SCN3B (sodium channel, voltage-gated, type III, beta ,human IgG1-Fc chimera) belongs to the sodium channel auxiliary subunit SCN3B family. It contains 1 Ig-like C2-type (immunoglobulin-like) domain. Voltage-gated sodium channels are transmembrane glycoprotein complexes composed of a large alpha subunit and one or more regulatory beta subunits. They are responsible for the generation and propagation of action potentials in neurons and muscle. SCN3B gene encodes one member of the sodium channel beta subunit gene family, and influences the inactivation kinetics of the sodium channel. Two alternatively spliced variants, encoding the same protein, have been identified. Defects in SCN3B are the cause of Brugada syndrome type 7. A tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram. It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset.
Immunoglobulin J chain, also known as IGJ and IGCJ, is a secreted polypeptide which is the first immunoglobulin-related polypeptide expressed during the embryogenesis and differentiation of B cells in the fetal liver. The joining Immunoglobulin J chain is a small polypeptide, expressed by mucosal and glandular plasma cells, which regulates polymer formation of immunoglobulin (Ig)A and IgM. Immunoglobulin J chain / IGJ serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. Immunoglobulin J chain / IGJ also help to bind these immunoglobulins to secretory component. J-chain incorporation into polymeric IgA (pIgA, mainly dimers) and pentameric IgM endows these antibodies with several salient features. Immunoglobulin J chain / IGJ is involved in creating the binding site for pIgR / SC in the Ig polymers, not only by determining the polymeric quaternary structure but apparently also by interacting directly with the receptor protein. Both the immunoglobulin J chain / IGJ and the pIgR/SC are key proteins in secretory immunity.
Immunoglobulin lambda constant region is constant region of immunoglobulin light chains. 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. IGLC2 is 105 amino acids (aa) in length. It contains one Ig-like domain (aa 7-100) and generates a disulfide bond with an IgH chain via Cys104.
Immunoglobulin superfamily member 11(IGSF11) is abundantly expressed in testis and ovary and to a lower extent in brain, kidney and skeletal muscle.IGSF11 functions as a cell adhesion molecule through homophilic interaction and can also stimulates cell growth.IGSF proteins share significant homology with endothelial cell-selective adhesion molecule and coxsackievirus and adenovirus receptor, which mediates cell attachment and homotypic intercellular interactions.
Immunoglobulin superfamily member 11(IGSF11) are expressed on the plasma membrane in the tesis and brain. These IGSF proteins undergo final modifications during capacitation and/or the acrosome reaction. IGSF proteins share significant homology with endothelial cell-selective adhesion molecule and coxsackievirus and adenovirus receptor, which mediates cell attachment and homotypic intercellular interactions. In clinical, the IGSF11 has been reported to over expressed in colorectal cancers and hepatocellular carcinomas as well as intestinal-type gastric cancers compared to their corresponding non- cancerous tissues. The IGSF11 has also been found expressed abundantly in testis and ovary and the IGSF11 can be used as a candidate of cancer-testis antigen.
Immunoglobulin superfamily member 3 (IGSF3), also known as Glu-Trp-Ile EWI motif-containing protein 3, IgSF3 and EWI-3 and IGSF3, is a single-pass type I membrane protein which belongs to the EWI subfamily of the Ig Superfamily of molecules. IGSF3 has an overall structural similarity and strong sequence similarity to V7, a human leukocyte surface protein. IGSF3 contains eight Ig-like C2-type (immunoglobulin-like) domains. IGSF3 is expressed in a wide range of tissues with high expression in Placenta, kidney and lung. EWI-2 is part of a novel Ig subfamily that includes EWI-F (F2alpha receptor regulatory protein (FPRP), CD9P-1 ), EWI-3 (IGSF3), and EWI-101 (CD101). All four members of this Ig subfamily contain a Glu-Trp-Ile (EWI) motif not seen in other Ig proteins. Human IGSF3 shares 92 % aa identity with mouse IGSF3.
IHPK1 is a inositol hexaphosphate kinase (IHPK) protein which belongs to the inositol phosphokinase (IPK) family. IHPK proteins are likely responsible for the conversion of inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). IHPK1 may also convert 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 and affect the growth suppressive and apoptotic activities of interferon-beta in some ovarian cancers. During cell death, IHPK1 activity is enhanced, and intracellular InsP7 level is augmented. The distribution of IHPK1 or another predisposing gene affected by position effect of translocation may explain the T2DM phenotype at least in this family.
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