PRR32
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| PRR32 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | PRR32, CXorf64, proline rich 32, chromosome x open reading frame 64, Cxorf33 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | MGI: 1916050; HomoloGene: 90132; GeneCards: PRR32; OMA:PRR32 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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PRR32 is a protein that in humans is encoded by the CXorf64 (Chromosome X open reading frame 64) gene. It was also found that the homologs of the PRR32 gene is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, and rat. It was also found through ncbi that 82 organisms have orthologs with human gene PRR323.[5]
PRR32 (CXorf64) seems to be involved with a group of genes over-expressed in ALS (Amyotrophic lateral sclerosis), evident from a study aiming to study gene expression patterns in muscles from patients with amyotrophic lateral sclerosis and multifocal motor neuropathy.[6]
Transcript
The gene is located on Chromosome X, at position Xq25, and is 2023 bases long (significantly small when compared to other genes). Its location is at the antisense (+) strand. As shown in the graphic below, it is flanked by upstream by the DKAF12l1 shown in green on the left and downstream by LOC10. CXorf64 is the blue column shown in the middle.[7]
CXorf64 has 1 exon which ultimately forms 1 transcript variant. This gene is expressed most in muscle tissue. There are no known isoforms in which CXorf64 is expressed.[8]
Protein
General Properties
| Property | Cleaved Protein | Mature Protein |
|---|---|---|
| Amino Acid Length | 298 | 298 |
| Isoelectric Point | 7.34 | ~7.2-7.4 |
| Molecular Weight | 31.9 kDa | ~31.9-33 kDa |
Structure
Shown to the right is a predicted tertiary structure of the protein. It is marked by long alpha-helices localized to the end of the protein opposite the N- and C- terminal ends
Expression
According to microarray-assessed tissue expression analysis by NCBI GEO, the gene CXorf64 has average expression levels in most tissues save for, prostate, and heart, fat, and endometrium which have relatively low levels of expression (~25th percentile of tissue gene expression) . Almost every microarray study determined very low levels of gene expression across all tissues assessed . This evidence prompted further analysis with other tools. While no tissue analysis was present on Allen Brain Atlas or genepaint, the Human Protein Atlas suggested that the gene was more highly expressed in heart, prostate, and a and fat tissues .
Sub-cellular Location
It synthesizes in the cell cytoplasm and is predicted to localize in the mitochondria. It is predicted to localize in the nucleus, plasma membrane, extracellular, mitochondrion, peroxisome, and cytosol.
Post-Translational Modification
N-linked glycosylation
It was found that there are several post-translational modifications that are performed on PRR32. These include several N-linked glycosylation sites that were predicted with high confidence. Glycosylation is known to play a part in cell-cell adhesion ( `a mechanism employed by cells of the immune system) via sugar-binding proteins. The graph illustrates predicted N-glyc sites across the protein chain (x-axis represents protein length from N- to C-terminal). A position with a potential (vertical lines) crossing the threshold (horizontal line at 0.5) is predicted glycosylated.[12]
