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) [1] Band 3p11.1 Start 89,107,621 bp [1] End 89,482,134 bp [1]
Gene location (Mouse) Chr. Chromosome 16 (mouse) [2] Band 16|16 C1.3 Start 63,363,897 bp [2] End 63,684,538 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 2042 13837 Ensembl ENSG00000044524 ENSMUSG00000052504 UniProt P29320 P29319 Q8BRB1 RefSeq (mRNA) NM_005233 NM_182644 NM_010140 NM_001362452 RefSeq (protein) NP_005224 NP_872585 NP_034270 NP_001349381 Location (UCSC) Chr 3: 89.11 – 89.48 Mb Chr 16: 63.36 – 63.68 Mb PubMed search [3] [4]
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

1. GRCh38: Ensembl release 89: ENSG00000044524 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000052504 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: EPHA3 EPH receptor A3".
8. 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.
9. 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.
10. 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.

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. doi:10.1242/dev.126.10.2033. PMID   10207129.
• Wilkinson DG (2000). "Eph receptors and ephrins: Regulators of guidance and assembly". A Survey of Cell Biology. International Review of Cytology. Vol. 196. pp. 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN   9780123646002. PMID   10730216.{{cite book}}: |journal= ignored (help)
• 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.