TMEM106C

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

TMEM106C is a gene that encodes the transmembrane protein 106C (TMEM106C) in Homo sapiens It has been found to be overexpressed in cancer cells and also is related to distal arthrogryposis,{{cite journal|date= 16 May 2006|title= Radiation Hybrid Mapping of 18 Positional and Physiological Candidate Genes for Arthrogryposis Multiplex Congenita on Porcine Chromosome 5. |author= Genini, S.|doi=10.1111/j.1365-2052.2006.01447.x|pmid= 16734683 |volume=37|issue = 3|journal=Animal Genetics|pages=239–244}}{{cite web|url=https://www.genecards.org/cgi-bin/carddisp.pl?gene=TMEM106C | title=Genecards | publisher= The Human Gene Compendium}} a condition of stiff joints and irregular muscle development. The TMEM106C gene contains a domain of unknown function, DUF1356, that spans most of the protein. Transmembrane protein 106C also goes by the aliases MGC5576 or MGC111210, LOC79022.{{cite web|url= https://www.ncbi.nlm.nih.gov/ieb/research/acembly/av.cgi?db=human&term=TMEM106C&submit=Go|date= 2 Jun 2010 |title= Homo sapiens complex locus TMEM106C, encoding transmembrane protein 106C|author=Thierry-Mieg, Danielle and Jean |publisher= Aceview National Center for BioInformation technology, National Library of Medicine, National Institutes of Health}}

Location and gene neighborhood

The TMEM106C gene is located on the long arm of the 12th chromosome. It is found at position 12q13.1. This gene spans from 48357225 to 48362667 on chromosome 12. This gene is in between COL2A1, the human type II collagen gene, and VDR, the human Vitamin D Receptor gene.{{cite web|url= https://www.ncbi.nlm.nih.gov/gene/79022|date= 4 May 2014 |title= TMEM106C transmembrane protein 106C Homo sapiens (human)|publisher= NCBI}}

This protein is found to be an integral part of the endoplasm reticulum membrane.{{cite web|url= http://psort.hgc.jp/form2.html|date= 19 Nov 1999|title= PSORT II Prediction |author= Nakai, K.}}

Protein structure

File:Protein Structure (2).png The TMEM106A protein has a molecular weight of 27.9 kdal with a PI of 6.325.{{cite web|url= http://workbench.sdsc.edu/ |date=11 May 2011 |title= Biology Workbench 3.2|publisher= SDSC: San Diego SuperComputer Center}} It has 250 amino acids, 230 of which are in the domain of unknown function. No signal peptide has been found for this protein but TMEM106C has transmembrane regions which gives evidence for an internal signal peptide.{{cite web|url= http://www.cbs.dtu.dk/services/TMHMM-2.0/|date= 12 Jun 2013|title= TMHMM Server v 2.0|author= Krogh, Anders}} This protein spans the ER membrane 2 times. There is evidence that these transmembrane regions take on helical structures.{{cite web|url= http://www.enzim.hu/hmmtop/|date= 2001|title= HMMTop: Prediction of transmembrane helices and topology of proteins v 2.0|author= Tusnady, G.E.}} The predicted structure of the protein is shown to the left:

TMEM106C is valine-rich with no tryptophan.

There are several areas for post-translational modification for TMEM106A including:{{cite journal|url= http://www.expasy.org/proteomics/post-translational_modification|date= 2012|title= ExPASy: SIB bioinformatics resource portal|publisher= Nucleic Acids Res, 40(W1):W597-W603|vauthors=Artimo P, Jonnalagedda M, Arnold K, Baratin D, Csardi G, de Castro E, Duvaud S, Flegel V, Fortier A, Gasteiger E, Grosdidier A, Hernandez C, Ioannidis V, Kuznetsov D, Liechti R, Moretti S, Mostaguir K, Redaschi N, Rossier G, Xenarios I, Stockinger H |journal= Nucleic Acids Research|volume= 40|issue= Web Server issue|pages= W597-603|pmid= 22661580|doi= 10.1093/nar/gks400|pmc= 3394269}}

:* Phosphorylation{{cite journal | vauthors = Blom N, Gammeltoft S, Brunak S | title = Sequence and structure-based prediction of eukaryotic protein phosphorylation sites | journal = Journal of Molecular Biology | volume = 294 | issue = 5 | pages = 1351–62 | date = December 1999 | pmid = 10600390 | doi = 10.1006/jmbi.1999.3310 }}

:* Kinase-Specific Phosphoylation{{cite web|url= http://gps.biocuckoo.org/|date= 10 Aug 2012|title= Tool to Predict Kinase-specific Phosphorylation Sites in Hierarchy|publisher= GPS |author1=Yu Xue |author2=Jian Ren |author3=Xinjiao Gao |author4=Changjiang Jin |author5=Longping Wen |author6=Xuebiao Yao |name-list-style=amp }}

:* N-glycosylation{{cite web|url= http://www.cbs.dtu.dk/services/NetNGlyc/|date= 2004|title= Prediction of N-glycosylation sites in human proteins|publisher= NetNGlyc 1.0 Server|author1=R. Gupta, E. Jung |author2=S. Brunak. |name-list-style=amp }}

Expression

This gene is highly expressed. TMEM106C is expressed 4.9 times the average gene. TMEM106C has ubiquitous expression. It can be found expressed in many tissues types. Tissue types with high expression included the adrenal gland, eye, reproductive organs, cervix and blood. High expression was found using EST and GEO data.

File:Expression Patterns.png

This gene is also found overexpressed in cancer cells. This gene has found to be expressed three times more in adrenal tumor and twice more in bladder carcinoma and retinoblastoma than normal expression. File:Expression Patterns -cancer.png It is also found to be highly expressed in breast (mammary gland) tumor, cervical tumor, esophageal tumor, leukemia, liver tumor; lung tumor, pancreatic tumor, prostate cancer, and soft tissue/muscle tissue tumor.{{cite web|url= http://www.itb.cnr.it/breastcancer/php/geneReport.php?id=79022|date= 3 Jul 2010 |title= TMEM106C |vauthors=Mosca E, Alfieri R, Merelli I, Viti F, Calabria A, Milanesi L |publisher= Genes to Systems Breast Cancer Database}}

TMEM106C is found in all stages of development from embryoid body, blastocyst, fetus, infant, juvenile and adult.{{cite web|url= https://www.ncbi.nlm.nih.gov/UniGene/ESTProfileViewer.cgi?uglist=Hs.596726|date= 28 Oct 2009|title= TMEM106C: Transmembrane protein 106C |publisher= EST profile. First Gov. Health and Human Services}}

Homology

= Paralogs =

There are two paralogs for TMEM106C. These paralogs are TMEM106A and TMEM106B. Both genes are found highly conserved in Mammalia. TMEM106A is also found to be conserved in invertebrates as well. The protein was found in tapeworms and other invertebrate worms.{{cite web|url= http://blast.st-va.ncbi.nlm.nih.gov/Blast.cgi|date= 2014|title= BLAST|publisher= National Center for Biotechnology Information. National Library of Medicine}}

class="wikitable"
ProteinAccession numberAmino acidsIdentity percent
TMEM106A[https://www.ncbi.nlm.nih.gov/protein/AAI46977.1 AAI46977]26236
TMEM106B[https://www.ncbi.nlm.nih.gov/protein/NP_001127704.1 NP_001127704]27443
TMEM106C[https://www.ncbi.nlm.nih.gov/protein/NP_001137314.1 NP_001137314.1]250100

= Orthologs =

TMEM106C is highly conserved in Mammalia. Links to sequences can be found in the table below:

class="wikitable sortable"
OrganismCommon nameAccession numberAmino acidsIdentity percentNotes
Homo sapiensHuman[https://www.ncbi.nlm.nih.gov/protein/NP_001137314.1 NP_001137314.1]250100Mammal
Macaca mulattaRhesus macaque[https://www.ncbi.nlm.nih.gov/protein/NP_001253653.1 NP_001253653.1]24998Mammal
Equus caballusHorse[https://www.ncbi.nlm.nih.gov/protein/XP_001490277.1 XP_001490277.1]24990Mammal
Mus musculusMouse[https://www.ncbi.nlm.nih.gov/protein/NP_001239082.1 NP_001239082.1]26079Mammal
Alligator mississippiensisAmerican alligator[https://www.ncbi.nlm.nih.gov/protein/XP_006273403.1 XP_006273403.1]27177Reptile
Chrysemys picta belliiPainted turtle[https://www.ncbi.nlm.nih.gov/protein/XP_005291963.1 XP_005291963.1]27073Reptile
Falco cherrugSaker falcon[https://www.ncbi.nlm.nih.gov/protein/XP_005436184.1 XP_005436184.1]27474Aves
Gallus gallusChicken[https://www.ncbi.nlm.nih.gov/protein/XP_003643471.1 XP_003643471.1]25365Aves
Xenopus tropicalisWestern clawed frog[https://www.ncbi.nlm.nih.gov/protein/NP_001016848.1 NP_001016848.1]26364Amphibia
Latimeria chalumnaeCoelacanth[https://www.ncbi.nlm.nih.gov/protein/XP_005986345.1 XP_005986345.1]25861Actinoterygii
Danio rerioZebrafish[https://www.ncbi.nlm.nih.gov/protein/NP_001070764.1 NP_001070764.1]27557Actinoterygii

References

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