Gene
C16orf95 is a Homo sapiens gene oriented on the minus strand of chromosome 16. It is located on the cytogenic band 16q24.2 and spans 14.62 kilobases. [1] The gene contains 6 introns and 7 exons. [1]
Chromosome 16 open reading frame 95 (C16orf95) is a gene which in humans encodes the protein C16orf95. It has orthologs in mammals, and is expressed at a low level in many tissues. C16orf95 evolves quickly compared to other proteins.
C16orf95 is a Homo sapiens gene oriented on the minus strand of chromosome 16. It is located on the cytogenic band 16q24.2 and spans 14.62 kilobases. [1] The gene contains 6 introns and 7 exons. [1]
There are no known paralogs of C16orf95.
Orthologs of C16orf95 exist only in mammals (identified with BLAST). [3] The most distant orthologs are found in opossums and Tasmanian devils.
| Genus and species | Common name | NCBI accession | Date of divergence | Sequence identity |
| Homo sapiens | Human | NP_001182053 | 0 mya | 100% |
| Pan paniscus | Bonobo | XP_008972565 | 6.2 mya | 92% |
| Gorilla gorilla gorilla | Gorilla | XP_004058157 | 8.3 mya | 95% |
| Nomascus leucogenys | White-cheeked gibbon | XP_003272503 | 19.3 mya | 88% |
| Mandrillus leucophaeus | Drill | XP_011827052 | 27.3 mya | 78% |
| Propithecus coquereli | Lemur | XP_012513111 | 77.1 mya | 62% |
| Tupaia chinensis | Tree shrew | XP_006152612 | 86.5 mya | 58% |
| Oryctolagus cuniculus | European rabbit | XP_008250325 | 90.1 mya | 56% |
| Mus musculus | Mouse | NP_083873 | 90.1 mya | 54% |
| Rattus norvegicus | Rat | XP_006222844 | 90.1 mya | 51% |
| Camelus bactrianus | Camel | XP_010966555 | 95 mya | 63% |
| Canis lupus familiaris | Dog | XP_005620646 | 95 mya | 63% |
| Equus caballus | Horse | XP_005608538 | 95 mya | 60% |
| Felis catus | Cat | XP_011288582 | 95 mya | 60% |
| Bos taurus | Cattle | XP_015331266 | 95 mya | 60% |
| Lipotes vexillifer | Yangtze river dolphin | XP_007468528 | 95 mya | 50% |
| Myotis lucifugus | Brown bat | XP_014318589 | 95 mya | 56% |
| Trichechus manatus latirostris | Manatee | XP_004377854 | 102 mya | 66% |
| Loxodonta africana | Elephant | XP_003418190 | 102 mya | 59% |
| Orycteropus afer afer | Aardvark | XP_007937409 | 102 mya | 54% |
| Monodelphis domestica | Opossum | XP_007477328 | 162.4 mya | 42% |
| Sarcophilus harrisii | Tasmanian devil | XP_012395810 | 162.4 mya | 41% |
There are three splice variants of C16orf95. [6] The longest transcript contains 1156 base pairs and 7 exons. [7] Compared to variant 1, the second transcript variant lacks exons 4 and 5. [8] This alternative splicing results in a frameshift of the 3' coding region, and a shorter, unique C-terminus. The third transcript variant lacks exons 4 and 5, and uses an alternate 5' exon and start codon. [9] The resulting peptide has unique N- and C-termini compared to variant 1.
| Size (base pairs) | |||
|---|---|---|---|
| Exon # | Variant 1 | Variant 2 | Variant 3 |
| 1 | 330 | 330 | 334 |
| 2 | 52 | 52 | 52 |
| 3 | 126 | 126 | 126 |
| 4 | 147 | – | – |
| 5 | 37 | – | – |
| 6 | 187 | 187 | 187 |
| 7 | 277 | 278 | 278 |
| Total | 1,156 | 973 | 977 |
The 3' untranslated region of the C16orf95 mRNA contains binding sites for KH domain-containing, RNA-binding, signal transduction-associated protein 3 (KHDRBS3) within an internal loop structure. KHDRBS3 regulates mRNA splicing and may act as a negative regulator of cell growth. [12]
The expression of C16orf95 is not well characterized. However, it has been detected at low levels in the following tissue types: bone, brain, ear, eye, intestine, kidney, lung, lymph nodes, prostate, testes, tonsils, skin, and uterus. [13]
The longest isoform of the C16orf95 protein has 239 amino acids. [14] It has a conserved domain of unknown function spanning residues 76 to 239. [14] C16orf95 has a calculated molecular weight of 26.5 kDa, and a predicted isoelectric point of 9.8. [5] Compared to other human proteins, C16orf95 has more cysteine, arginine, and glutamine residues. [5] It has fewer aspartate, glutamate, and asparagine. [5] The high ratio of basic to acidic amino acids contributes to the protein's higher isoelectric point.
C16orf95 is predicted to have several alpha-helices in its C-terminus. [5] This is true for the human and mouse proteins. The N-terminus does not have significant cross-program consensus for secondary structure.
The tools available at ExPASy were used to predict post-translational modification sites on C16orf95. [16] The following modifications are predicted: palmitoylation, phosphorylation, and O-linked glycosylation. Bolded residues in the table indicate sites that are conserved in more than one species.
| Predicted modification | Sites - Homo sapiens | Sites - Mus musculus | Sites - Canis lupus familiaris | Tool |
|---|---|---|---|---|
| Palmitoylation | C77, C80, C126, C178, C187 | C24, C41, C90 | C64, C113, C174 | CSS-Palm [17] |
| Phosphorylation | S6, S9, S53, T57, S68, S91, S111, T122, S166 | S30, S76, S89, S120, T134, S141 | S15, S35, T39, S153 | NetPhos 2.0 [18] |
| O-β-GlcNAc | S4, S6, S9, T57, S111 | None | None | NetOGlyc 4.0 [19] |
C16orf95 has a large number of amino acid changes over time, indicating it is a quickly evolving protein.
There are no proteins known to interact with C16orf95.
Deletions of C16orf95 have been associated with hydronephrosis, microcephaly, distichiasis, vesicoureteral reflux, and intellectual impairment. [21] [22] However, the deletions included coding regions of the following genes: F-box Protein 31 (FBXO31), Microtubule-Associated Protein 1 Light Chain 3 Beta (MAP1LC3B), and Zinc Finger CCHC Type 14 (ZCCHC14). The contributions of each of these genes to the observed phenotypes has yet to be scientifically determined.
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