EFNA5

From Wikipedia, the free encyclopedia

Ephrin-A5

PDB rendering based on 1shw.

Available structures: 1shw, 1shx

Identifiers

Symbol(s)

EFNA5; AF1; EFL5; EPLG7; GLC1M; LERK7; RAGS

External IDs

OMIM: 601535 MGI: 107444 HomoloGene: 1482

Gene ontology
Molecular Function:	• chemorepellant activity • ephrin receptor binding • GPI anchor binding
Cellular Component:	• extracellular space • membrane • anchored to plasma membrane
Biological Process:	• cell-cell signaling • multicellular organismal development • nervous system development • cell differentiation • retinal ganglion cell axon guidance

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001962 (mRNA)
NP_001953 (protein)

NM_010109 (mRNA)
NP_034239 (protein)

Location

Chr 5: 106.74 - 107.03 Mb

Chr 17: 62.29 - 62.57 Mb

Pubmed search

[1]

[2]

Ephrin-A5, also known as EFNA5, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: EFNA5 ephrin-A5.

[edit] 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.
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.
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.
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.
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.
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.
"Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee." (1997). Cell 90 (3): 403-4. 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.
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.
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.
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.