Probable non-functional immunoglobulin lambda variable 3-32
1_MAWTP 6_ PLLVL 11_ TLCTG 16_ SVISS 21_ GPTQV 26_ PAVSV 31_ ALGQM 36_ ARITC 41_ QGDSM 46_ EGSYE 51_ HWYQQ 56_ KPGQA 61_ PVLVI 66_ YDSSD 71_ RPSRI 76_ PERFS 81_ GSKSG 86_ NTTTL 91_ TITGA 96_ QAEDE 101_ ADYYY 106_QLIDN
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)