ID:EFNA1_HUMAN DESCRIPTION: RecName: Full=Ephrin-A1; AltName: Full=EPH-related receptor tyrosine kinase ligand 1; Short=LERK-1; AltName: Full=Immediate early response protein B61; AltName: Full=Tumor necrosis factor alpha-induced protein 4; Short=TNF alpha-induced protein 4; Contains: RecName: Full=Ephrin-A1, secreted form; Flags: Precursor; FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis. SUBUNIT: Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and EPHA7. Also binds with low affinity to EPHA1. INTERACTION: P29317:EPHA2; NbExp=5; IntAct=EBI-715194, EBI-702104; SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SUBCELLULAR LOCATION: Ephrin-A1, secreted form: Secreted. TISSUE SPECIFICITY: Brain. Down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells (at protein level). INDUCTION: By TNF and IL1B/interleukin-1 beta. PTM: Undergoes proteolysis by a metalloprotease to give rise to a soluble monomeric form. SIMILARITY: Belongs to the ephrin family. SIMILARITY: Contains 1 ephrin RBD (ephrin receptor-binding) domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P20827
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.