Ephrin A1

From Wikipedia, the free encyclopedia

Ephrin-A1

Rendering based on PDB 3CZU.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3HEI, 3MBW

Identifiers

Symbols

EFNA1; B61; ECKLG; EFL1; EPLG1; LERK-1; LERK1; TNFAIP4

External IDs

OMIM: 191164 MGI: 103236 HomoloGene: 3262 GeneCards: EFNA1 Gene

Gene Ontology
Molecular function	• receptor binding • protein binding • ephrin receptor binding
Cellular component	• extracellular region • integral to plasma membrane • anchored to plasma membrane
Biological process	• negative regulation of transcription from RNA polymerase II promoter • activation of MAPK activity • angiogenesis • aortic valve morphogenesis • mitral valve morphogenesis • endocardial cushion to mesenchymal transition involved in heart valve formation • cell-cell signaling • negative regulation of epithelial to mesenchymal transition • notochord formation • cell migration • neuron differentiation • regulation of cell adhesion mediated by integrin • substrate adhesion-dependent cell spreading • regulation of blood vessel endothelial cell migration • regulation of angiogenesis • ephrin receptor signaling pathway • regulation of peptidyl-tyrosine phosphorylation • positive regulation of peptidyl-tyrosine phosphorylation • regulation of axonogenesis • negative regulation of dendritic spine morphogenesis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
155.1 – 155.11 Mb

Chr 3:
89.27 – 89.28 Mb

PubMed search

Ephrin-A1 is a protein that in humans is encoded by the EFNA1 gene.^[1]^[2]^[3]

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.^[3]

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^[4]
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal^[5]
Plasma immunoglobulins	Normal
Haematology	Normal
Micronucleus test	Normal
Heart weight	Normal
Tail epidermis wholemount	Normal
Brain histopathology	Normal
Salmonella infection	Normal^[6]
Citrobacter infection	Normal^[7]
All tests and analysis from^[8]^[9]

Model organisms have been used in the study of EFNA1 function. A conditional knockout mouse line, called Efna1^{tm1a(EUCOMM)Wtsi}^[10]^[11] 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.^[12]^[13]^[14]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[8]^[15] 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. ^[8]

References

↑ Holzman LB, Marks RM, Dixit VM (Dec 1990). "A novel immediate-early response gene of endothelium is induced by cytokines and encodes a secreted protein". Mol Cell Biol 10 (11): 5830–8. PMC 361366. PMID 2233719.
↑ Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW (Jan 1997). "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.
↑ 3.0 3.1 "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.
↑ 8.0 8.1 8.2 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, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
↑ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
↑ Collins FS, Rossant J, Wurst W (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 Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Pandey A, Lindberg RA, Dixit VM (1996). "Cell signalling. Receptor orphans find a family.". Curr. Biol. 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.". 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. PMID 10207129.
Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly.". Int. Rev. Cytol. 196: 177–244. doi:10.1016/S0074-7696(00)96005-4. 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.
Mahadevan D, Thanki N, Singh J, et al. (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, et al. (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, et al. (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, et al. (1994). "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors.". EMBO J. 13 (16): 3757–62. PMC 395287. PMID 8070404.
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. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474.
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.
Nagel W, Schilcher P, Zeitlmann L, Kolanus W (1998). "The PH domain and the polybasic c domain of cytohesin-1 cooperate specifically in plasma membrane association and cellular function.". Mol. Biol. Cell 9 (8): 1981–94. PMC 25450. PMID 9693361.

v t e Intercellular signaling peptides and proteins / ligands

Growth factors	Endothelial growth factor Epidermal growth factor Fibroblast growth factor Nerve growth factor Platelet-derived growth factor Transforming growth factor beta superfamily

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 B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

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Ephrin A1

Model organisms

References

References

Further reading