EFNA5

Ephrin-A5
PDB rendering based on 1shw.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1shw​, 1shx​
Identifiers
Symbols	EFNA5 ; AF1; EFL5; EPLG7; GLC1M; LERK7; RAGS
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1482
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Ephrin-A5, also known as EFNA5, is a human gene.

Ephrin-A5, a member of the ephrin gene family, prevents axon bundling in cocultures of cortical neurons with astrocytes, a model of late stage nervous system development and differentiation. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are similarly divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.

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. PMID 9576626.
• 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. 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. PMID 11128993.CS1 maint: Multiple names: authors list (link)
• Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci. 2 (3): 155–64. PMID 11256076.
• Winslow JW, Moran P, Valverde J; et al. (1995). "Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation". Neuron. 14 (5): 973–81. PMID 7748564.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Cerretti DP, Copeland NG, Gilbert DJ; et al. (1996). "The gene encoding LERK-7 (EPLG7, Epl7), a ligand for the Eph-related receptor tyrosine kinases, maps to human chromosome 5 at band q21 and to mouse chromosome 17". Genomics. 35 (2): 376–9. doi:10.1006/geno.1996.0371. PMID 8661153.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gale NW, Holland SJ, Valenzuela DM; et al. (1996). "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron. 17 (1): 9–19. PMID 8755474.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9195962.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell. 90 (3): 403–4. 1997. PMID 9267020.
• 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. PMID 9751130.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Janis LS, Cassidy RM, Kromer LF (1999). "Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum". J. Neurosci. 19 (12): 4962–71. PMID 10366629.CS1 maint: Multiple names: authors list (link)
• Gerlai R, Shinsky N, Shih A; et al. (1999). "Regulation of learning by EphA receptors: a protein targeting study". J. Neurosci. 19 (21): 9538–49. PMID 10531456.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Davy A, Gale NW, Murray EW; et al. (2000). "Compartmentalized signaling by GPI-anchored ephrin-A5 requires the Fyn tyrosine kinase to regulate cellular adhesion". Genes Dev. 13 (23): 3125–35. PMID 10601038.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)