IGKC

IGKC (Immunoglobulin Kappa Constant) is a Protein Coding gene. Diseases associated with IGKC include Immunoglobulin Kappa Light Chain Deficiency and Extramedullary Plasmacytoma. Among its related pathways are Immune response Fc epsilon RI pathway and Immune response Lectin induced complement pathway. Gene Ontology (GO) annotations related to this gene include antigen binding. An important paralog of this gene is IGLC3.

Immunoglobulin Kappa Constant

Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268).

The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).

B cell receptor signaling pathway Source: GO_Central
Complement activation, classical pathway Source: GO_Central
Defense response to bacterium Source: GO_Central
Immune response Source: UniProtKB
Innate immune response Source: GO_Central
Phagocytosis, engulfment Source: GO_Central
Phagocytosis, recognition Source: GO_Central
Positive regulation of B cell activation Source: GO_Central
Retina homeostasis Source: UniProtKB

Secreted; Cell membrane

Immunoglobulin kappa light chain deficiency (IGKCD):
A disease characterized by the complete absence of immunoglobulin kappa chains.