ANTXR1

Anthrax toxin receptor 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3N2N​
Identifiers
Symbols	ANTXR1 ; ATR; GAPO; TEM8
External IDs	OMIM: 606410 MGI: 1916788 HomoloGene: 12976 GeneCards: ANTXR1 Gene
Gene ontology Molecular function • transmembrane signaling receptor activity • protein binding • collagen binding • metal ion binding • actin filament binding Cellular component • plasma membrane • cell surface • endosome membrane • integral component of membrane • lamellipodium membrane • filopodium membrane • extracellular exosome Biological process • signal transduction • reproductive process • actin cytoskeleton reorganization • substrate adhesion-dependent cell spreading Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	84168	69538
Ensembl	ENSG00000169604	ENSMUSG00000033420
UniProt	Q9H6X2	Q9CZ52
RefSeq (mRNA)	NM_018153	NM_054041
RefSeq (protein)	NP_060623	NP_473382
Location (UCSC)	Chr 2: 69.01 – 69.25 Mb	Chr 6: 87.13 – 87.34 Mb
PubMed search

Anthrax toxin receptor 1 is a protein that in humans is encoded by the ANTXR1 gene.^[1][2][3]

The protein encoded by this gene is a type I transmembrane protein and is a tumor-specific endothelial marker that has been implicated in colorectal cancer. This protein has been shown to also be a docking protein or receptor for Bacillus anthracis toxin, the causative agent of the disease, anthrax. The binding of the protective antigen (PA) component, of the tripartite anthrax toxin, to this receptor protein mediates delivery of toxin components to the cytosol of cells. Once inside the cell, the other two components of anthrax toxin, edema factor (EF) and lethal factor (LF) disrupt normal cellular processes. Three alternatively spliced variants have been described.^[3]

See also

• Anthrax toxin

References

1. St Croix B, Rago C, Velculescu V, Traverso G, Romans KE, Montgomery E, Lal A, Riggins GJ, Lengauer C, Vogelstein B, Kinzler KW (Aug 2000). "Genes expressed in human tumor endothelium". Science 289 (5482): 1197–202. doi:10.1126/science.289.5482.1197. PMID 10947988.
2. Carson-Walter EB, Watkins DN, Nanda A, Vogelstein B, Kinzler KW, St Croix B (Sep 2001). "Cell surface tumor endothelial markers are conserved in mice and humans". Cancer Res 61 (18): 6649–55. PMID 11559528.
3. "Entrez Gene: ANTXR1 anthrax toxin receptor 1".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Schmidt DR, Schreiber SL (1999). "Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4". Biochemistry 38 (44): 14711–7. doi:10.1021/bi991614n. PMID 10545197.
• Liu XH, Collier RJ, Youle RJ (2002). "Inhibition of axotomy-induced neuronal apoptosis by extracellular delivery of a Bcl-XL fusion protein". J. Biol. Chem. 276 (49): 46326–32. doi:10.1074/jbc.M108930200. PMID 11574549.
• Bradley KA, Mogridge J, Mourez M; et al. (2001). "Identification of the cellular receptor for anthrax toxin". Nature 414 (6860): 225–9. doi:10.1038/n35101999. PMID 11700562.
• Latonen L, Taya Y, Laiho M (2001). "UV-radiation induces dose-dependent regulation of p53 response and modulates p53-HDM2 interaction in human fibroblasts". Oncogene 20 (46): 6784–93. doi:10.1038/sj.onc.1204883. PMID 11709713.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Scobie HM, Rainey GJ, Bradley KA, Young JA (2003). "Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor". Proc. Natl. Acad. Sci. U.S.A. 100 (9): 5170–4. doi:10.1073/pnas.0431098100. PMC 154317. PMID 12700348.
• Bradley KA, Mogridge J, Jonah G; et al. (2004). "Binding of anthrax toxin to its receptor is similar to alpha integrin-ligand interactions". J. Biol. Chem. 278 (49): 49342–7. doi:10.1074/jbc.M307900200. PMID 14507921.
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Jones GG, Reaper PM, Pettitt AR, Sherrington PD (2004). "The ATR-p53 pathway is suppressed in noncycling normal and malignant lymphocytes". Oncogene 23 (10): 1911–21. doi:10.1038/sj.onc.1207318. PMID 14755251.
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Bonuccelli G, Sotgia F, Frank PG; et al. (2005). "ATR/TEM8 is highly expressed in epithelial cells lining Bacillus anthracis' three sites of entry: implications for the pathogenesis of anthrax infection". Am. J. Physiol., Cell Physiol. 288 (6): C1402–10. doi:10.1152/ajpcell.00582.2004. PMID 15689409.
• Hotchkiss KA, Basile CM, Spring SC; et al. (2005). "TEM8 expression stimulates endothelial cell adhesion and migration by regulating cell-matrix interactions on collagen". Exp. Cell Res. 305 (1): 133–44. doi:10.1016/j.yexcr.2004.12.025. PMID 15777794.
• Rmali KA, Puntis MC, Jiang WG (2005). "TEM-8 and tubule formation in endothelial cells, its potential role of its vW/TM domains". Biochem. Biophys. Res. Commun. 334 (1): 231–8. doi:10.1016/j.bbrc.2005.06.085. PMID 15993844.
• Rainey GJ, Wigelsworth DJ, Ryan PL; et al. (2005). "Receptor-specific requirements for anthrax toxin delivery into cells". Proc. Natl. Acad. Sci. U.S.A. 102 (37): 13278–83. doi:10.1073/pnas.0505865102. PMC 1201603. PMID 16141341.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.