Probable non-functional immunoglobulin lambda variable 2-33
1_MAWAL 6_ LLLTL 11_ LTQGT 16_ GSWAQ 21_ SALTQ 26_ PPFVS 31_ GAPGQ 36_ SVTIS 41_ CTGTS 46_ SDVGD 51_ YDHVF 56_ WYQKR 61_ LSTTS 66_ RLLIY 71_ NVNTR 76_ PSGIS 81_ DLFSG 86_ SKSGN 91_ MASLT 96_ ISGLK 101_ SEVEA 106_ NYHCS 111_LYSSS
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)