Biology: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]

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.

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.

References

  1. ↑ 1.0 1.1 1.2 1.3 "EST Profile-TMEM217-Transmembrane Protein 217". NCBI. https://www.ncbi.nlm.nih.gov/UniGene/ESTProfileViewer.cgi?uglist=Hs.520101. 
  2. ↑ 2.0 2.1 "GEO Profiles-TMEM217". NCBI. https://www.ncbi.nlm.nih.gov/geoprofiles?LinkName=gene_geoprofiles&from_uid=221468. 
  3. ↑ 3.0 3.1 3.2 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. PMID 26484124. 
  4. ↑ 4.0 4.1 4.2 "TMEM217 Gene". https://www.genecards.org/cgi-bin/carddisp.pl?gene=TMEM217. 
  5. ↑ "TMEM217 Transmembrane Protein 217 [Homo Sapiens (human)-Gene-NCBI"]. NCBI. https://www.ncbi.nlm.nih.gov/gene/221468. 
  6. ↑ Homo Sapiens Transmembrane Protein 217 (TMEM217), Transcript Variant 1, mRNA. NCBI. 17 September 2018. https://www.ncbi.nlm.nih.gov/nuccore/NM_145316.3. 
  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. PMID 12824337. 
  8. ↑ 8.0 8.1 "Transmembrane Protein 217 Isoform 1 [Homo Sapiens - Protein - NCBI"]. NCBI. https://www.ncbi.nlm.nih.gov/protein/NP_001156372.1. 
  9. ↑ Kramer, Jack. "AASTATS". San Diego Supercomputer Center. http://workbench.sdsc.edu/. 
  10. ↑ Toldo, Luca. "Isoelectric Point Determination". San Diego Supercomputer Center. http://workbench.sdsc.edu/. 
  11. ↑ 11.0 11.1 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. doi:10.1073/pnas.89.6.2002. PMID 1549558. PMC 48584. Bibcode: 1992PNAS...89.2002B. http://workbench.sdsc.edu/. 
  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. PMID 27899674. 
  13. ↑ 13.0 13.1 "Predict Location of Transmembrane Helices and Location of Intervening Loop Regions". San Diego Supercomputer Center. http://workbench.sdsc.edu/. 
  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. http://workbench.sdsc.edu/. 
  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. http://www.cbs.dtu.dk/services/NetPhos/. 
  16. ↑ "Motif Scan". ExPasy. http://myhits.isb-sib.ch/cgi-bin/motif_scan. 
  17. ↑ Gupta, R.; Jung, E.; Brunak, S.. "Prediction of N-glycosylation sites in human proteins". Center for Biological Sequence Analysis. http://www.cbs.dtu.dk/services/NetNGlyc/. 
  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. 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. 
  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". http://www.timetree.org/. 
  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. PMID 11932250. 



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