Draft:TMEM141


Transmembrane protein 141 (TMEM141) is a protein which in humans is encoded by the TMEM141 gene.[1]

The predicted tertiary structure of the TMEM141 protein with the transmembrane domains highlighted in green.

It is a phenylalanine rich transmembrane protein found in the outer mitochondrial membrane.[2] It is well conserved in vertebrate species and has orthologs in multiple invertebrate species.

Gene

The TMEM141 gene is located on the long arm of chromosome 9 (9q34.3) between base pairs 136,791,344 and 136,793,317 on the plus strand. This gene contains five exons and four introns with no alternative splicing patterns.[1]

Expression

TMEM141 is expressed ubiquitously in human tissue at high rates. It is most expressed in the prostate, kidney, and thyroid glands with its lowest expression in skeletal muscle, the brain, and in lymphocytes.[3]

Protein

The TMEM141 protein has a length of 108 amino acids with no other isoforms.[4] It has a predicted molecular weight of 11.9 kilodaltons and a predicted isoelectric point of 8.69 which is similar across orthologs.[5] It is phenylalanine rich, containing an above average amount of phenylalanine, which is conserved across other mammal species. The TMEM141 protein is most abundant in heart and adrenal gland tissue.[6]

An annotated conceptual translation for the human TMEM141 protein

Transmembrane Domains

The TMEM141 protein contains two transmembrane domains, commonly predicted to be between amino acids 32 to 52 and 58 to 78.[4][7][8][9]

A prediction of the location of the transmembrane domains of TMEM141

Post Translational Modification

There is no experimental evidence of post-translational modification in the TMEM141 protein.[10] Protein sequence analysis tools have predicted there to be 6 unique phosphorylation sites, with the most commonly associated kinases being Case Kinase II and Protein Kinase C.[11][12]

Subcellular Localization

Experimental evidence has shown the TMEM141 protein to be localized in the outer mitochondrial membrane.[2] Predictive localization tools place the TMEM141 protein in both the endoplasmic reticulum and the mitochondria with high confidence.[13][7] Predictive tools used to detect signaling do not produce results for signal peptides or sequences.[14]

Homology

TMEM141 has orthologs conserved in mammals, marsupials, birds, some reptiles, fish, and some invertebrates. TMEM141 is noticeably missing from the marsupial orders Paucituberculata and Notoryctidae and invertebrate orders relating to worms such as; Nematoda, Hemichordata, and Annelida.[15]

Below is a table of orthologs of the human TMEM141 gene, varying from close to distant orthologs. The orthologs are listed in ascending order by date of divergence, sequence identity, and then sequence similarity if applicable.

Genus/Species Common Name Taxonomic Order Date of Divergence (MYA) Sequence Length (# Amino Acids) Sequence Identity (%) Sequence Similarity (%)
Homo sapiens Human Primates 0 108 100% 100%
Mus musculus Mouse Rodentia 87 108 81% 89%
Lynx rufus Bobcat Carnivora 94 108 81% 88%
Tamandua tetradactyla Southern tamandua Pilosa 99 108 86% 91%
Dromiciops gliroides Colocolo opossum Microbiotheria 160 126 74% 88%
Monodelphis domestica Gray short-tailed opossum Didelphimorphia 160 123 73% 88%
Sminthopsis crassicaudata Fat-tailed dunnart Dasyuromorphia 160 126 73% 86%
Notamacropus eugenii Tammar wallaby Diprotodontia 160 126 71% 85%
Eublepharis macularius Leopard gecko Squamata 319 129 73% 85%
Dermochelys coriacea Leatherback sea turtle Testudines 319 130 72% 86%
Alligator mississippiensis American alligator Crocodilia 319 130 58% 77%
Apteryx mantelli Brown kiwi Apterygiformes 319 164 64% 81%
Gavia stellata Red throated loon Gaviiforms 319 140 61% 81%
Colius striatus Speckled mousebird Coliiformes 319 138 61% 79%
Gallus gallus Chicken Galliformes 319 138 59% 81%
Rana temporaria Common frog Anura 352 128 64% 80%
Symphodus melops Corkwing wrasse Labriformes 429 125 67% 80%
Dicentrarchus labrax European seabass Acanthuriformes 429 125 66% 82%
Seriola aureovittata Yellowtail amberjack Carangiformes 429 125 66% 80%
Sebastes fasciatus Acadian redfish Perciformes 429 126 65% 81%
Danrio rerio Zebrafish Cypriniformes 429 124 58% 77%
Patiria miniata Bat star Valvatida 619 145 32% 57%
Haliotis rufescens Red abalone Lepetellida 686 118 40% 60%
Aedes aegypti Yellow fever mosquito Diptera 686 114 33% 51%
Lepisma saccharinum Silverfish Zygentoma 686 106 29% 45%
An unrooted phylogenetic tree of the TMEM141 protein showing both close and distant orthologs of the human TMEM141 protein.

Paralogs

There are no paralogs of the TMEM141 gene in the human genome.[15]

Clinical Significance

Academic literature has connected changes in TMEM141 to a few clinically significant conditions. When assessing genetic risk factors for suicide, one study found that variation in TMEM141 appeared in some pedigrees identified to have multiple individuals at high risk.[16] Another study found a loss of function variation in TMEM141 to possibly cause symptoms of neurodevelopmental disorders including a loss of motor function and lowered learning ability.[2]

References

  1. ^ a b TMEM141 Transmembrane Protein 141 [Homo Sapiens (Human)] - Gene - NCBI. https://www.ncbi.nlm.nih.gov/gene/85014. Accessed 4 June 2026.
  2. ^ a b c Sun, Liwei, et al. “Panoramic Variation Analysis of a Family with Neurodevelopmental Disorders Caused by Biallelic Loss-of-Function Variants in TMEM141, DDHD2, and LHFPL5.” Frontiers of Medicine, vol. 18, no. 1, Feb. 2024, pp. 81–97. Springer Link, https://doi.org/10.1007/s11684-023-1006-x.
  3. ^ GDS3113 / 211357. https://www.ncbi.nlm.nih.gov/geo/tools/profileGraph.cgi?ID=GDS3113:211357. Accessed 4 June 2026.
  4. ^ a b Transmembrane Protein 141 [Homo Sapiens] - Protein - NCBI. https://www.ncbi.nlm.nih.gov/protein/NP_116317.1. Accessed 4 June 2026.
  5. ^ Expasy - Compute pI/Mw Tool. https://web.expasy.org/compute_pi/. Accessed 4 June 2026.
  6. ^ PaxDb: Protein Abundance Database. https://pax-db.org/. Accessed 4 June 2026.
  7. ^ a b Almagro Armenteros, José Juan, et al. “DeepLoc: Prediction of Protein Subcellular Localization Using Deep Learning.” Bioinformatics, edited by John Hancock, vol. 33, no. 21, Nov. 2017, pp. 3387–95. DOI.org (Crossref), https://doi.org/10.1093/bioinformatics/btx431.
  8. ^ Omasits, Ulrich, et al. “Protter: Interactive Protein Feature Visualization and Integration with Experimental Proteomic Data.” Bioinformatics, vol. 30, no. 6, Mar. 2014, pp. 884–86. DOI.org (Crossref), https://doi.org/10.1093/bioinformatics/btt607
  9. ^ Klammt, Christian, et al. “Facile Backbone Structure Determination of Human Membrane Proteins by NMR Spectroscopy.” Nature Methods, vol. 9, no. 8, Aug. 2012, pp. 834–39. www.nature.com, https://doi.org/10.1038/nmeth.2033.
  10. ^ TMEM141 (Human). https://www.phosphosite.org/proteinAction.action?id=19092721&showAllSites=true. Accessed 4 June 2026.
  11. ^ Expasy - PROSITE. https://prosite.expasy.org/. Accessed 4 June 2026.
  12. ^ NetPhos 3.1 - DTU Health Tech - Bioinformatic Services. https://services.healthtech.dtu.dk/services/NetPhos-3.1/. Accessed 4 June 2026.
  13. ^ PSORT II Prediction. https://psort.hgc.jp/form2.html. Accessed 4 June 2026.
  14. ^ Teufel, Felix, et al. “SignalP 6.0 Predicts All Five Types of Signal Peptides Using Protein Language Models.” Nature Biotechnology, vol. 40, no. 7, July 2022, pp. 1023–25. DOI.org (Crossref), https://doi.org/10.1038/s41587-021-01156-3.
  15. ^ a b BLAST: Basic Local Alignment Search Tool. https://blast.ncbi.nlm.nih.gov/Blast.cgi. Accessed 4 June 2026.
  16. ^ Coon, H., et al. “Genetic Risk Factors in Two Utah Pedigrees at High Risk for Suicide.” Translational Psychiatry, vol. 3, no. 11, Nov. 2013, pp. e325–e325. www.nature.com, https://doi.org/10.1038/tp.2013.100.

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