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TEKTIP1

[edit]

TEKTIP1, also known as tektin-bundle interacting protein 1 is a protein that in humans is encoded by the TEKTIP1 gene.[1]

GeneCard for C19orf71


Gene

[edit]

Tektin bundle interacting protein 1 (TEKTIP1) is a protein which in humans is encoded by the TEKTIP1 mRNA.[1] The longest mRNA produced is 826 bases long.[2]

Aliases

[edit]

Alias of the protein is C19orf71.[3] Locus

The TEKTIP1 gene is located at 19p13.3.[4]

Transcriptional Regulation

Several predicted transcription factors may bind in the promoter region: TFDP1, PLAGL1, ZSCAN4, POU2F3.[5][6][7][8][9][10][11]

Chemical Interactions

Acrylamide[12], cisplatin[13], and silicon dioxide[14] decrease expression, while butanal (butyraldehyde), and pentanal increase expression[15] of TEKTIP1 mRNA.

Sequence orthology also suggests that valproic acid increases methylation of TEKTIP1 mRNA.[16]

Protein

[edit]

The mRNA of TEKTIP1 is 654 nucleotides long.[1][3] It contains five exons.[1] The human TEKTIP1 protein is 209 amino acids long and and has a predicted molecular mass of 24.5 kDa.[3] The human protein has a theoretical isoelectric point of 9.1.[17]

Isoforms

There are two splice isoforms of the protein, X1[18] and X2[19].

X1 & X2 Isoform Orthologs
X1 X2
Tibetan macaque[20] Chimpanzee[21]
Olive baboon[22] Olive baboon[23]
Panamanian white-faced capuchin[24] Common marmoset[25]
Golden[26] and Black[27]

snub-nosed monkeys

Golden sub-nosed monkey[28]
Elk[29] Elk[30]
Red deer[31] Red deer[32]
Greater horseshoe bat[33] Bats[34][35][36]
Red fox[37] Polar bear[38]
File:TEKTIP1 structure (PHYRE2).png
Proposed tertiary structure for 27% of TEKTIP1. Image is in rainbow color, from the amino (N-terminus) to the carboxyl (C-terminus).[39]


Characteristics & structure

TEKTIP1 is highly enriched in tryptophan and tyrosine.[40] Additionally, the protein is semi-enriched in arginine and proline.[41]








Expression

[edit]

TEKTIP1 is tissue specific and is found in higher levels in the kidney, testis and thymus.[4]

In fetal development, it is found in higher levels in the Adrenal glands during weeks 16-20.[4]

TEKTIP1 protein is said to be specific to the testis and is found in early spermatids during spermatogenesis.[42]

Evolution

[edit]

Orthologs

[edit]
File:TEKTIP1 Phylogenetic Tree.jpg
TEKTIP1 phylogenetic tree schematic. Line length between organisms represent degree of species divergence.[43]

Over 240 organisms have orthologs with human gene TEKTIP1.[4] The most distant organism with an orthologous sequence to human TEKTIP1 is the West African lungfish (estimated date of divergence of 408 MYA).[44][45]

Selected Orthologs for TEKTIP1
Genus and Species Common Name Taxonomic Group Median Date of Divergence (MYA) Accession # Sequence length (aa) Sequence Identity to Human Protein % Sequence Similarity to Human Protein %
Homo sapein Human Primates/Hominidae 0 NP_001129052.1 209 100 100
Pan troglodyte Chimpanzee Primates 6.4 XP_003316050.1 209 98.1 98.6
Mus musculus Mouse Rodentia 87 NP_001014836.2 217 45.6 60.4
Bos taurus Cow Artiodactyla 94 NP_001070550 208 76.6 84.2
Panthera tigris Tiger Carnivora 94 XP_042833719.1 210 34.1 38.9
Orcinus orca Killer whale Cetacea 94 XP_012394771.2 216 63 73.1
Phascolarctos cinereus Koala Diprodontia 160 XP_020824948.1 211 52.9 67.4
Haliaeetus leucocephalus Bald Eagle Accipitiformes 319 XP_010580112.1 206 41.4 52
Dromaius novaehollandiae Emu Aves 319 XP_025961204.1 190 44.8 56.7
Gallus gallus domesticus Chicken Aves 319 XP_015155269.2 188 38.2 48.4
Crocodylus porosus Saltwater Crocodile Crocodilia 319 XP_019406144.1 210 54.3 68.3
Caretta caretta Loggerhead Sea Turtle Testudines 319 XP_048687032.1 216 47.8 57.3
Zootoca vivipara Common lizard Squamata 319 XP_034975173.1 200 48.8 59.5
Crotalus tigris Tiger Rattlesnake Squamata 319 XP_039190693.1 199 45.8 57.5
Protobothrops mucrosquamatus Venomous Pit Viper Squamata 319 XP_015665555.1 199 45.1 56.7
Bufo bufo Common Toad Salientia 353 XP_040276375 136 24.7 34.3
Geotrypetes seraphini Gaboon Caecilian Caecilians 353 XP_033813379.1 156 36.1 45.8
Microcaecilia unicolor Tiny Caecilian Caecilians 353 XP_030074922.1 142 34.3 42.6
Protopterus annectens West African Lungfish Actinopterygii 408 XP_043910031.1 142 28.6 39
  1. ^ a b c d "Homo sapiens tektin bundle interacting protein 1 (TEKTIP1), mRNA". 2022-08-14. {{cite journal}}: Cite journal requires |journal= (help)
  2. ^ "PREDICTED: Homo sapiens tektin bundle interacting protein 1 (TEKTIP1), transcript variant X1, mRNA". 2022-04-05. {{cite journal}}: Cite journal requires |journal= (help)
  3. ^ a b c "tektin bundle interacting protein 1 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-20.
  4. ^ a b c d "TEKTIP1 tektin bundle interacting protein 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-12-14.
  5. ^ Zaragoza, Katrin; Bégay, Valérie; Schuetz, Anja; Heinemann, Udo; Leutz, Achim (2010-05). "Repression of transcriptional activity of C/EBPalpha by E2F-dimerization partner complexes". Molecular and Cellular Biology. 30 (9): 2293–2304. doi:10.1128/MCB.01619-09. ISSN 1098-5549. PMC 2863587. PMID 20176812. {{cite journal}}: Check date values in: |date= (help)
  6. ^ Wu, C. L.; Zukerberg, L. R.; Ngwu, C.; Harlow, E.; Lees, J. A. (1995-05). "In vivo association of E2F and DP family proteins". Molecular and Cellular Biology. 15 (5): 2536–2546. doi:10.1128/MCB.15.5.2536. ISSN 0270-7306. PMID 7739537. {{cite journal}}: Check date values in: |date= (help)
  7. ^ Helin, K.; Wu, C. L.; Fattaey, A. R.; Lees, J. A.; Dynlacht, B. D.; Ngwu, C.; Harlow, E. (1993-10). "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation". Genes & Development. 7 (10): 1850–1861. doi:10.1101/gad.7.10.1850. ISSN 0890-9369. PMID 8405995. {{cite journal}}: Check date values in: |date= (help)
  8. ^ Zaragoza, Katrin; Bégay, Valérie; Schuetz, Anja; Heinemann, Udo; Leutz, Achim (2010-05). "Repression of transcriptional activity of C/EBPalpha by E2F-dimerization partner complexes". Molecular and Cellular Biology. 30 (9): 2293–2304. doi:10.1128/MCB.01619-09. ISSN 1098-5549. PMC 2863587. PMID 20176812. {{cite journal}}: Check date values in: |date= (help)
  9. ^ Wu, C. L.; Zukerberg, L. R.; Ngwu, C.; Harlow, E.; Lees, J. A. (1995-05). "In vivo association of E2F and DP family proteins". Molecular and Cellular Biology. 15 (5): 2536–2546. doi:10.1128/MCB.15.5.2536. ISSN 0270-7306. PMID 7739537. {{cite journal}}: Check date values in: |date= (help)
  10. ^ Hildesheim, J.; Foster, R. A.; Chamberlin, M. E.; Vogel, J. C. (1999-09-10). "Characterization of the regulatory domains of the human skn-1a/Epoc-1/Oct-11 POU transcription factor". The Journal of Biological Chemistry. 274 (37): 26399–26406. doi:10.1074/jbc.274.37.26399. ISSN 0021-9258. PMID 10473598.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  11. ^ Portney, Benjamin A.; Khatri, Raju; Meltzer, W. Alex; Mariano, Jennifer M.; Zalzman, Michal (2018-03-25). "ZSCAN4 is negatively regulated by the ubiquitin-proteasome system and the E3 ubiquitin ligase RNF20". Biochemical and Biophysical Research Communications. 498 (1): 72–78. doi:10.1016/j.bbrc.2018.02.155. ISSN 1090-2104. PMC 5928792. PMID 29477841.
  12. ^ Bu, Qian; Huang, Yan; Li, Meng; Dai, Yanping; Fang, Xin; Chen, Ke; Liu, Qian; Xue, Aiqin; Zhong, Kai; Huang, Yina; Gao, Hong; Cen, Xiaobo (2020-10). "Acrylamide exposure represses neuronal differentiation, induces cell apoptosis and promotes tau hyperphosphorylation in hESC-derived 3D cerebral organoids". Food and Chemical Toxicology: An International Journal Published for the British Industrial Biological Research Association. 144: 111643. doi:10.1016/j.fct.2020.111643. ISSN 1873-6351. PMID 32763439. {{cite journal}}: Check date values in: |date= (help)
  13. ^ Lu, Jun; Chen, Jian; Xu, Nianjun; Wu, Jun; Kang, Yani; Shen, Tingting; Kong, Hualei; Ma, Chao; Cheng, Ming; Shao, Zhifeng; Xu, Ling; Zhao, Xiaodong (2016-09-06). "Activation of AIFM2 enhances apoptosis of human lung cancer cells undergoing toxicological stress". Toxicology Letters. 258: 227–236. doi:10.1016/j.toxlet.2016.07.002. ISSN 1879-3169. PMID 27392435.
  14. ^ Pisani, Cédric; Gaillard, Jean-Charles; Nouvel, Virginie; Odorico, Michaël; Armengaud, Jean; Prat, Odette (2015-04-18). "High-throughput, quantitative assessment of the effects of low-dose silica nanoparticles on lung cells: grasping complex toxicity with a great depth of field". BMC genomics. 16 (1): 315. doi:10.1186/s12864-015-1521-5. ISSN 1471-2164. PMC 4404697. PMID 25895662.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  15. ^ Song, Mi-Kyung; Lee, Hyo-Sun; Ryu, Jae-Chun (2015-08-06). "Integrated analysis of microRNA and mRNA expression profiles highlights aldehyde-induced inflammatory responses in cells relevant for lung toxicity". Toxicology. 334: 111–121. doi:10.1016/j.tox.2015.06.007. ISSN 1879-3185. PMID 26079696.
  16. ^ van Breda, Simone G. J.; Claessen, Sandra M. H.; van Herwijnen, Marcel; Theunissen, Daniël H. J.; Jennen, Danyel G. J.; de Kok, Theo M. C. M.; Kleinjans, Jos C. S. (2018-01-15). "Integrative omics data analyses of repeated dose toxicity of valproic acid in vitro reveal new mechanisms of steatosis induction". Toxicology. 393: 160–170. doi:10.1016/j.tox.2017.11.013. ISSN 1879-3185. PMID 29154799.
  17. ^ "Expasy - Compute pI/Mw tool". web.expasy.org. Retrieved 2022-12-14.
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  19. ^ "uncharacterized protein C19orf71 isoform X2 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-20.
  20. ^ "tektin bundle interacting protein 1 isoform X1 [Macaca thibetana thibe - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-20.
  21. ^ "uncharacterized protein C19orf71 homolog isoform X2 [Pan troglodytes] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-20.
  22. ^ "uncharacterized protein C19orf71 homolog isoform X1 [Papio anubis] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-20.
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  24. ^ "uncharacterized protein C19orf71 homolog isoform X1 [Cebus imitator] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-20.
  25. ^ "uncharacterized protein C19orf71 homolog isoform X2 [Callithrix jacchu - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-20.
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