C2orf27
From Wikipedia, the free encyclopedia
The mRNA is 1,222bp in length and is located at 2q21.2 with a total of five exons in Homo sapiens.[1][2] Other sources list C2orf27B as a paralog but this is unlikely because both genes are located in the same place on chromosome 2.[3] It seems to be generally accepted that they are the same gene.[1] Other gene aliases include C2orf27 and chromosome 2 open reading frame 27A. The gene is surrounded upstream by POTEKP and downstream by ANKRD30BL.
Protein
The length of the C2orf27 protein sequence is 203 a.a. in length and has a molecular weight of 21.5 kDa with a pI of 5.13 in Homo sapiens.[4][5] When taking into account the primate orthologs, the molecular weights range from 21.4 to 36.7 kDa with the isoelectric point ranging from 4.58 to 5.25.[6][5] This gene is located in the nucleus of the cell and, it doesn't contain any transmembrane regions.[7][8]
Looking at the motifs of the protein sequence, a few important ones are present. All of the repeat sequences are concentrated near the N-terminus of the protein and are highly conserved through all the orthologs.
| PGTA | LELE | PVPA | PPGTALEL / PPGSALEL | |
|---|---|---|---|---|
| Location 1 | P37-A40 | L41-E44 | P21-A24 | P36-L43 |
| Location 2 | P54-A57 | L86-E89 | P27-A30 | P75-L82 |
Post-translationally, there are multiple glycosylation sites scattered throughout the protein sequence, phosphorylation site positioned at S13, and a nuclear export signal located at L80 - V90, which also happens to be within a coiled coil region.
Expression
C2orf27 is ubiquitously expressed in most tissues but with increased expression in the brain, pancreas, kidneys, and testis.[9][10]
Interactions
The protein is said to interaction with another protein called ataxin-1 which was discovered by performing a two hybrid prey pooling (Y2H) approach.[11] They share the similar characteristics of being located in the nucleus of cells and are expressed in the brain.
Structure
The overall structure of this protein is predicted to be composed of both alpha-helices and beta-sheets. The majority of the alpha-helices fall on the N-terminus of the protein and the beta-sheets fall near the C-terminus of the protein. There is a sequence of four prolines located from P185 to P188 has the secondary structure of a type II polyproline helix.
