TMEM271

Last updated
TMEM271
Identifiers
Aliases TMEM271 , transmembrane protein 271
External IDs GeneCards: TMEM271
Orthologs
SpeciesHumanMouse
Entrez

112441426

115490131

Ensembl

ENSG00000273238

n/a

UniProt

n
a

n/a

RefSeq (mRNA)

NM_001362796

XM_030254964

RefSeq (protein)

n/a

n/a

Location (UCSC) Chr 4: 0.57 – 0.58 Mb n/a
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse
Figure 1: Map of Chromosome 4 Map of Chromosome 4.png
Figure 1: Map of Chromosome 4

Transmembrane protein 271, or TMEM271 is a protein in Homo sapiens encoded by the TMEM271 gene, located at 4p16.3 on the minus strand. The protein is located on the plasma membrane of cells and highly expressed in several regions of the brain.

Contents

Gene

Locus

TMEM271 is located on chromosome 4 on the minus strand at 4p16.3, near the gene associated with Huntington's Disease. [4]

Figure 2: Conceptual translation of TMEM271. The conserved protein domains, motifs, and post-translational modifications are annotated and highlighted within the amino acid sequence. The mRNA sequence is aligned to the protein sequence. TMEM271 Conceptual Translation.pdf
Figure 2: Conceptual translation of TMEM271. The conserved protein domains, motifs, and post-translational modifications are annotated and highlighted within the amino acid sequence. The mRNA sequence is aligned to the protein sequence.

Size

The gene that encodes TMEM271 is 2,416 nucleotides long. [5] The coding sequence spans from nucleotides 234 to 1391. [4]

mRNA

Isoforms

The gene has one exon, and a single protein transcript is produced, no isoforms.

Protein

Characteristics

TMEM271 is 385 amino acids in length, and has a molecular weight of 39.1 kD. [6] It is a basic protein with an estimated isoelectric point is 9.55. [7] It is enriched in alanine, glycine, and arginine residues, and is deficient in methionine, asparagine, threonine, isoleucine, lysine, and glutamine residues. [8]

Domains and Motifs

TMEM271 has three transmembrane domains at residues 50 to 70, 121 to 141, and 219 to 239, and the first two of these are hydrophobic. [6] [8] An arginine-rich region from residues 248 to 294 correlates with positively charged sequence of the protein. [8]

Secondary Structure

Figure 3: The tertiary structure of the human TMEM271 protein has four alpha helices, as predicted by AlphaFold. Predicted Tertiary Structure of TMEM271.png
Figure 3: The tertiary structure of the human TMEM271 protein has four alpha helices, as predicted by AlphaFold.

AlphaFold predictive modeling shows four alpha helices located from residues 5 to 37, 45 to 71, 117 to 151, and 199 to 257. [9] These sequences generally align with the transmembrane regions.

Tertiary and Quaternary Structure

TMEM271 has type 3a topology, meaning that the N-terminus is in the extracellular space. [10] There are no disulfide bridges within the protein. The AlphaFold Database predicts that there are four alpha helices in the human TMEM271 protein. [7] [9]

Gene-Level Regulation

Figure 4: Schematic diagram of the human TMEM271 protein. The topology of the protein is depicted, as are the signal peptide, three transmembrane regions, and nuclear localization signal. PROTTER Diagram.pdf
Figure 4: Schematic diagram of the human TMEM271 protein. The topology of the protein is depicted, as are the signal peptide, three transmembrane regions, and nuclear localization signal.

Expression Pattern

TMEM271 mRNA is found to be expressed highly in the brain, and minimally in the adrenal gland and skin. Within the brain, the highest expression occurs in the cerebral cortex, followed by the hippocampus, amygdala, and basal ganglia. [5] TMEM271 is also included in the CADO-ES1 cell line, a human Ewing’s sarcoma cell line that functions in glutamate signaling, regulation of postsynaptic neurotransmitter receptors, and the biological process of learning. [5]

Protein-Level Regulation

Sub-cellular Location

The sub-cellular location of TMEM271 is predicted to be the plasma membrane, or another membranous organelle such as the endoplasmic reticulum. [11] There is a conserved pattern 7 nuclear localization sequence, with an amino acid sequence of PASRARR, at position 275.

Signal Peptide

There is a signal peptide at the N-terminus of the protein from residues 1 to 28 with a cleavage site at 28/29, [11] indicating that TMEM271 is a secretory protein and will be transferred to the endoplasmic reticulum during post-translational modification.

Post-Translational Modifications

There is a cAMP/cGMP dependent kinase (protein kinase A) phosphorylation site at residue 151, a casein kinase II (CK2) phosphorylation site at residue 147, and a protein kinase C (PKC) site at residue 4. There is one amidation site from residues 249 to 252. Lastly, there are two myristoylation sites at residues 7 to 12 and 131 to 136. [12]

Interacting Proteins

Figure 5: A table of human TMEM271 orthologs. TMEM271 Orthologs.pdf
Figure 5: A table of human TMEM271 orthologs.

TMEM271 has no directly interacting proteins. However, it is included in the CADO-ES1 cell line, an Ewing's sarcoma cell line, which functions in glutamate signaling, postsynaptic receptor regulation, and the learning process. One of the neighboring genes encodes another transmembrane proteins, TMEM114, which plays a role in eye development, and is highly expressed in the hypothalamus. [13]

Homology and Evolution

Orthologs

There are several orthologs for Homo sapiens TMEM271 within mammals, reptiles, aves, and both bony and cartilaginous fishes. Mammalian orthologs have high identity matches with H. sapiens, and are therefore considered strict orthologs. There are more distant orthologs, or homologs, within reptiles, aves, and fishes. The most distant ortholog is Callorhinchus milii, which dates back to 464 million years ago. [14]

Clinical Significance

The TMEM271 protein is not cancer prognostic, but has been detected in gliomas. [5] A study done in June of 2022 included a 17 year old patient with osteosarcoma who had a BRCA1 gene fusion with TMEM271. [15] Another study cited the TMEM271 gene as having increased expression in a tissue with resistance to SP, a lysine-specific demethylase-1 inhibitor drug used to treat Ewing’s Sarcoma. [16]

Related Research Articles

<span class="mw-page-title-main">TMEM242</span> Protein-coding gene in the species Homo sapiens

Transmembrane protein 242 (TMEM242) is a protein that in humans is encoded by the TMEM242 gene. The tmem242 gene is located on chromosome 6, on the long arm, in band 2 section 5.3. This protein is also commonly called C6orf35, BM033, and UPF0463 Transmembrane Protein C6orf35. The tmem242 gene is 35,238 base pairs long, and the protein is 141 amino acids in length. The tmem242 gene contains 4 exons. The function of this protein is not well understood by the scientific community. This protein contains a DUF1358 domain.

<span class="mw-page-title-main">FAM214A</span> Protein-coding gene in the species Homo sapiens

Protein FAM214A, also known as protein family with sequence similarity 214, A (FAM214A) is a protein that, in humans, is encoded by the FAM214A gene. FAM214A is a gene with unknown function found at the q21.2-q21.3 locus on Chromosome 15 (human). The protein product of this gene has two conserved domains, one of unknown function (DUF4210) and another one called Chromosome_Seg. Although the function of the FAM214A protein is uncharacterized, both DUF4210 and Chromosome_Seg have been predicted to play a role in chromosome segregation during meiosis.

<span class="mw-page-title-main">CCDC94</span> Protein found in humans

Coiled-coil domain containing 94 (CCDC94) is a protein that in humans is encoded by the CCDC94 gene. The CCDC94 protein contains a coiled-coil domain, a domain of unknown function (DUF572), an uncharacterized conserved protein (COG5134), and lacks a transmembrane domain.

<span class="mw-page-title-main">CCDC138</span> Protein found in humans

Coiled-coil domain-containing protein 138, also known as CCDC138, is a human protein encoded by the CCDC138 gene. The exact function of CCDC138 is unknown.

<span class="mw-page-title-main">EVI5L</span> Protein-coding gene in the species Homo sapiens

EVI5L is a protein that in humans is encoded by the EVI5L gene. EVI5L is a member of the Ras superfamily of monomeric guanine nucleotide-binding (G) proteins, and functions as a GTPase-activating protein (GAP) with a broad specificity. Measurement of in vitro Rab-GAP activity has shown that EVI5L has significant Rab2A- and Rab10-GAP activity.

C5orf34 is a protein that in humans is encoded by the C5orf34 gene (5p12).

TMEM156 is a gene that encodes the transmembrane protein 156 (TMEM156) in Homo sapiens. It has the clone name of FLJ23235.

<span class="mw-page-title-main">C3orf62</span> Protein

Chromosome 3 open reading frame 62 (C3orf62) is a protein that in humans is encoded by the C3orf62 gene. C3orf62 is a glycine-depleted protein relative to the amount of glycine in proteins in the rest of the genome. C3orf62 has a KKXX-like motif and is predicted to be localized in the nucleus. Expression of C3orf62 remains highest in whole blood.

<span class="mw-page-title-main">C17orf98</span> Protein-coding gene in the species Homo sapiens

C17orf98 is a protein which in humans is coded by the gene c17orf98. The protein is derived from Homo sapiens chromosome 17. The C17orf98 gene consists of a 6,302 base sequence. Its mRNA has three exons and no alternative splice sites. The protein has 154 amino acids, with no abnormal amino acid levels. C17orf98 has a domain of unknown function (DUF4542) and is 17.6kDa in weight. C17orf98 does not belong to any other families nor does it have any isoforms. The protein has orthologs with high percent similarity in mammals and reptiles. The protein has additional distantly related orthologs across the metazoan kingdom, culminating with the sponge family.

Uncharacterized protein Chromosome 1 Open Reading Frame 27 is a protein in humans, encoded by the C1orf27 gene. It is accession number NM_017847. This is a membrane protein that is 3926 base pairs long with the most extensive string of amino acids being 454aa long. C1orf27 exhibits cytoplasmic expression in epidermal tissues. Predicted associated biological processes of the gene include cell fate specification and developmental properties.

<span class="mw-page-title-main">TEX55</span> Protein-coding gene in the species Homo sapiens

Testis expressed 55 (TEX55) is a human protein that is encoded by the C3orf30 gene located on the forward strand of human chromosome three, open reading frame 30 (3q13.32). TEX55 is also known as Testis-specific conserved, cAMP-dependent type II PK anchoring protein (TSCPA), and uncharacterized protein C3orf30.

<span class="mw-page-title-main">SMCO3</span> Protein-coding gene in the species Homo sapiens

Single-pass membrane and coiled-coil domain-containing protein 3 is a protein that is encoded in humans by the SMCO3 gene.

<span class="mw-page-title-main">SMIM11</span>

Small integral membrane protein 11 is a protein which in humans is encoded by the SMIM11 gene.

<span class="mw-page-title-main">WD Repeat and Coiled Coil Containing Protein</span> Protein-coding gene in humans

WD Repeat and Coiled-coiled containing protein (WDCP) is a protein which in humans is encoded by the WDCP gene. The function of the protein is not completely understood, but WDCP has been identified in a fusion protein with anaplastic lymphoma kinase found in colorectal cancer. WDCP has also been identified in the MRN complex, which processes double-stranded breaks in DNA.

<span class="mw-page-title-main">SMIM19</span> Protein-coding gene in the species Homo sapiens

SMIM19, also known as Small Integral Membrane Protein 19, encodes the SMIM19 protein. SMIM19 is a confirmed single-pass transmembrane protein passing from outside to inside, 5' to 3' respectively. SMIM19 has ubiquitously high to medium expression with among varied tissues or organs. The validated function of SMIM19 remains under review because of on sub-cellular localization uncertainty. However, all linked proteins research to interact with SMIM19 are associated with the endoplasmic reticulum (ER), presuming SMIM19 ER association

<span class="mw-page-title-main">C2orf72</span> Human protein encoding gene

C2orf72 is a gene in humans that encodes a protein currently named after its gene, C2orf72. It is also designated LOC257407 and can be found under GenBank accession code NM_001144994.2. The protein can be found under UniProt accession code A6NCS6.

<span class="mw-page-title-main">C11orf98</span> Protein-coding gene in the species Homo sapiens

C11orf98 is a protein-encoding gene on chromosome 11 in humans of unknown function. It is otherwise known as c11orf48. The gene spans the chromosomal locus from 62,662,817-62,665,210. There are 4 exons. It spans across 2,394 base pairs of DNA and produces an mRNA that is 646 base pairs long.

<span class="mw-page-title-main">TEDDM1</span> Protein-coding gene in the species Homo sapiens

Transmembrane epididymal protein 1 is a transmembrane protein encoded by the TEDDM1 gene. TEDDM1 is also commonly known as TMEM45C and encodes 273 amino acids that contains six alpha-helix transmembrane regions. The protein contains a 118 amino acid length family of unknown function. While the exact function of TEDDM1 is not understood, it is predicted to be an integral component of the plasma membrane.

<span class="mw-page-title-main">C13orf46</span> C13of46 Gene and Protein

Chromosome 13 Open Reading Frame 46 is a protein which in humans is encoded by the C13orf46 gene. In humans, C13orf46 is ubiquitously expressed at low levels in tissues, including the lungs, stomach, prostate, spleen, and thymus. This gene encodes eight alternatively spliced mRNA transcript, which produce five different protein isoforms.

<span class="mw-page-title-main">TMEM248</span> Transmembrane protein 248/TMEM248 gene

Transmembrane protein 248, also known as C7orf42, is a gene that in humans encodes the TMEM248 protein. This gene contains multiple transmembrane domains and is composed of seven exons.TMEM248 is predicted to be a component of the plasma membrane and be involved in vesicular trafficking. It has low tissue specificity, meaning it is ubiquitously expressed in tissues throughout the human body. Orthology analyses determined that TMEM248 is highly conserved, having homology with vertebrates and invertebrates. TMEM248 may play a role in cancer development. It was shown to be more highly expressed in cases of colon, breast, lung, ovarian, brain, and renal cancers.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000273238 - 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 "Homo sapiens transmembrane protein 271 (TMEM271), mRNA". 2022-10-29.
  5. 1 2 3 4 "TMEM271 protein expression summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2022-12-08.
  6. 1 2 "transmembrane protein 271 precursor [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-12-08.
  7. 1 2 "ExPASy - Compute pI/Mw tool". web.expasy.org. Retrieved 2022-12-08.
  8. 1 2 3 "SAPS < Sequence Statistics < EMBL-EBI". www.ebi.ac.uk. Retrieved 2022-12-08.
  9. 1 2 "AlphaFold Protein Structure Database". alphafold.com. Retrieved 2022-12-08.
  10. ↑ "PredictProtein - Protein Sequence Analysis, Prediction of Structural and Functional Features". predictprotein.org. Retrieved 2022-12-08.
  11. 1 2 "PSORT II Prediction". psort.hgc.jp. Retrieved 2022-12-08.
  12. ↑ "Motif Scan". myhits.sib.swiss. Retrieved 2022-12-14.
  13. ↑ "TMEM114 protein expression summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2023-02-13.
  14. ↑ "TimeTree :: The Timescale of Life". timetree.org. Retrieved 2022-12-08.
  15. ↑ Meng F, Zhang Q, Pang F, Shi X (2022-06-15). "Abstract 5668: DNA damage response gene mutations and their association with PD-L1 expression in sarcoma and bone tumor". Cancer Research. 82 (12_Supplement): 5668. doi:10.1158/1538-7445.am2022-5668. ISSN   1538-7445. S2CID   249732129.
  16. ↑ Scarborough JA, McClure E, Anderson P, Dhawan A, Durmaz A, Lessnick SL, et al. (July 2020). "Identifying States of Collateral Sensitivity during the Evolution of Therapeutic Resistance in Ewing's Sarcoma". iScience. 23 (7): 101293. Bibcode:2020iSci...23j1293S. doi:10.1016/j.isci.2020.101293. PMC   7334607 . PMID   32623338.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.