Probable non-functional immunoglobulin kappa variable 3-7
1_MEAPA 6_ QLLFL 11_ LLLWL 16_ PDTTR 21_ EIVMT 26_ QSPPT 31_ LSLSP 36_ GERVT 41_ LSCRA 46_ SQSVS 51_ SSYLT 56_ WYQQK 61_ PGQAP 66_ RLLIY 71_ GASTR 76_ ATSIP 81_ ARFSG 86_ SGSGT 91_ DFTLT 96_ ISSLQ 101_ PEDFA 106_ VYYCQ 111_QDYNL
1: Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin light chains (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). 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:20176268, PubMed:22158414). 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)