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EMR4
The EGF module-containing Mucin-like hormone Receptors (EMRs) are closely related subgroup of G protein-coupled receptors (GPCRs). These receptors have a unique hybrid structure in which an extracellular epidermal growth factor (EGF)-like domain is fused to a GPCR domain through a mucin-like stalk. There are four variants of EMR labeled 1–4, each encoded by a separate gene. These receptors are predominantly expressed in cells of the immune system and bind ligands such as CD55 Complement decay-accelerating factor, also known as CD55 or DAF, is a protein that, in humans, is encoded by the ''CD55'' gene. DAF regulates the complement system on the cell surface. It recognizes C4b and C3b fragments that are created during a .... References External links * * * * G protein-coupled receptors {{transmembranereceptor-stub ...
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EMR2
EGF-like module-containing mucin-like hormone receptor-like 2 also known as CD312 (cluster of differentiation 312) is a protein encoded by the ''ADGRE2'' gene. EMR2 is a member of the adhesion GPCR family. Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain. EMR2 is expressed by monocytes/macrophages, dendritic cells and all types of granulocytes. In the case of EMR2 the N-terminal domains consist of alternatively spliced epidermal growth factor-like ( EGF-like) domains. EMR2 is closely related to CD97 with 97% amino-acid identity in the EGF-like domains. The N-terminal fragment (NTF) of EMR2 presents 2-5 EGF-like domains in human. Mice lack the ''Emr2'' gene. This gene is closely linked to the gene encoding EGF-like molecule containing mucin-like hormone receptor 3 EMR3 on chromosome 19. Ligand Like the related CD9 ...
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EMR1
EGF-like module-containing mucin-like hormone receptor-like 1 also known as F4/80 is a protein encoded by the ''ADGRE1'' gene. EMR1 is a member of the adhesion GPCR family characterized by an extended extracellular region containing EGF-like domains. EMR1 is predominantly expressed on the surface of macrophages and plays a significant role in immune response modulation and inflammation. Its expression has been linked to various inflammatory diseases. Structure Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain. The N-terminal fragment (NTF) of EMR1 contains 4-6 Epidermal Growth Factor-like ( EGF-like) domains in human and 4-7 EGF-like domains in the mouse. Tissue distribution EMR1 expression in human is restricted to eosinophils and is a specific marker for these cells. The murine homolog of EMR1, F4/80, is ...
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EMR3
EGF-like module-containing mucin-like hormone receptor-like 3 is a protein encoded by the ''ADGRE3'' gene. EMR3 is a member of the adhesion GPCR family. Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain. EMR3 expression is restricted to monocytes/macrophages, myeloid dendritic cells, and mature granulocytes in human. Transcription of the EMR3 gene results in two alternative spliced forms: a surface protein with extracellular, 7TM, and intracellular domains as well as a truncated soluble form of only the extracellular domain. Mice, next to Emr2, lack the Emr3 gene. Function The protein may play a role in myeloid Myeloid tissue, in the bone marrow sense of the word '' myeloid'' ('' myelo-'' + '' -oid''), is tissue of bone marrow, of bone marrow cell lineage, or resembling bone marrow, and myelogenous tissue ...
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G Protein-coupled Receptor
G protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large group of evolutionarily related proteins that are cell surface receptors that detect molecules outside the cell and activate cellular responses. They are coupled with G proteins. They pass through the cell membrane seven times in the form of six loops (three extracellular loops interacting with ligand molecules, three intracellular loops interacting with G proteins, an N-terminal extracellular region and a C-terminal intracellular region) of amino acid residues, which is why they are sometimes referred to as seven-transmembrane receptors. Text was copied from this source, which is available under Attribution 2.5 Generic (CC BY 2.5) licence/ref> Ligands can bind either to the extracellular N-terminus and loops (e.g. glutamate receptors) or to the binding site wi ...
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Mucin
Mucins () are a family of high molecular weight, heavily glycosylated proteins ( glycoconjugates) produced by epithelial tissues in most animals. Mucins' key characteristic is their ability to form gels; therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. They often take an inhibitory role. Some mucins are associated with controlling mineralization, including nacre formation in mollusks, calcification in echinoderms and bone formation in vertebrates. They bind to pathogens as part of the immune system. Overexpression of the mucin proteins, especially MUC1, is associated with many types of cancer. Although some mucins are membrane-bound due to the presence of a hydrophobic membrane-spanning domain that favors retention in the plasma membrane, most mucins are secreted as principal components of mucus by mucous membranes or are secreted to become a component of saliva. Gene ...
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CD55
Complement decay-accelerating factor, also known as CD55 or DAF, is a protein that, in humans, is encoded by the ''CD55'' gene. DAF regulates the complement system on the cell surface. It recognizes C4b and C3b fragments that are created during activation of C4 ( classical or lectin pathway) or C3 (alternative pathway). Interaction of DAF with cell-associated C4b of the classical and lectin pathways interferes with the conversion of C2 to C2b, thereby preventing formation of the C4b2a C3-convertase, and interaction of DAF with C3b of the alternative pathway interferes with the conversion of factor B to Bb by factor D, thereby preventing formation of the C3bBb C3 convertase of the alternative pathway. Thus, by limiting the amplification convertases of the complement cascade, DAF indirectly blocks the formation of the membrane attack complex. This glycoprotein is broadly distributed among hematopoietic and non-hematopoietic cells. It is a determinant for the Cromer blood group syste ...
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