G MOG SERIES

Twelve family members had narcolepsy and cataplexy, 7 of whom were obese and 4 of whom had type 2 diabetes. In vitro expression studies in murine oligodendroglial precursor cells demonstrated that the mutant protein was ectopically expressed in the cytoplasm, although membrane localization did not appear to be affected. The mutation was predicted to cause abnormal protein folding and a nonfunctional protein. (2011) identified a heterozygous 398C-G transversion in the MOG gene, resulting in a ser133-to-cys (S133C) substitution at the tip of the solvent-exposed loop in the extracellular Ig-like domain. In affected members of a large Spanish family with narcolepsy and cataplexy (NRCLP7 614250), Hor et al.

G MOG SERIES

OMG belongs to the family of proteins with a series of tandem leucine-rich repeats, while MOG is a member of the Ig superfamily. MOG is an intrinsic membrane molecule with 2 transmembrane domains, whereas OMG is anchored in the outer leaflet of the plasma membrane through a glycophospholipid tail. The 2 glycoproteins are associated specifically with oligodendrocytes and myelin, but have quite different roles in myelinogenesis and are structurally unrelated ( Pham-Dinh, 1994). It has a potential N-linked glycosylation site at asn31.Дespite the similar names, oligodendrocyte-myelin glycoprotein (OMG 164345) is a separate protein encoded within a large intron of the NF1 gene ( 613113). Like its bovine and murine counterparts, it contains an Ig-like domain and 2 putative transmembrane domains. (1995) cloned a human MOG cDNA encoding a predicted polypeptide containing a signal peptide of 29 amino acids followed by 218 amino acids of mature protein. The N terminus shows strong homology with the N terminus of butyrophilin ( 601610), a protein expressed in the lactating mammary gland. All contain 2 transmembrane segments and have an N-terminal, extracellular region with characteristics of an immunoglobulin variable domain. The predicted sequences of the mature MOG proteins are highly conserved. (1993) isolated bovine, mouse, and rat MOG cDNAs.

G mog