P52793 · EFNA1_MOUSE
- ProteinEphrin-A1
- GeneEfna1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids205 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEphrin-A1
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP52793
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor, GPI-anchor
Ephrin-A1, secreted form
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MEFLWAPLLGLCCSLAA | ||||||
Chain | PRO_0000389631 | 18-? | Ephrin-A1, secreted form | |||
Sequence: MEFLWAPLLGLCCSLAA | ||||||
Chain | PRO_0000008355 | 18-182 | Ephrin-A1 | |||
Sequence: ADRHIVFWNSSNPKFREEDYTVHVQLNDYLDIICPHYEDDSVADAAMERYTLYMVEHQEYVACQPQSKDQVRWNCNRPSAKHGPEKLSEKFQRFTPFILGKEFKEGHSYYYISKPIYHQESQCLKLKVTVNGKITHNPQAHVNPQEKRLQADDPEVQVLHSIGYS | ||||||
Glycosylation | 26 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 51↔92 | |||||
Sequence: CPHYEDDSVADAAMERYTLYMVEHQEYVACQPQSKDQVRWNC | ||||||
Disulfide bond | 80↔140 | |||||
Sequence: CQPQSKDQVRWNCNRPSAKHGPEKLSEKFQRFTPFILGKEFKEGHSYYYISKPIYHQESQC | ||||||
Lipidation | 182 | GPI-anchor amidated serine | ||||
Sequence: S | ||||||
Propeptide | PRO_0000008356 | 183-205 | Removed in mature form | |||
Sequence: AAPRLFPLVWAVLLLPLLLLQSQ |
Post-translational modification
Undergoes proteolysis by a metalloprotease to give rise to a soluble monomeric form.
N-Glycosylation is required for binding to EPHA2 receptor and inducing its internalization.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in myogenic progenitor cells.
Developmental stage
In myogenic progenitor cells, expressed during the acquisition of muscle stem cell properties, from 18.5 dpc to adulthood.
Gene expression databases
Interaction
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 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P52793 | EPHA7 Q15375 | 2 | EBI-5241529, EBI-1383428 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-161 | Ephrin RBD | ||||
Sequence: ADRHIVFWNSSNPKFREEDYTVHVQLNDYLDIICPHYEDDSVADAAMERYTLYMVEHQEYVACQPQSKDQVRWNCNRPSAKHGPEKLSEKFQRFTPFILGKEFKEGHSYYYISKPIYHQESQCLKLKVTVNGKITHNPQAHVNP |
Sequence similarities
Belongs to the ephrin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length205
- Mass (Da)23,802
- Last updated1996-10-01 v1
- Checksum5A8F3A6E2091E868
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 74 | in Ref. 1; BAA07344 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 79 | in Ref. 1; BAA07344 | ||||
Sequence: A → T | ||||||
Sequence conflict | 81 | in Ref. 1; BAA07344 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 91 | in Ref. 1; BAA07344 | ||||
Sequence: N → K | ||||||
Sequence conflict | 94 | in Ref. 1; BAA07344 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 112 | in Ref. 1; BAA07344 | ||||
Sequence: T → S | ||||||
Sequence conflict | 115 | in Ref. 1; BAA07344 | ||||
Sequence: I → T | ||||||
Sequence conflict | 138 | in Ref. 1; BAA07344 | ||||
Sequence: S → T | ||||||
Sequence conflict | 154 | in Ref. 1; BAA07344 | ||||
Sequence: N → S | ||||||
Sequence conflict | 156 | in Ref. 1; BAA07344 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 159 | in Ref. 1; BAA07344 | ||||
Sequence: V → A | ||||||
Sequence conflict | 181 | in Ref. 1; BAA07344 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 204 | in Ref. 1; BAA07344 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D38146 EMBL· GenBank· DDBJ | BAA07344.1 EMBL· GenBank· DDBJ | mRNA | ||
U26188 EMBL· GenBank· DDBJ | AAA67563.1 EMBL· GenBank· DDBJ | mRNA | ||
U90662 EMBL· GenBank· DDBJ | AAB50237.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002046 EMBL· GenBank· DDBJ | AAH02046.1 EMBL· GenBank· DDBJ | mRNA |