Probable non-functional immunoglobulin kappa variable 1D-42
1_MDMRV 6_ PAQLL 11_ GLLLL 16_ WLPGV 21_ RFDIQ 26_ MTQSP 31_ SFLSA 36_ SVGDR 41_ VSIIC 46_ WASEG 51_ ISSNL 56_ AWYLQ 61_ KPGKS 66_ PKLFL 71_ YDAKD 76_ LHPGV 81_ SSRFS 86_ GRGSG 91_ TDFTL 96_ TIISL 101_ KPEDF 106_ AAYYC 111_KQDFS
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)