MMGT1: A Transmembrane Protein Identified as a Potential Drug Target and Biomarker

Target Name: MMGT1

NCBI ID: G93380

MMGT1

MMGT1: A Transmembrane Protein Identified as a Potential Drug Target and Biomarker

Introduction

Membrane-bound proteins are a class of proteins that play a vital role in cellular signaling, structure, and function. Membrane-bound proteins are also known as transmembrane proteins (TMPs) or integral membrane proteins (IMMs), and they are involved in various physiological processes in the cell, including signal transduction, ion channels, and protein-protein interactions. In this article, we will focus on one of the promising TMPs, known as transmembrane protein 32 (MMGT1), and its potential as a drug target and biomarker.

MMGT1: Structural and Functional Characterization

MMGT1 is a 21-kDa protein that is expressed in various tissues and cell types, including brain, heart, skeletal muscles, and tissues. It is primarily localized to the endoplasmic reticulum (ER) and can also be found in the mitochondrial outer membrane ( MOM) and in the endosomal system. MMGT1 is aTMP that consists of an N-terminal transmembrane region, a catalytic region, and a C-terminal cytoplasmic region.

The N-terminal transmembrane region of MMGT1 contains a protein kinase-like domain (PKD) and a short extracellular domain (ECD). The PKD is a structural domain that is known to be involved in protein-protein interactions and signaling. The ECD is a short region that is involved in the formation of the transmembrane (TM) state.

The catalytic region of MMGT1 contains a catalytic domain (CAD) and a nucleotide-binding domain (NBD). The CAD is a structural domain that is known to be involved in protein-protein interactions and catalytic activities. The NBD is a structural domain that is known to be involved in the regulation of protein-protein interactions.

The C-terminal cytoplasmic region of MMGT1 contains a unique N-terminal region that is known as the cytoplasmic loop. The cytoplasmic loop is a structural domain that is involved in the regulation of protein-protein interactions and the formation of the endosomal system.

Functional Characterization of MMGT1

MMGT1 is involved in various physiological processes in the cell, including the regulation of protein-protein interactions, intracellular signaling pathways, and the formation of the endosomal system. One of the most significant functions of MMGT1 is its role in the regulation of protein-protein interactions.

MMGT1 has been shown to play a role in the regulation of protein-protein interactions in various cellular processes. For example, studies have shown that MMGT1 can interact with various protein partners, including casein kinase (CK) 2, casein kinase 3 (CK- 3), and myosin regulatory light chain 2 (MLC2). These interactions are critical for the regulation of various cellular processes, including cell signaling pathways, protein-protein interactions, and intracellular signaling pathways.

MMGT1 has also been shown to play a role in the regulation of intracellular signaling pathways. For example, studies have shown that MMGT1 can interact with various partners protein, including the transcription factor, activator protein 1 (TA-1), and the protein kinase B (PKB). These interactions are critical for the regulation of various cellular processes, including cell signaling pathways, protein-protein interactions, and intracellular signaling pathways.

MMGT1 has also been shown to play a role in the regulation of

Protein Name: Membrane Magnesium Transporter 1

Functions: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176, PubMed:32439656). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:30415835, PubMed:29809151, PubMed:29242231). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:30415835, PubMed:29809151). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (By similarity). May be involved in Mg(2+) transport (By similarity)

The "MMGT1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about MMGT1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets