Mannan-Binding Lectin Serine Protease 1 (MASP-1) belongs to the peptidase S1 family. MASP1 contains two CUB domains, one EGF-like domain, one peptidase S1 domain and two Sushi (CCP/SCR) domains. MASP1 is primarily expressed in liver. MASP1 involved in the lectin pathway of the complement, performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. MASP1 is synthesized as a zymogen and activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. MASP1 is not directly involved in complement activation but may act as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP2. MASP1 is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. MASP1 is inhibited by SERPING1 and A2M.
MYC associated factor X contains 1 basic helix-loop-helix (bHLH) domain and belongs to MAX family. It is highly expressed in the brain, heart and lung while lower levels are seen in the liver, kidney and skeletal muscle. MYC associated factor X can form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. MYC associated factor X may also repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Multiple alternatively spliced transcript variants have been described for MYC associated factor X gene but the full-length nature for some of them is unknown.
Myc-Associated Factor X (MAX) is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It contains 1 basic helix-loop-helix (bHLH) domain. It is found in the brain, heart, and lung at high levels while lower levels are seen in the liver, kidney, and skeletal muscle. MAX forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. It may repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity.
MAP3K12-binding inhibitory protein 1 (MBIP) is a 39kD protein high expression in the heart and lung. It is a component of the ADA2A-containing complex (ATAC) complex, a complex with histone acetyltransferase activity on histones H3 and H4, and composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, CSRP2BP and WDR5. It’s function to inhibit the MAP3K12 activity to induce the activation of the JNK/SAPK pathway.
MBL (mannose-binding lectin) is primarily a liver-derived collagen-like serum protein, which binds sugar structures on micro-organisms and on dying host cells and is one of the four known mediators that initiate activation of the complement system via the lectin pathway. MBL and the ficolins (Ficolin-1, Ficolin-2 and Ficolin-3) are soluble collagen-like proteins that are involved in innate immune defence. They bind sugar structures or acetylated compounds present on microorganisms and on dying host cells and they initiate activation of the lectin complement pathway in varying degrees. MBL2 encodes the mannose-binding lectin, which is a key player in the innate immune system and has recently been found to play a role in development of type 1 diabetes and gestational diabetes mellitus. Common variant alleles situated both in promoter and structural regions of the MBL2 gene influence the stability and the serum concentration of the protein. Several polymorphisms in the promoter and structural regions of MBL2 adversely affect the plasma concentration and oligomeric state of MBL. The possession of mutant alleles has been linked to disease outcome for a variety of bacterial and viral infections. Mutant MBL2 haplotypes have been linked to disease progression and response to therapy in HCV infection.
Mannose-Binding Protein C (MBP-C) belongs to the Collectin family of innate immune defense proteins. MBL binds to an array of carbohydrate patterns on pathogen surfaces. Collectin family members share common structural features: a cysteine rich amino-terminal domain, a collagen-like region, an α-helical coiled-coil neck domain and a carboxy terminal C-type Lectin or carbohydrate recognition domain (CRD). MBL homotrimerizes to form a structural unit joined by N-terminal disulfide bridges. These homotrimers further associates into oligomeric structures of up to 6 units. Whereas two forms of MBL proteins exist in rodents and other animals. Human MBL-2 is 25 kDa. Human MBL-2 is a secreted glycoprotein that is synthesized as a 248 amino acid (aa) precursor that contains a 20 aa signal sequence, a 21 aa cysteine-rich region, a 58 aa collagen-like segment and a 111 aa C-type lectin domain that binds to neutral bacterial carbohydrates.
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