Ephrin A1

EFNA1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3HEI, 3MBW, 3CZU
Identifiers
Aliases	EFNA1, B61, ECKLG, EFL1, EPLG1, LERK-1, LERK1, TNFAIP4, Ephrin A1, GMAN
External IDs	OMIM: 191164 MGI: 103236 HomoloGene: 3262 GeneCards: EFNA1
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	155,134,899 bp[1]
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)[2]
End	89,281,142 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• GO:0001948 protein binding; • receptor binding; • ephrin receptor binding;
Cellular component	• membrane; • cell membrane; • integral component of plasma membrane; • anchored component of membrane; • extracellular exosome; • intracellular; • extracellular region; • anchored component of plasma membrane;
Biological process	• regulation of cell adhesion mediated by integrin; • ephrin receptor signaling pathway; • aortic valve morphogenesis; • cell-cell signaling; • negative regulation of transcription from RNA polymerase II promoter; • regulation of angiogenesis; • mitral valve morphogenesis; • endocardial cushion to mesenchymal transition involved in heart valve formation; • regulation of blood vessel endothelial cell migration; • regulation of axonogenesis; • activation of MAPK activity; • neuron differentiation; • notochord formation; • positive regulation of peptidyl-tyrosine phosphorylation; • substrate adhesion-dependent cell spreading; • cell migration; • negative regulation of epithelial to mesenchymal transition; • negative regulation of dendritic spine morphogenesis; • regulation of peptidyl-tyrosine phosphorylation; • negative regulation of thymocyte apoptotic process; • MAPK cascade; • angiogenesis; • axon guidance; • positive regulation of protein phosphorylation; • negative regulation of MAPK cascade; • positive regulation of MAPK cascade; • protein stabilization; • positive regulation of protein tyrosine kinase activity; • positive regulation of amyloid-beta formation; • positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; • negative regulation of proteolysis involved in cellular protein catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	1942
	13636
	ENSG00000169242
	ENSMUSG00000027954
	P20827
	P52793
	NM_004428; NM_182685
	NM_001162425; NM_010107
	NP_004419; NP_872626
	NP_001155897; NP_034237
	Wikidata
View/Edit Human	View/Edit Mouse

Ephrin A1 is a protein that in humans is encoded by the EFNA1 gene.[5][6][7]

This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. 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. This gene encodes an EFNA class ephrin which binds to the EPHA2, EPHA4, EPHA5, EPHA6, and EPHA7 receptors. Two transcript variants that encode different isoforms were identified through sequence analysis.[7]

Model organisms

*Efna1* knockout mouse phenotype
Characteristic	Phenotype
Homozygote viability	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Abnormal[8]
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal[9]
Plasma immunoglobulins	Normal
Haematology	Normal
Micronucleus test	Normal
Heart weight	Normal
Tail epidermis wholemount	Normal
Brain histopathology	Normal
Salmonella infection	Normal[10]
Citrobacter infection	Normal[11]
All tests and analysis from[12][13]

Model organisms have been used in the study of EFNA1 function. A conditional knockout mouse line, called Efna1^{tm1a(EUCOMM)Wtsi}[14][15] was generated as part of the International Knockout Mouse Consortium program—a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[16][17][18]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[12][19] Twenty four tests were carried out on homozygous mutant mice and one significant abnormality was observed: a transformation in vertebral number from lumbar vertebrae to sacral vertebrae.[12]

References

GRCh38: Ensembl release 89: ENSG00000169242 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000027954 - 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.
Holzman LB, Marks RM, Dixit VM (Nov 1990). "A novel immediate-early response gene of endothelium is induced by cytokines and encodes a secreted protein". Molecular and Cellular Biology. 10 (11): 5830–8. doi:10.1128/mcb.10.11.5830. PMC 361366. PMID 2233719.
Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW (Apr 1996). "The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3". Genomics. 33 (2): 277–82. doi:10.1006/geno.1996.0192. PMID 8660976.
"Entrez Gene: EFNA1 ephrin-A1".
"Radiography data for Efna1". Wellcome Trust Sanger Institute.
"Clinical chemistry data for Efna1". Wellcome Trust Sanger Institute.
"Salmonella infection data for Efna1". Wellcome Trust Sanger Institute.
"Citrobacter infection data for Efna1". Wellcome Trust Sanger Institute.
Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
Mouse Resources Portal, Wellcome Trust Sanger Institute.
"International Knockout Mouse Consortium".
"Mouse Genome Informatics".
Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Pandey A, Lindberg RA, Dixit VM (Sep 1995). "Cell signalling. Receptor orphans find a family". Current Biology. 5 (9): 986–9. doi:10.1016/S0960-9822(95)00195-3. PMID 8542290.
Flanagan JG, Vanderhaeghen P (1998). "The ephrins and Eph receptors in neural development". Annual Review of Neuroscience. 21: 309–45. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499.
Zhou R (Mar 1998). "The Eph family receptors and ligands". Pharmacology & Therapeutics. 77 (3): 151–81. doi:10.1016/S0163-7258(97)00112-5. PMID 9576626.
Holder N, Klein R (May 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". 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 (Jul 2000). "Roles of Eph receptors and ephrins in segmental patterning". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 355 (1399): 993–1002. doi:10.1098/rstb.2000.0635. PMC 1692797. PMID 11128993.
Wilkinson DG (Mar 2001). "Multiple roles of EPH receptors and ephrins in neural development". Nature Reviews. Neuroscience. 2 (3): 155–64. doi:10.1038/35058515. PMID 11256076.
Mahadevan D, Thanki N, Singh J, McPhie P, Zangrilli D, Wang LM, Guerrero C, LeVine H, Humblet C, Saldanha J (Jul 1995). "Structural studies on the PH domains of Db1, Sos1, IRS-1, and beta ARK1 and their differential binding to G beta gamma subunits". Biochemistry. 34 (28): 9111–7. doi:10.1021/bi00028a021. PMID 7619809.
Kozlosky CJ, Maraskovsky E, McGrew JT, VandenBos T, Teepe M, Lyman SD, Srinivasan S, Fletcher FA, Gayle RB, Cerretti DP (Jan 1995). "Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins". Oncogene. 10 (2): 299–306. PMID 7838529.
Davis S, Gale NW, Aldrich TH, Maisonpierre PC, Lhotak V, Pawson T, Goldfarb M, Yancopoulos GD (Nov 1994). "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity". Science. 266 (5186): 816–9. doi:10.1126/science.7973638. PMID 7973638.
Beckmann MP, Cerretti DP, Baum P, Vanden Bos T, James L, Farrah T, Kozlosky C, Hollingsworth T, Shilling H, Maraskovsky E (Aug 1994). "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors". The EMBO Journal. 13 (16): 3757–62. doi:10.1002/j.1460-2075.1994.tb06685.x. PMC 395287. PMID 8070404.
Gale NW, Holland SJ, Valenzuela DM, Flenniken A, Pan L, Ryan TE, Henkemeyer M, Strebhardt K, Hirai H, Wilkinson DG, Pawson T, Davis S, Yancopoulos GD (Jul 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.
Ephnomenclaturecommittee (Aug 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.
Nagel W, Schilcher P, Zeitlmann L, Kolanus W (Aug 1998). "The PH domain and the polybasic c domain of cytohesin-1 cooperate specifically in plasma membrane association and cellular function". Molecular Biology of the Cell. 9 (8): 1981–94. doi:10.1091/mbc.9.8.1981. PMC 25450. PMID 9693361.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000169242 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000027954 - 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.

[pmid2233719-5] Holzman LB, Marks RM, Dixit VM (Nov 1990). "A novel immediate-early response gene of endothelium is induced by cytokines and encodes a secreted protein". Molecular and Cellular Biology. 10 (11): 5830–8. doi:10.1128/mcb.10.11.5830. PMC 361366. PMID 2233719.

[pmid8660976-6] Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW (Apr 1996). "The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3". Genomics. 33 (2): 277–82. doi:10.1006/geno.1996.0192. PMID 8660976.

[entrez-7] "Entrez Gene: EFNA1 ephrin-A1".

[Radiography-8] "Radiography data for Efna1". Wellcome Trust Sanger Institute.

[Clinical_chemistry-9] "Clinical chemistry data for Efna1". Wellcome Trust Sanger Institute.

[''Salmonella''_infection-10] "Salmonella infection data for Efna1". Wellcome Trust Sanger Institute.

[''Citrobacter''_infection-11] "Citrobacter infection data for Efna1". Wellcome Trust Sanger Institute.

[mgp_reference-12] Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.

[13] Mouse Resources Portal, Wellcome Trust Sanger Institute.

[allele_ref-14] "International Knockout Mouse Consortium".

[mgi_allele_ref-15] "Mouse Genome Informatics".

[pmid21677750-16] Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.

[mouse_library-17] Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.

[mouse_for_all_reasons-18] Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.

[pmid21722353-19] van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

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

Ephrin A1

Model organisms

References

Further reading