| ARL6IP4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | ARL6IP4 , SFRS20, SR-25, SRp25, SRrp37, ADP ribosylation factor like GTPase 6 interacting protein 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 607668 MGI: 1929500 HomoloGene: 9606 GeneCards: ARL6IP4 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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ADP-ribosylation-like factor 6 interacting protein 4 (ARL6IP4), also called SRp25 is the product of the ARL6IP4 gene located on chromosome 12q24. 31. Its function is unknown.
It is 360 amino acids in length. It is expressed ubiquitously but only in G1/S phase of the cell cycle. [5] The human and mouse mRNAs of this protein have 77% homology. [6]
Two types of amino acid clusters have been observed, a serine cluster and a basic cluster. [6]
Its function(s) are unknown. However, due to sequence homology of its protein with SR splicing factors, it is widely believed that the protein is nuclear and may have a role in splicing regulation. [6] The protein is believed to be a mediator in the RAC1 signalling pathway. [7]
The pre-mRNA of the ARL6IP4 gene product is subject to RNA Editing. [8]
A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA (ADARs) that specifically recognize adenosines within double-stranded regions of pre-mRNAs and deaminate them to inosine. Inosines are recognised as guanosine by cellular translational machinery. ADAR 1 and ADAR 2 are the only enzymatically active members. ADAR3 is thought to have a regulatory role in the brain. ADAR1 and ADAR 2 are widely expressed in tissues while ADAR 3 is restricted to the brain. The double stranded regions of RNA are formed by base-pairing between residues in the region close to the editing site with residues usually in a neighboring intron but can be an exonic sequence. The region that base pairs with the editing region is known as an Editing Complementary Sequence (ECS).
Editing occurs at a K/R editing site within amino acid position 225 of the final protein. Using RT-PCR and sequencing of 100 individual clones, 7% of isoform 3 of the protein showed a G instead of an A at this position during sequencing. Other minor editing sites may be potentially present including some in the same exon as the major editing site. As is the case of IGFBP7, pre-mRNA, editing is unusual as the RNA fold back structure is made up off exonic sequence only. [8]
Editing at this site results in a codon changed from a Lysine to an Arginine. This occurs in a highly basic region of the protein. [8]
The function of the unedited protein is largely uncharacterised. Therefore, the effect of editing on the pre-mRNA on the proteins function is also unknown. The amino acid change is conservative and is unlikely to massively alter protein function. However, the editing site may be important since the amino acid being altered is a Lysine, which may be involved in the regulation of protein expression. Lysines can be sites of post-translational modification and the conversion of Lysine to an Arginine could affect post-translational modification. [8]
Protein biosynthesis is a core biological process, occurring inside cells, balancing the loss of cellular proteins through the production of new proteins. Proteins perform a number of critical functions as enzymes, structural proteins or hormones. Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences.
RNA editing is a molecular process through which some cells can make discrete changes to specific nucleotide sequences within an RNA molecule after it has been generated by RNA polymerase. It occurs in all living organisms and is one of the most evolutionarily conserved properties of RNAs. RNA editing may include the insertion, deletion, and base substitution of nucleotides within the RNA molecule. RNA editing is relatively rare, with common forms of RNA processing not usually considered as editing. It can affect the activity, localization as well as stability of RNAs, and has been linked with human diseases.
RNA-binding proteins are proteins that bind to the double or single stranded RNA in cells and participate in forming ribonucleoprotein complexes. RBPs contain various structural motifs, such as RNA recognition motif (RRM), dsRNA binding domain, zinc finger and others. They are cytoplasmic and nuclear proteins. However, since most mature RNA is exported from the nucleus relatively quickly, most RBPs in the nucleus exist as complexes of protein and pre-mRNA called heterogeneous ribonucleoprotein particles (hnRNPs). RBPs have crucial roles in various cellular processes such as: cellular function, transport and localization. They especially play a major role in post-transcriptional control of RNAs, such as: splicing, polyadenylation, mRNA stabilization, mRNA localization and translation. Eukaryotic cells express diverse RBPs with unique RNA-binding activity and protein–protein interaction. According to the Eukaryotic RBP Database (EuRBPDB), there are 2961 genes encoding RBPs in humans. During evolution, the diversity of RBPs greatly increased with the increase in the number of introns. Diversity enabled eukaryotic cells to utilize RNA exons in various arrangements, giving rise to a unique RNP (ribonucleoprotein) for each RNA. Although RBPs have a crucial role in post-transcriptional regulation in gene expression, relatively few RBPs have been studied systematically.It has now become clear that RNA–RBP interactions play important roles in many biological processes among organisms.
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Double-stranded RNA-specific editase 1 is an enzyme that in humans is encoded by the ADARB1 gene. The enzyme is a member of ADAR family.
Glutamate receptor, ionotropic, kainate 1, also known as GRIK1, is a protein that in humans is encoded by the GRIK1 gene.
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