. The results showed that cardiac TMBIM1 exerted its protective function against aortic banding-induce cardiac hypertrophy by promoting the lysosome-mediated degradation of activated TLR4.
This study demonstrated that TMBIM1 was an effective suppressor of steatohepatitis and a regulator of the multivesicular body (MVB)-lysosomal pathway. Overexpression of Tmbim1 in the liver effectively inhibited NAFLD in mice and NASH progression in monkeys. These findings indicated that targeting TMBIM1 may be a promising strategy to treat NASH.
This study characterized the structure, subcellular localization, tissue expression, and the effect on Ca2+ homeostasis of the members of TMBIM family. The results showed that the members all played a role in the intracellular Ca2+ homeostasis maintenance.
This study assessed whether RECS1 KO mice have altered gelatinase levels and whether they were prone to aortic dilation. The results showed that RECS1 inhibited aortic MMP-9 production and the deficiency of RECS1 induced susceptibility to aortic dilation and cystic medial degeneration in the mice, indicating a protective role of RECS1 in vascular remodeling.
Using RECS1 knockout mice, this study demonstrated that these mice are prone to cystic medial degeneration, suggesting a protective role of this protein in vascular remodeling.
Creative Biolabs now provides first-class membrane protein production/preparation services using various techniques and tools. Supported by our leading Magic™ Membrane Protein Production Platform, we provide high-quality membrane proteins incorporated in detergent micelles, liposomes, nanodiscs, and polymers. With the help of our experienced scientists, proteins can be isolated and stabilized efficiently while maximally keeping the structural and functional integrity. Besides, we are also experienced in dealing with anti-membrane protein antibody discovery that is proudly aided by our powerful Magic™ Anti-Membrane Protein Antibody Discovery Platform.
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