LOC101928193 is a protein which in humans is encoded by the LOC101928193 gene. There are no known aliases for this gene or protein. Similar copies of this gene, called orthologs, are known to exist in several different species across mammals, amphibians, fish, mollusks, cnidarians, fungi, and bacteria. The human LOC101928193 gene is located on the long (q) arm of chromosome 9 with a cytogenic location at 9q34.2. The molecular location of the gene is from base pair 133,189,767 to base pair 133,192,979 on chromosome 9 for an mRNA length of 3213 nucleotides. The gene and protein are not yet well understood by the scientific community, but there is data on its genetic makeup and expression. The LOC101928193 protein is targeted for the cytoplasm and has the highest level of expression in the thyroid, ovary, skin, and testes in humans.
Gene
Locus
The cytogenic location of LOC101928193 in humans is located on the positive strand at 9q34.2. The molecular location of the protein-encoding region of LOC101928193 is from base pairs 133,189,767 to 133,192,979. Within this region, there is 1 intron and 2 exons.
Gene neighborhood
LOC101928193 is flanked by GBGT1 and 0BP2B on chromosome 9. GBGT1 encodes a member of the ABO gene family and also plays a role in synthesizing glycolipids that are involved in tropism and binding pathogens. 0BP2B is a gene that associates with E-Selectin Level in the ABO gene region.
mRNA
In humans, the LOC101928193 gene produces 3 transcript variants, which produce 3 isoforms of the protein. The LOC101928193 isoform X1 is the longest one at 406 codons in length. LOC101928193 isoform X2 is 388 codons long and LOC101928193 isoform X3 is 399 codons long. All isoforms have 2 exons and their coding mRNA is 3213 nucleotides long.
Protein
The molecular weight of LOC101928193 is 43.5 kiloDaltons. The isoelectric point is 9 pI.
Composition
Compared to most human proteins, there are more valine, glycine, serine, histidine, and phenylalanine residues in LOC101928193. LOC101928193 is an alanine, methionine, asparagine, aspartic acid, glutamic acid, and lysine poor protein. The enrichment of all other amino acids is normal compared to other human proteins. LOC101928193 composition is highly conserved between mammals.
LOC101928193 has an amino acid charge distribution of 0.7% negative, 4.9% positive, and 94.4% neutral. There are no charge runs, hydrophobic segments, or transmembrane domains.
Domains and motifs
There are two different motifs present in LOC101928193. Myristoylation sites are found in the protein sequence 17 times, and a zinc finger domain motif occurs once. The presence of myristoylation sites indicates that LOC101928193 may function in membrane targeting, protein-protein interactions, and signal transduction pathways. Zinc finger domain motifs aid in gene transcription, cell adhesion, protein folding, and chromatin remodeling.
Primary sequence
The LOC101928193 primary coding sequence mRNA is 3213 nucleotides long. There are no upstream open-reading frames, Kozak consensus sequences, or transmembrane regions.
Secondary structure
LOC101928193 has a predicted secondary structure of 56.40% random coils and 43.60% beta sheets. No alpha helices are predicted to occur. Due to the lack of alpha helices in the protein, no coiled coils are predicted to occur in the LOC101928193 secondary structure.
Tertiary structure
The tertiary structure of LOC101928193 is an all beta-sheet protein, as can be seen by its predicted tertiary structure. Both the N-terminus and the C-terminus lack beta-sheets.
Post-translational modifications
O-GlcNAc
There are 13 predicted O-GlcNAc sites within the LOC101928193 protein. O-GlcNAc is a unique form of protein glycosylation that occurs exclusively in the nuclear and cytoplasmic compartments of the cell. O-Glc-NAcylated proteins are abundant on proteins involved in signaling pathways, stress responses, cytoskeletal assembly, and energy metabolism.
N-linked glycosylation
There are no N-linked glycosylation sites due to the absence of asparagine residues.
Phosphorylation
LOC101928193 has many sites of phosphorylation at several serines, threonines, and tyrosines throughout its structure that results in a conformational change and aids in signaling pathways and regulation. There are 33 predicted phosphorylation sites. The relative amount of phosphorylation sites is highly conserved throughout orthologs of LOC101928193.