Protein
Known Protein Isoforms
Alternative splicing produces two known isoforms of the human protein. They are XP_006711141.1 which is 1489aa in length and XP_003307860.2 which is 713aa in length. [9] [10]
Composition
The protein has an isoelectric point (pI) of 11. The predicted molecular weight (mW) is 160kDa for the human protein, but ranges from 140-180kDa for more distant orthologs. [11] Compositional analysis revealed the most abundant amino acid to be Alanine (A) at 12.4% of the total protein. The analysis also revealed C1orf167 protein to be rich in Tryptophan (W) and deficient in Tyrosine (Y) and Isoleucine (I). [12]
Subcellular Localization
C1orf167 is predicted to be localized to the cell nucleus. [13]
Post-Translational Modifications
C1orf167 is predicted to undergo phosphorylation, O-Glycosylation, SUMOylation, glycation, and cleavage by staphylococcal peptidase I (Q105, Q321) and Glutamyl endopeptidase (Q1101). [14] [15] [16] [17] [18]
| Species | ||||||
|---|---|---|---|---|---|---|
| H. sapiens | T. manatus latirostris | U. parryii | D. novaehollandiae | P. vitticeps | C. milli | |
| SUMOylation | K22 | IVTLE447-451, K604, K605, VRVVP 684-688, | VAVVD502-506 | K434 | K57,K128,K578, K993, K1388 | ISILH 121-125, K264,K477, K497, K522 IVSIC 621-625 LCLVY 703-707 VVVLR 975-979, VLQLR 1027-1031 K1199 K1208 |
| O-GlcNAcylation | Many* | Similar Distribution (but more sites) | Similar Distribution (but fewer sites) | Similar Distribution (but fewer sites) | Similar Distribution | Similar Distribution (but fewer sites) |
| Glycation of ε amino groups of lysines | K -22, 114, 323,399, 433,505, 701, 710,720, 832,975, 1138,1279, 1306,1394, 1418 | K-335,516, 534,605, 747,757, 1080,1125, 1189, 1382 | K-114, 123,333, 462,651, 660,661, 938, 1111, 1149 | K-72,103,128, 133, 183,240,241, 248,290,398, 437,466,483, 494,505,552, 589,718, 767,772,820, 974,1106 | K-14,57,60,89,96, 128,133,157,275, 423,488,578,619, 647,890,900,952, 983,993,1208,1279, 1288, | K-4,56,106,131,163,169, 177,235,291, 480, 566,660,666,717, 780,814,827, 853, 857, 936, 954, 964,974, 986, 1015, 1079, 1208 |
| Nuclear Export Signal | L84 | L808 | L84 | L589 | V869, L874 | L186, L188, L1117 |
| Phosphorylation | Many* | Similar Distribution | Similar Distribution | Similar Distribution | Similar Distribution | Similar Distribution |
| Proteinase Cleavage Sites | Q105, Q321, Q1101 | Q441, Q1030 | Q72 | Q60 | Q90, Q155, Q498 | Q520, Q809, Q908, |
Table 1. Post-Translational Modifications determined for C1orf167.
*GPS, NetPhos results indicated hyper-phosphorylation of C1orf167 in H. sapiens and five of its orthologs.
Domain and Motifs by Homology
One domain of unknown function, located from 954aa-1418aa, is 465 amino acids in length.
Secondary Structure
C1orf167 was determined to be rich in alpha helices. No notable regions of beta pleated sheets or coils were predicted. [20] In particular, high confidence was indicated for 42 alpha helices with the longest alpha helix region spanning from residues 450aa to 1182aa. This long alpha helix region includes a significant portion of the conserved DUF which spans 954aa-1418aa. [21] [22] [23] [24] [25]
Tertiary Structure
The best-aligned structural analog, generated by I-TASSER, of C1orf167 had a confidence (c-score) score of -0.68 given a range of [-5,2] with higher values indicating a higher confidence. [25] Per Swiss Model, two monomers are predicted to form an alpha helix. [26] Both of the helices are aligned facing outwards with hydrophobic amino acids such as glutamic acid (E) on the interior and asparagine (R), Serine (and lysine (K) on the exterior. Asparagine residues may serve as an important oligosaccharide binding site. [27]
