TANGO2

TANGO2
Identifiers
Aliases TANGO2, C22orf25, MECRCN, transport and golgi organization 2 homolog
External IDs MGI: 101825 HomoloGene: 44029 GeneCards: TANGO2
Orthologs
Species Human Mouse
Entrez

128989

27883

Ensembl

ENSG00000183597

n/a

UniProt

Q6ICL3

P54797

RefSeq (mRNA)

NM_138583

RefSeq (protein)

n/a

Location (UCSC) Chr 22: 20.02 – 20.07 Mb Chr 16: 18.3 – 18.35 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Transport and golgi organization 2 homolog (TANGO2) also known as chromosome 22 open reading frame 25 (C22orf25) is a protein that in humans is encoded by the TANGO2 gene.

The function of C22orf25 is not currently known. It is characterized by the NRDE superfamily domain (DUF883), which is strictly known for the conserved amino acid sequence of (N)-Asparagine (R)-Arginine (D)-Aspartic Acid (E)-Glutamic Acid. This domain is found among distantly related species from the six kingdoms:[3] Eubacteria, Archaebacteria, Protista, Fungi, Plantae, and Animalia and is known to be involved in Golgi organization and protein secretion.[4] It is likely that it localizes in the cytoplasm but is anchored in the cell membrane by the second amino acid.[5][6] C22orf25 is also xenologous to T10 like proteins in the Fowlpox Virus and Canarypox Virus. The gene coding for C22orf25 is located on chromosome 22 and the location q11.21, so it is often associated with 22q11.2 deletion syndrome.[7]

Protein

Gene Size Protein Size # of exons Promoter Sequence Signal Peptide Molecular Weight Domain Length
2271 bp 276 aa 9[8] 687 bp No[9] 30.9 kDa[10] 270 aa

Gene neighborhood

The C22orf25 gene is located on the long arm (q) of chromosome 22 in region 1, band 1, and sub-band 2 (22q11.21) starting at 20,008,631 base pairs and ending at 20,053,447 base pairs.[7] There is a 1.5-3.0 Mb deletion containing around 30-40 genes, spanning this region that causes the most survivable genetic deletion disorder known as 22q11.2 deletion syndrome, which is most commonly known as DiGeorge syndrome or Velocaridofacial syndrome.[11][12] 22q11.2 deletion syndrome has a vast array of phenotypes and is not attributed to the loss of a single gene. The vast phenotypes arise from deletions of not only DiGeorge Syndrome Critical Region (DGCR) genes and disease genes but other unidentified genes as well.[13]

C22orf25 is in close proximity to DGCR8 as well as other genes known to play a part in DiGeorge Syndrome such as armadillo repeat gene deleted in Velocardiofacial syndrome (ARVCF), Cathechol-O-methyltransferase (COMT) and T-box 1 (TBX1).[14][15]

Predicted mRNA features

Promoter

The promoter for the C22orf25 gene spans 687 base pairs from 20,008,092 to 20,008,878 with a predicted transcriptional start site that is 104 base pairs and spans from 20,008,591 to 20,008,694.[16] The promoter region and beginning of the C22orf25 gene (20,008,263 to 20,009,250) is not conserved past primates. This region was used to determine transcription factor interactions.

Transcription factors

Some of the main transcription factors that bind to the promoter are listed below.[17]

Reference Detailed Family Information Start (amino acid) End (amino acid) Strand
XBBF X-box binding factors 227 245 -
GCMF Chorion-specific transcription factors (with a GCM DNA binding domain) 151 165 -
YBXF Y-box binding transcription factors 158 170 -
RUSH SWI/SNF related nucleophosphoproteins (with a RING finger binding motif) 222 232 -
NEUR NeuroD, Beta2, HLH domain 214 226 -
PCBE PREB core-binding element 148 162 -
NR2F Nuclear receptor subfamily 2 factors 169 193 -
AP1R MAF and AP1 related factors 201 221 -
ZF02 C2H2 zinc finger transcription factors 2 108 130 -
TALE TALE homeodomain class recognizing TG motifs 216 232 -
WHNF Winged helix transcription factors 271 281 -
FKHD Forkhead domain factors 119 135 +
MYOD Myoblast determining factors 218 234 +
AP1F AP1, activating protein 1 118 130 +
BCL6 POZ domain zinc finger expressed in B cells 190 206 +
CARE Calcium response elements 196 206 +
EVI1 EVI1 nuclear transcription factor 90 106 +
ETSF ETS transcription factor 162 182 +
TEAF TEA/ATTS DNA binding domain factors 176 188 +

Expression analysis

Expression data from Expressed Sequence Tag mapping, microarray and in situ hybridization show high expression for Homo sapiens in the blood, bone marrow and nerves.[18][19][20] Expression is not restricted to these areas and low expression is seen elsewhere in the body. In Caenorhabditis elegans, the snt-1 gene (C22orf25 homologue) was expressed in the nerve ring, ventral and dorsal cord processes, sites of neuromuscular junctions, and in neurons.[21]

Evolutionary history

The NRDE (DUF883) domain, is a domain of unknown function spanning majority of the C22orf25 gene and is found among distantly related species, including viruses.

Genus and Species Common Name Accession Number Seq.
Length
Seq.
Identity
Seq.
Similarity
Kingdom Time of Divergence
Homo sapienshumansNP_690870.3276aa--Animalia-
Pan troglodytescommon chimpanzeeBAK62258.1276aa99%100%Animalia6.4 mya
Ailuropoda melanoleucagiant pandaXP_002920626276aa91%94%Animalia94.4 mya
Mus musculushouse mouseNP_613049.2276aa88%95%Animalia92.4 mya
Meleagris gallopavoturkeyXP_003210928276aa74%88%Animalia301.7 mya
Gallus gallusRed JunglefowlNP_001007837276aa73%88%Animalia301.7 mya
Xenopus laevisAfrican clawed frogNP_001083694275aa69%86%Animalia371.2 mya
Xenopus (Silurana) tropicalisWestern clawed frogNP_001004885.1276aa68%85%Animalia371.2 mya
Salmo salarAtlantic salmonNP_001167100274aa66%79%Animalia400.1 mya
Danio reriozebrafishNP_001003781273aa64%78%Animalia400.1 mya
CanarypoxvirusNP_955117275aa50%69%--
FowlpoxvirusNP_039033273aa44%63%--
CupriavidusproteobacteriaYP_002005507.1275aa38%52%Eubacteria2313.2 mya
BurkholderiaproteobacteriaYP_004977059273aa37%53%Eubacteria2313.2 mya
Physcomitrella patensmossXP_001781807275aa37%54%Plantae1369 mya
Zea maysmaize/cornACG35095266aa33%53%Plantae1369 mya
Trichophyton rubrumfungusXP_003236126306aa32%47%Fungi1215.8 mya
Sporisorium reilianumPlant pathogenCBQ69093321aa32%43%Fungi1215.8 mya
Perkinsus marinuspathogen of oystersXP_002787624219aa31%48%Protista1381.2 mya
Tetrahymena thermophiliaCiliate protozoaXP_001010229277aa26%44%Protista1381.2 mya
Natrialba magadiiextremophileYP_003481665300aa25%39%Archaebacteria3556.3 mya
Halopiger xanaduensishalophilic archaeonYP_004597780.1264aa24%39%Archaebacteria3556.3 mya

Clinical significance

Avipoxvirus infection

C22orf25 protein shows 48.7% identity with the CNPV094 T10-like protein of the Canarypox virus and 44.1% identity with the T10 protein of the Fowlpox virus, both of which are Avipoxviruses. Poxviruses evade immune invasion by regulating innate immunity primary mediators including interferons, tumor necrosis factors, and chemokines.[22] The T10 protein resembles the NF-κB2 protein and is known to interact with immune mediators and transcriptional regulatory proteins.[23]

Predicted protein features

Post translational modifications

Post translational modifications of the C22orf25 gene that are evolutionarily conserved in the Animalia and Plantae kingdoms as well as the Canarypox Virus include glycosylation (C-mannosylation),[24] glycation,[25] phosphorylation (kinase specific),[26] and palmitoylation.[27]

Predicted topology

C22orf25 localizes to the cytoplasm and is anchored to the cell membrane by the second amino acid. As mentioned previously, the second amino acid is modified by palmitoylation. Palmitoylation is known to contribute to membrane association[28] because it contributes to enhanced hydrophobicity.[5] Palmitoylation is known to play a role in the modulation of proteins' trafficking,[29] stability[30] and sorting.[31] Palmitoylation is also involved in cellular signaling[32] and neuronal transmission.[33]

Protein Interactions

C22orf25 has been shown to interact with NFKB1,[34] RELA,[34] RELB,[34] BTRC,[34] RPS27A,[34] BCL3,[35] MAP3K8,[34] NFKBIA,[34] SIN3A,[34] SUMO1,[34] Tat.[36]

References

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  2. "Mouse PubMed Reference:".
  3. "BLAST (NCBI)".
  4. "Conserved Domains (NCBI)".
  5. 1 2 "CSS-Palm".
  6. "PSORTII".
  7. 1 2 "Gene (NCBI)".
  8. "ElDorado (Genomatix)".
  9. "SignalP (ExPASy)".
  10. "Statistical Analysis of Protein Sequence (Biology Workbench)".
  11. Meechan DW, Maynard TM, Tucker ES, LaMantia AS (2011). "Three phases of DiGeorge/22q11 deletion syndrome pathogenesis during brain development: Patterning, proliferation, and mitochondrial functions of 22q11 genes". International Journal of Developmental Neuroscience. 29 (3): 283–294. doi:10.1016/j.ijdevneu.2010.08.005. PMID 20833244.
  12. Kniffin, C. "DiGeorge Syndrome; DGS. Retrieved April 2012, from Online Mendelian Inheritance in Man". Retrieved April 8, 2012.
  13. Scambler PJ (2000). "The 22q11 deletion syndromes". Hum. Mol. Genet. 9 (16): 2421–6. doi:10.1093/hmg/9.16.2421. PMID 11005797.
  14. "22q11.2 Deletion Syndrome". Retrieved March 2012. Check date values in: |access-date= (help)
  15. "BLAT UCSC Genome Browser".
  16. "El Durado (Genomatix)".
  17. "El Durado-Genomatix".
  18. "Unigene NCBI".
  19. "GEO Profiles NCBI".
  20. "Bio GPS".
  21. "WormBase".
  22. Seet BT, Johnston JB, Brunetti CR, Barrett JW, Everett H, Cameron C, Sypula J, Nazarian SH, Lucas A, McFadden G (2003). "Poxviruses and Immune Evasion". Annual Review of Immunology. 21: 377–423. doi:10.1146/annurev.immunol.21.120601.141049. PMID 12543935.
  23. "MINT".
  24. "NetCGly (ExPASy)".
  25. "NetGlycate (ExPASy)".
  26. "Phos (ExPASy)".
  27. "CSS Palm (ExPASy)".
  28. Resh MD (2006). "Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules". Science STKE (359): 14. doi:10.1126/stke.3592006re14. PMID 17077383.
  29. Draper JM, Xia Z, Smith CD (Aug 2007). "Cellular palmitoylation and trafficking of lipated peptides". NIH Public Access. 48 (8): 1873–1884. doi:10.1194/jlr.m700179-jlr200. PMID 17525474.
  30. Linder ME, Deschenes RJ (Jan 2007). "Palmitoylation: policing protein stability and traffic". Nature Reviews Molecular Cell Biology. 8 (1): 74–84. doi:10.1038/nrm2084. PMID 17183362.
  31. Greaves J, Chamberlain LH (Jan 2007). "Palmitoylation-dependent protein sorting". Cellular Biology. 176 (3): 249–254. doi:10.1083/jcb.200610151. PMID 17242068.
  32. Casey PJ (1995). "Protein lipidation in cell signaling". Science. 268 (5208): 221–5. doi:10.1126/science.7716512. PMID 7716512.
  33. Roth AF, Wan J, Bailey AO, Sun B, Kuchar JA, Green WN, Phinney BS, Yates JR, Davis NG (June 2006). "Global analysis of protein palmitoylation in yeast". Cell. 125 (5): 1003–1013. doi:10.1016/j.cell.2006.03.042. PMID 16751107.
  34. 1 2 3 4 5 6 7 8 9 "Molecular Interaction Database".
  35. "Molecular Interaction Database".
  36. "Viral Molecular Interaction Database".
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