Pro-neuregulin-4, membrane-bound isoform
Domain
The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization (By similarity).
ERBB receptor binding is elicited entirely by the EGF-like domain.
Function
Low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Does not bind to the ERBB1, ERBB2 and ERBB3 receptors (By similarity).
Post-translational modifications
Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.
Extensive glycosylation precedes the proteolytic cleavage.
Sequence Similarities
Belongs to the neuregulin family.
Cellular localization
- Pro-neuregulin-4, membrane-bound isoform
- Cell membrane
- Single-pass type I membrane protein
- Does not seem to be active.
- Neuregulin-4
- Secreted
Alternative names
Pro-NRG4, NRG4