EPH receptor A3

EPH receptor A3
PDB rendering based on 2gsf.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2GSF, 2QO2, 2QO7, 2QO9, 2QOB, 2QOC, 2QOD, 2QOF, 2QOI, 2QOK, 2QOL, 2QON, 2QOO, 2QOQ, 3DZQ, 3FXX, 3FY2, 4G2F, 4GK2, 4GK3, 4GK4
Identifiers
Symbols	EPHA3; EK4; ETK; ETK1; HEK; HEK4; TYRO4
External IDs	OMIM: 179611 MGI: 99612 HomoloGene: 21083 ChEMBL: 4954 GeneCards: EPHA3 Gene
EC number	2.7.10.1
Gene Ontology Molecular function • GPI-linked ephrin receptor activity • protein binding • ATP binding Cellular component • extracellular region • early endosome • integral to plasma membrane Biological process • apoptotic process • cell adhesion • regulation of epithelial to mesenchymal transition • positive regulation of neuron projection development • cell migration • regulation of Rho GTPase activity • regulation of actin cytoskeleton organization • ephrin receptor signaling pathway • regulation of focal adhesion assembly • regulation of microtubule cytoskeleton organization • cellular response to retinoic acid • fasciculation of sensory neuron axon • fasciculation of motor neuron axon Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2042	13837
Ensembl	ENSG00000044524	ENSMUSG00000052504
UniProt	P29320	P29319
RefSeq (mRNA)	NM_005233	NM_010140
RefSeq (protein)	NP_005224	NP_034270
Location (UCSC)	Chr 3: 89.16 – 89.53 Mb	Chr 16: 63.54 – 63.86 Mb
PubMed search	[1]	[2]

EPH receptor A3 (ephrin type-A receptor 3) is a protein that in humans is encoded by the EPHA3 gene.

This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands. Two alternatively spliced transcript variants have been described for this gene.

Interactions

EPH receptor A3 has been shown to interact with EFNB2 and EFNA5.

Further reading

• Flanagan JG, Vanderhaeghen P (1998). "The ephrins and Eph receptors in neural development.". Annu. Rev. Neurosci. 21: 309–45. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499. 
• Zhou R (1998). "The Eph family receptors and ligands.". Pharmacol. Ther. 77 (3): 151–81. doi:10.1016/S0163-7258(97)00112-5. PMID 9576626. 
• Ernst AF, Jurney WM, McLoon SC (1999). "Mechanisms involved in development of retinotectal connections: roles of Eph receptor tyrosine kinases, NMDA receptors and nitric oxide.". Prog. Brain Res. 118: 115–31. doi:10.1016/S0079-6123(08)63204-5. PMID 9932438. 
• Holder N, Klein R (1999). "Eph receptors and ephrins: effectors of morphogenesis.". Development 126 (10): 2033–44. PMID 10207129. 
• Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly.". Int. Rev. Cytol. 196: 177–244. doi:10.1016/S0074-7696(00)96005-4. PMID 10730216. 
• Xu Q, Mellitzer G, Wilkinson DG (2001). "Roles of Eph receptors and ephrins in segmental patterning.". Philos. Trans. R. Soc. Lond., B, Biol. Sci. 355 (1399): 993–1002. doi:10.1098/rstb.2000.0635. PMC 1692797. PMID 11128993. 
• Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development.". Nat. Rev. Neurosci. 2 (3): 155–64. doi:10.1038/35058515. PMID 11256076. 
• Beckmann MP, Cerretti DP, Baum P, et al. (1994). "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors.". EMBO J. 13 (16): 3757–62. PMC 395287. PMID 8070404. 
• Wicks IP, Lapsys NM, Baker E, et al. (1994). "Localization of a human receptor tyrosine kinase (ETK1) to chromosome region 3p11.2.". Genomics 19 (1): 38–41. doi:10.1006/geno.1994.1009. PMID 8188238. 
• Cerretti DP, Vanden Bos T, Nelson N, et al. (1996). "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases.". Mol. Immunol. 32 (16): 1197–205. doi:10.1016/0161-5890(95)00108-5. PMID 8559144. 
• Lackmann M, Mann RJ, Kravets L, et al. (1997). "Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor.". J. Biol. Chem. 272 (26): 16521–30. doi:10.1074/jbc.272.26.16521. PMID 9195962. 
• Kozlosky CJ, VandenBos T, Park L, et al. (1997). "LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain.". Cytokine 9 (8): 540–9. doi:10.1006/cyto.1997.0199. PMID 9245480. 
• Ephnomenclaturecommittee, (1997). "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee.". Cell 90 (3): 403–4. doi:10.1016/S0092-8674(00)80500-0. PMID 9267020. 
• Lackmann M, Oates AC, Dottori M, et al. (1998). "Distinct subdomains of the EphA3 receptor mediate ligand binding and receptor dimerization.". J. Biol. Chem. 273 (32): 20228–37. doi:10.1074/jbc.273.32.20228. PMID 9685371. 
• Ciossek T, Monschau B, Kremoser C, et al. (1998). "Eph receptor-ligand interactions are necessary for guidance of retinal ganglion cell axons in vitro.". Eur. J. Neurosci. 10 (5): 1574–80. doi:10.1046/j.1460-9568.1998.00180.x. PMID 9751130.