Transmembrane protein 217

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Transmembrane Protein 217 is a protein encoded by the gene TMEM217. TMEM217 has been found to have expression correlated with the lymphatic system and endothelial tissues and has been predicted to have a function linked to the cytoskeleton. [1] [2] [3]

Contents

Gene

TMEM217 is located on the chromosome 6 minus strand at 6p21.2. [4] The gene consists of 46,857 base pairs and is flanked by TBC1D22B (TBC1 Domain Family Member 22B) and PIM1. [4] [5] It was previously known as C6orf128 (Chromosome 6 open reading frame 128). [4]

mRNA

TMEM217 has three common isoforms formed from the alternative splicing of three exons. Isoform 1 translates for the longest polypeptide, consisting of 1590 nucleotides. [6] The 5’ un-translated region of isoform 1 is relatively short and is predicted to fold into several stem loop domains within conserved areas of the un-translated region. [7]

Protein

Primary Protein Sequence

The longest polypeptide of transmembrane protein 217 consists of 229 amino acids. [8] This protein isoform has a predicted weight of 26.6 kDa and isoelectric point at a pH of 9.3. [9] [10] It is notably rich in isoleucine and phenylalanine, and deficient in alanine, aspartate, and proline compared to other proteins. [11] Transmembrane protein 217 contains the domain of unknown function, DUF4534, between amino acids 11-171. [12]

Secondary Structure

Transmembrane protein 217 is predicted to have four transmembrane domains. [8] [13] These transmembrane domains consist primarily of uncharged amino acids in predicted alpha helices. [11] [14] The N-terminus and C-terminus of the protein are predicted to be facing the cytosol with the C-terminus containing a long predicted coiled tail extending from the final transmembrane domain. [13]

Post-Translational Modifications

There are several predicted phosphorylation and glycosylation sites on transmembrane protein 217 in highly conserved parts of the protein, where the phosphorylation sites are located primarily on the C-terminal tail. [15] [16] [17] There are also two highly conserved cysteine residues, which have the potential to form a disulfide bond in the extracellular space between the first and second transmembrane domains.

The image depicts a conceptual diagram of transmembrane protein 217. The protein is given from N-terminus to C-terminus with predicted cellular, transmembrane and extracellular domains present (colored blue, grey, and orange respectively). The most highly conserved predicted post-translational modifications are provided as well. The following predicted post-translational modifications are provided: phosphorylation sites, disulfide bond, and a C-linked mannosylation. Transmembrane 217 Conceptual Protein.svg
The image depicts a conceptual diagram of transmembrane protein 217. The protein is given from N-terminus to C-terminus with predicted cellular, transmembrane and extracellular domains present (colored blue, grey, and orange respectively). The most highly conserved predicted post-translational modifications are provided as well. The following predicted post-translational modifications are provided: phosphorylation sites, disulfide bond, and a C-linked mannosylation.

Expression

TMEM217 is not ubiquitously expressed. The gene tends to have expression correlated to lymphatic system, vascular/arterial endothelial tissue, and notable expression in the bladder based on expression profiles and microarray analysis. [1] [2] Other tissues that have been shown to express TMEM217 include: connective tissues, the liver, mammary glands, the testis, and the cervix. [1] Co-expression analyses have found that TMEM217 was up-regulated in response to mechanical stretch in dermal fibroblast cells and in response to the resveratrol derivative, DMU-212, in vascular endothelial tissues. [3] [18]

Function

No known function has been attributed to TMEM217, however a co-expression analysis in dermal fibroblasts has predicted the protein to have a potential association with the cytoskeleton. [3]

Clinical Significance

Single nucleotide polymorphisms in TMEM217 have been linked to Alzheimer’s disease and diabetic retinopathy. [19] [20] TMEM217 was also found to have similar expression patterns as TRPM2, a biomarker linked to breast carcinoma. [21] Expression profiles have also linked elevated TMEM217 expression to bladder cancer and lymphoma. [1]

Homology

TMEM217 was found to have orthologs in organisms as early as the scaled fish, which diverged 420 million years ago. [22] Although found in organisms as early as fish and reptiles, TMEM217 has no known orthologs in any bird species. [23] [24]

TMEM217 has no known paralogs.

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References

  1. 1 2 3 4 "EST Profile-TMEM217-Transmembrane Protein 217". National Center for Biotechnology Information. NCBI.
  2. 1 2 "GEO Profiles-TMEM217". National Center for Biotechnology Information. NCBI.
  3. 1 2 3 Reichenbach, M.; Reimann, K.; Reuter, H. (2014). "Gene expression in response to cyclic mechanical stretch in primary human dermal fibroblasts". Genomics Data. 2: 335–9. doi:10.1016/j.gdata.2014.09.010. PMC   4535970 . PMID   26484124.
  4. 1 2 3 "TMEM217 Gene". GeneCards.
  5. ↑ "TMEM217 Transmembrane Protein 217 [Homo Sapiens (human)]-Gene-NCBI". National Center for Biotechnology Information. NCBI.
  6. ↑ "Homo Sapiens Transmembrane Protein 217 (TMEM217), Transcript Variant 1, mRNA". National Center for Biotechnology Information. NCBI. 17 September 2018.
  7. ↑ Zuker, M (2003). "Mfold web server for nucleic acid folding and hybridization prediction". Nucleic Acids Research. 13 (31): 3406–3415. doi:10.1093/nar/gkg595. PMC   169194 . PMID   12824337.
  8. 1 2 "Transmembrane Protein 217 Isoform 1 [Homo Sapiens] - Protein - NCBI". National Center for Biotechnology Information. NCBI.
  9. ↑ Kramer, Jack. "AASTATS". Biology Workbench. San Diego Supercomputer Center.
  10. ↑ Toldo, Luca. "Isoelectric Point Determination". Biology Workbench. San Diego Supercomputer Center.
  11. 1 2 Brendel, V.; Bucher, P.; Nourbakhsh, I.R.; Blaisdell, B.E.; Karlin, S. (1992). "Methods and algorithms for statistical analysis of protein sequences". Proceedings of the National Academy of Sciences. 89 (6): 2002–2006. Bibcode:1992PNAS...89.2002B. doi: 10.1073/pnas.89.6.2002 . PMC   48584 . PMID   1549558.
  12. ↑ Marchler-Baur, A.; Bo, Y.; Han, L.; He, J; Lanczycki, C.J. (2017). "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures". Nucleic Acids Research. 45 (D1): D200–D203. doi: 10.1093/nar/gkw1129 . PMC   5210587 . PMID   27899674.
  13. 1 2 "Predict Location of Transmembrane Helices and Location of Intervening Loop Regions". Biology Workbench. San Diego Supercomputer Center.
  14. ↑ Chou, P. Y.; Fasman, G. D. (1978). "Prediction of the secondary structure of proteins from their amino acid sequence". Advances in Enzymology. 47: 45–148.
  15. ↑ Blom, N.; Sicheritz, T.; Gupta, R.; Gammeltoft, S.; Brunak, S. (2004). "Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence". Proteomics. 4 (6): 1633–1649. doi:10.1002/pmic.200300771. PMID   15174133. S2CID   18810164.
  16. ↑ "Motif Scan". MyHits. ExPasy.
  17. ↑ Gupta, R.; Jung, E.; Brunak, S. "Prediction of N-glycosylation sites in human proteins". NetNGlyc 1.0 Server. Center for Biological Sequence Analysis.
  18. ↑ Miao, Y.; Cui, L.; Chen, Z.; Zhang, L (2016). "Gene expression profiling of DMU-212-induced apoptosis and anti-angiogenesis in vascular endothelial cells". Pharmaceutical Biology. 54 (4): 660–666. doi: 10.3109/13880209.2015.1071414 . PMID   26428916.
  19. ↑ Floudas, C. S.; Um, N.; Kamboh, M. I.; Barmada, M. M.; Visweswaran, S. (2014). "Identifying genetic interactions associated with late-onset Alzheimer's disease". BioData Mining. 7 (1): 35. doi:10.1186/s13040-014-0035-z. PMC   4300162 . PMID   25649863.
  20. ↑ Lin, H.; Huang, Y.; Lin, J.; Wu, J. (2013). "Association of Genes on Chromosome 6, GRIK2, TMEM217 and TMEM63B (Linked to MRPL14) with Diabetic Retinopathy". Ophthalmologica. 229 (1): 54–60. doi:10.1159/000342616. PMID   23037145. S2CID   20024729.
  21. ↑ Sumoza-Toledo, A.; Espinoza-Gabriel, M.; Montiel-Condado, D. (2016). "Evaluation of the TRPM2 channel as a biomarker in breast cancer using public databases analysis". Boletín Médico del Hospital Infantil de México. 73 (6): 397–404. doi: 10.1016/j.bmhime.2017.11.038 . PMID   29421284.
  22. ↑ "TimeTree".
  23. ↑ Altschul, S.F.; Gish, W.; Miller, W.; Meyers, E.W.; Lipman, D.J. (1990). "Basic local alignment search tool". Molecular Biology. 215 (3): 403–410. doi:10.1006/jmbi.1990.9999. PMID   2231712.
  24. ↑ Kent, W.J. (2002). "BLAT- the BLAST-like alignment tool". Genome Research. 12 (4): 656–664. doi:10.1101/gr.229202. PMC   187518 . PMID   11932250.
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