Transmembrane protein 217

TMEM217
Identifiers
AliasesTMEM217, C6orf128, dJ355M6.2, transmembrane protein 217
External IDsMGI: 3646280; GeneCards: TMEM217
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

221468

71138

Ensembl

ENSG00000172738

ENSMUSG00000079580

UniProt

Q8N7C4

Q14AF1

RefSeq (mRNA)

NM_001162901
NM_001162902

RefSeq (protein)

NP_001156372
NP_001273330
NP_660359

NP_001156373
NP_001156374

Location (UCSC)n/aChr 17: 29.74 – 29.77 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

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.[4][5][6]

Gene

TMEM217 is located on the chromosome 6 minus strand at 6p21.2.[7] The gene consists of 46,857 base pairs and is flanked by TBC1D22B (TBC1 Domain Family Member 22B) and PIM1.[7][8] It was previously known as C6orf128 (Chromosome 6 open reading frame 128).[7]

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.[9] 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.[10]

Protein

Primary protein sequence

The longest polypeptide of transmembrane protein 217 consists of 229 amino acids.[11] This protein isoform has a predicted weight of 26.6 kDa and isoelectric point at a pH of 9.3.[12][13] It is notably rich in isoleucine and phenylalanine, and deficient in alanine, aspartate, and proline compared to other proteins.[14] Transmembrane protein 217 contains the domain of unknown function, DUF4534, between amino acids 11-171.[15]

Secondary structure

Transmembrane protein 217 is predicted to have four transmembrane domains.[11][16] These transmembrane domains consist primarily of uncharged amino acids in predicted alpha helices.[14][17] 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.[16]

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.[18][19][20] 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.[4][5] Other tissues that have been shown to express TMEM217 include: connective tissues, the liver, mammary glands, the testis, and the cervix.[4] 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.[6][21]

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.[6]

Clinical significance

Single nucleotide polymorphisms in TMEM217 have been linked to Alzheimer’s disease and diabetic retinopathy.[22][23] TMEM217 was also found to have similar expression patterns as TRPM2, a biomarker linked to breast carcinoma.[24] Expression profiles have also linked elevated TMEM217 expression to bladder cancer and lymphoma.[4]

Homology

TMEM217 was found to have orthologs in organisms as early as the scaled fish, which diverged 420 million years ago.[25] Although found in organisms as early as fish and reptiles, TMEM217 has no known orthologs in any bird species.[26][27]

TMEM217 has no known paralogs.

References

  1. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000079580 – Ensembl, May 2017
  2. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. 1 2 3 4 "EST Profile-TMEM217-Transmembrane Protein 217". National Center for Biotechnology Information. NCBI.
  5. 1 2 "GEO Profiles-TMEM217". National Center for Biotechnology Information. NCBI.
  6. 1 2 3 Reichenbach M, Reimann K, Reuter H (December 2014). "Gene expression in response to cyclic mechanical stretch in primary human dermal fibroblasts". Genomics Data. 2: 335–339. doi:10.1016/j.gdata.2014.09.010. PMC 4535970. PMID 26484124.
  7. 1 2 3 "TMEM217 Gene". GeneCards.
  8. ↑ "TMEM217 Transmembrane Protein 217 [Homo Sapiens (human)]-Gene-NCBI". National Center for Biotechnology Information. NCBI.
  9. ↑ "Homo Sapiens Transmembrane Protein 217 (TMEM217), Transcript Variant 1, mRNA". National Center for Biotechnology Information. NCBI. 17 September 2018.
  10. ↑ Zuker M (July 2003). "Mfold web server for nucleic acid folding and hybridization prediction". Nucleic Acids Research. 31 (13): 3406–3415. doi:10.1093/nar/gkg595. PMC 169194. PMID 12824337.
  11. 1 2 "Transmembrane Protein 217 Isoform 1 [Homo Sapiens] - Protein - NCBI". National Center for Biotechnology Information. NCBI.
  12. ↑ Kramer J. "Aastats". Biology Workbench. San Diego Supercomputer Center.
  13. ↑ Toldo L. "Isoelectric Point Determination". Biology Workbench. San Diego Supercomputer Center.
  14. 1 2 Brendel V, Bucher P, Nourbakhsh IR, Blaisdell BE, Karlin S (March 1992). "Methods and algorithms for statistical analysis of protein sequences". Proceedings of the National Academy of Sciences of the United States of America. 89 (6): 2002–2006. Bibcode:1992PNAS...89.2002B. doi:10.1073/pnas.89.6.2002. PMC 48584. PMID 1549558.
  15. ↑ Marchler-Bauer A, Bo Y, Han L, He J, Lanczycki CJ, Lu S, et al. (January 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.
  16. 1 2 Workbench NB. "Predict Location of Transmembrane Helices and Location of Intervening Loop Regions". Biology Workbench. San Diego Supercomputer Center.
  17. ↑ Chou PY, Fasman GD (1978). "Prediction of the secondary structure of proteins from their amino acid sequence". Advances in Enzymology. 47: 45–148.
  18. ↑ Blom N, Sicheritz-Pontén T, Gupta R, Gammeltoft S, Brunak S (June 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.
  19. ↑ "Motif Scan". MyHits. ExPasy.
  20. ↑ Gupta R, Jung E, Brunak S. "Prediction of N-glycosylation sites in human proteins". NetNGlyc 1.0 Server. Center for Biological Sequence Analysis.
  21. ↑ 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.
  22. ↑ Floudas CS, Um N, Kamboh MI, Barmada MM, 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.
  23. ↑ Lin HJ, Huang YC, Lin JM, Wu JY, Chen LA, Tsai FJ (2013). "Association of genes on chromosome 6, GRIK2 , TMEM217 and TMEM63B (linked to MRPL14 ) with diabetic retinopathy". Ophthalmologica. Journal International D'ophtalmologie. International Journal of Ophthalmology. Zeitschrift Fur Augenheilkunde. 229 (1): 54–60. doi:10.1159/000342616. PMID 23037145. S2CID 20024729.
  24. ↑ Sumoza-Toledo A, Espinoza-Gabriel MI, Montiel-Condado D (2016). "Evaluation of the TRPM2 channel as a biomarker in breast cancer using public databases analysis". Boletin Medico Del Hospital Infantil De Mexico. 73 (6): 397–404. doi:10.1016/j.bmhime.2017.11.038. PMID 29421284.
  25. ↑ "TimeTree".
  26. ↑ Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (October 1990). "Basic local alignment search tool". Journal of Molecular Biology. 215 (3): 403–410. doi:10.1006/jmbi.1990.9999. PMID 2231712.
  27. ↑ Kent WJ (April 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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