Probable non-functional immunoglobulin heavy variable 3-35
1_MEFGL 6_ SWVFL 11_ AAILK 16_ GVQCE 21_ VQLVE 26_ SGGGL 31_ VQPGG 36_ SLRLS 41_ CAASG 46_ FTFSN 51_ SDMNW 56_ VHQAP 61_ GKGLE 66_ WVSGV 71_ SWNGS 76_ RTHYA 81_ DSVKG 86_ RFIIS 91_ RDNSR 96_ NTLYL 101_ QTNSL 106_ RAEDT 111_AVYYC
1: Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin heavy 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)