Ephrin A2

EFNA2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2WO3
Identifiers
Aliases	EFNA2, ELF-1, EPLG6, HEK7-L, LERK-6, LERK6, ephrin A2
External IDs	OMIM: 602756; MGI: 102707; HomoloGene: 1075; GeneCards: EFNA2; OMA:EFNA2 - orthologs
Gene location (Human)
Chr.	Chromosome 19 (human)
End	1,301,431 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	80,025,844 bp
RNA expression pattern
	Top expressed in
	mucosa of ileum; ; mucosa of sigmoid colon; ; buccal mucosa cell; ; mucosa of transverse colon; ; pancreatic ductal cell; ; jejunal mucosa; ; gonad; ; duodenum; ; right lobe of liver; ; sural nerve;
	Top expressed in
	internal carotid artery; ; external carotid artery; ; Rostral migratory stream; ; abdominal wall; ; gastrula; ; limb bud; ; Gonadal ridge; ; fossa; ; condyle; ; ganglionic eminence;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	ephrin receptor binding; protein binding;
Cellular component	anchored component of membrane; neuromuscular junction; perikaryon; membrane; plasma membrane;
Biological process	cell-cell signaling; olfactory bulb development; axon guidance; osteoclast differentiation; bone remodeling; ephrin receptor signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	1943
	13637
	ENSG00000099617
	ENSMUSG00000003070
	O43921
	P52801
	NM_001405
	NM_007909
	NP_001396
	NP_031935
	Wikidata
View/Edit Human	View/Edit Mouse

Ephrin-A2 is a protein that in humans is encoded by the EFNA2 gene.^[5]

This gene encodes a member of the ephrin family. The protein is composed of a signal sequence, a receptor-binding region, a spacer region, and a hydrophobic region. 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. 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. Posttranslational modifications determine whether this protein localizes to the nucleus or the cytoplasm.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000099617 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000003070 – 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.
^ ^a ^b "Entrez Gene: EFNA2 ephrin-A2".

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.
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 978-0-12-364600-2. 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.
Gale NW, Holland SJ, Valenzuela DM, Flenniken A, Pan L, Ryan TE, Henkemeyer M, Strebhardt K, Hirai H (1996). "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron. 17 (1): 9–19. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474. S2CID 1075856.
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.
Cerretti DP, Nelson N (1998). "Characterization of the genes for mouse LERK-3/Ephrin-A3 (Epl3), mouse LERK-4/Ephrin-A4 (Epl4), and human LERK-6/Ephrin-A2 (EPLG6): conservation of intron/exon structure". Genomics. 47 (1): 131–5. doi:10.1006/geno.1997.5088. PMID 9465306.
Ciossek T, Monschau B, Kremoser C, Loschinger J, Lang S, Muller 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.
Aasheim HC, Pedeutour F, Grosgeorge J, Logtenberg T (1998). "Cloning, chromosal mapping, and tissue expression of the gene encoding the human Eph-family kinase ligand ephrin-A2". Biochem. Biophys. Res. Commun. 252 (2): 378–82. doi:10.1006/bbrc.1998.9618. PMID 9826538.
Gerlai R, Shinsky N, Shih A, Williams P, Winer J, Armanini M, Cairns B, Winslow J, Gao W (1999). "Regulation of learning by EphA receptors: a protein targeting study". J. Neurosci. 19 (21): 9538–49. doi:10.1523/JNEUROSCI.19-21-09538.1999. PMC 6782889. PMID 10531456.
Hattori M, Osterfield M, Flanagan JG (2000). "Regulated cleavage of a contact-mediated axon repellent". Science. 289 (5483): 1360–5. Bibcode:2000Sci...289.1360H. doi:10.1126/science.289.5483.1360. PMID 10958785.
Rodger J, Lindsey KA, Leaver SG, King CE, Dunlop SA, Beazley LD (2002). "Expression of ephrin-A2 in the superior colliculus and EphA5 in the retina following optic nerve section in adult rat". Eur. J. Neurosci. 14 (12): 1929–36. doi:10.1046/j.0953-816x.2001.01822.x. PMID 11860487. S2CID 24040732.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000099617 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000003070 – 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.

[entrez-5] "Entrez Gene: EFNA2 ephrin-A2".

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v t e Intercellular signaling peptides and proteins / ligands
Growth factors	Epidermal growth factor Fibroblast growth factor Nerve growth factor Platelet-derived growth factor Transforming growth factor beta superfamily Vascular endothelial growth factor
Ephrin	EFNA1 EFNA2 EFNA3 EFNA4 EFNA5 EFNB1 EFNB2 EFNB3
Other	Adipokine Agouti signaling protein Agouti-related protein Angiogenic protein CCN intercellular signaling protein Cysteine-rich protein 61 Connective tissue growth factor Nephroblastoma overexpressed protein Cytokine Endothelin EDN1 EDN2 EDN3 Hedgehog protein Interferon Kinin Parathyroid hormone-related protein Semaphorin Somatomedin Tolloid-like metalloproteinase Tumor necrosis factor Wnt protein
see also extracellular ligand disorders

References

Further reading