EPH receptor A3

EPHA3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2GSF, 2QO7, 2QO9, 2QOB, 2QOC, 2QOD, 2QOF, 2QOI, 2QOK, 2QOL, 2QON, 2QOO, 2QOQ, 3DZQ, 3FXX, 3FY2, 4G2F, 4GK2, 4GK3, 4GK4, 4L0P, 4P4C, 4P5Q, 4P5Z, 4TWN, 4TWO
Identifiers
Aliases	EPHA3, Epha3, AW492086, Cek4, ETK1, End3, Hek, Hek4, Mek4, Tyro4, EK4, ETK, EPH receptor A3, HEK, HEK4, TYRO4
External IDs	OMIM: 179611; MGI: 99612; HomoloGene: 21083; GeneCards: EPHA3; OMA:EPHA3 - orthologs
Gene location (Human)
Chr.	Chromosome 3 (human)
End	89,482,134 bp
Gene location (Mouse)
Chr.	Chromosome 16 (mouse)
End	63,684,538 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; buccal mucosa cell; ; urethra; ; gallbladder; ; mucosa of urinary bladder; ; tibia; ; Achilles tendon; ; prostate; ; right coronary artery; ; placenta;
	Top expressed in
	maxillary part of mouth; ; upper jaw; ; ganglionic eminence; ; tongue; ; calvaria; ; medial ganglionic eminence; ; human fetus; ; left lung lobe; ; efferent ductule; ; abdominal wall;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; GPI-linked ephrin receptor activity; kinase activity; protein binding; transmembrane receptor protein tyrosine kinase activity; protein tyrosine kinase activity; ATP binding; ephrin receptor activity; receptor tyrosine kinase; transmembrane signaling receptor activity; transmembrane-ephrin receptor activity;
Cellular component	integral component of membrane; membrane; plasma membrane; integral component of plasma membrane; extracellular region; early endosome; cytoplasm; neuron projection; receptor complex;
Biological process	cellular response to retinoic acid; regulation of actin cytoskeleton organization; fasciculation of motor neuron axon; phosphorylation; transmembrane receptor protein tyrosine kinase signaling pathway; regulation of GTPase activity; regulation of epithelial to mesenchymal transition; regulation of microtubule cytoskeleton organization; protein phosphorylation; cell adhesion; positive regulation of neuron projection development; regulation of focal adhesion assembly; fasciculation of sensory neuron axon; cell migration; ephrin receptor signaling pathway; peptidyl-tyrosine phosphorylation; negative regulation of endocytosis; positive regulation of protein localization to plasma membrane; negative regulation of signal transduction; cell differentiation; negative regulation of apoptotic process; positive regulation of ERK1 and ERK2 cascade; axon guidance;
	Sources:Amigo / QuickGO
Orthologs
	2042
	13837
	ENSG00000044524
	ENSMUSG00000052504
	P29320
	P29319; Q8BRB1
	NM_005233; NM_182644
	NM_010140; NM_001362452
	NP_005224; NP_872585
	NP_034270; NP_001349381
	Wikidata
View/Edit Human	View/Edit Mouse

EPH receptor A3 (ephrin type-A receptor 3) is a protein that in humans is encoded by the EPHA3 gene.^[5]^[6]^[7]

Function

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.^[7]

Interactions

EPH receptor A3 has been shown to interact with EFNB2^[8]^[9] and EFNA5.^[9]^[10]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000044524 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000052504 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Boyd AW, Ward LD, Wicks IP, Simpson RJ, Salvaris E, Wilks A, Welch K, Loudovaris M, Rockman S, Busmanis I (March 1992). "Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell line". J Biol Chem. 267 (5): 3262–7. doi:10.1016/S0021-9258(19)50725-6. PMID 1737782.
^ Wicks IP, Wilkinson D, Salvaris E, Boyd AW (April 1992). "Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines". Proc Natl Acad Sci U S A. 89 (5): 1611–5. Bibcode:1992PNAS...89.1611W. doi:10.1073/pnas.89.5.1611. PMC 48502. PMID 1311845.
^ ^a ^b "Entrez Gene: EPHA3 EPH receptor A3".
^ Cerretti DP, Vanden Bos T, Nelson N, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ (November 1995). "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.
^ ^a ^b Lackmann M, Mann RJ, Kravets L, Smith FM, Bucci TA, Maxwell KF, Howlett GJ, Olsson JE, Vanden Bos T, Cerretti DP, Boyd AW (June 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, Cerretti DP, Carpenter MK (August 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.

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. doi:10.1242/dev.126.10.2033. PMID 10207129.
Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly". Int. Rev. Cytol. International Review of Cytology. 196: 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN 9780123646002. 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. S2CID 205014301.
Beckmann MP, Cerretti DP, Baum P, Vanden Bos T, James L, Farrah T, Kozlosky C, Hollingsworth T, Shilling H, Maraskovsky E (1994). "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors". EMBO J. 13 (16): 3757–62. doi:10.1002/j.1460-2075.1994.tb06685.x. PMC 395287. PMID 8070404.
Wicks IP, Lapsys NM, Baker E, Campbell LJ, Boyd AW, Sutherland GR (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, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ (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, Smith FM, Bucci TA, Maxwell KF, Howlett GJ, Olsson JE, Vanden Bos T, Cerretti DP, Boyd AW (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, Cerretti DP, Carpenter MK (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. S2CID 26773768.
Lackmann M, Oates AC, Dottori M, Smith FM, Do C, Power M, Kravets L, Boyd AW (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, Löschinger J, Lang S, Müller BK, Bonhoeffer F, Drescher U (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. S2CID 20470923.

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

EPH receptor A3

Function

Interactions

References

Further reading

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