Probable non-functional immunoglobulin lambda variable 11-55
1_MALTP 6_ LLLLL 11_ LSHCT 16_ GSLSR 21_ PVLTQ 26_ PPSLS 31_ ASPGA 36_ TARLP 41_ CTLSS 46_ DLSVG 51_ GKNMF 56_ WYQQK 61_ LGSSP 66_ RLFLY 71_ HYSDS 76_ DKQLG 81_ PGVPS 86_ RVSGS 91_ KETSS 96_ NTAFL 101_ LISGL 106_ QPEDE 111_ ADYYC 116_QVYES
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)