Contents

Search


neuregulin-2, neural-& thymus-derived activator for ERBB kinases; divergent of neuregulin 1; DON-1 (NRG2, NTAK1)

Function: - direct ligand for ERBB3 receptor & ERBB4 receptors - concomitantly recruits ERBB1 oreceptor & ERBB2 coreceptor, resulting in ligand-stimulated Tyr phosphorylation & activation of the ERBB receptors - may also promote heterodimerization with the EGF receptor - proteolytic cleavage close to the plasma membrane on the external face leads to the release of soluble growth factor form (putative) - extensive glycosylation precedes the proteolytic cleavage - interacts with ERBB3 & ERBB4 Structure: - the cytoplasmic domain may be involved in regulation of trafficking & proteolytic processing - regulation of proteolytic processing involves initial intracellular domain dimerization (putative) - ERBB receptor binding is elicited entirely by the EGF-like domain (putative) - belongs to the neuregulin family - contains 1 EGF-like domain - contains 1 Ig-like C2-type domain Compartment: - pro-neuregulin-2 - cell membrane; single-pass type 1 membrane protein - does not seem to be active (putative) - neuregulin-2: secreted (putative) Alternative splicing: named isoforms=8 Expression: restricted to the cerebellum in the adult

General

glycoprotein neuregulin phosphoprotein

Properties

SIZE: entity length = 850 aa MW = 92 kD COMPARTMENT: cellular membrane MOTIF: proline-rich region SITE: 10-13 MOTIF: proline residue (SEVERAL) serine-rich region {20-30} MOTIF: serine residue (SEVERAL) serine-rich region {33-47} MOTIF: serine residue (SEVERAL) N-glycosylation site {N52} N-glycosylation site {N53} alanine-rich region {87-90} MOTIF: alanine residue (SEVERAL) N-glycosylation site {N147} immunoglobulin superfamily domain {237-332} MOTIF: cysteine residue {C257} MODIFICATION: cysteine residue {C311} N-glycosylation site {N278} cysteine residue {C311} MODIFICATION: cysteine residue {C257} threonine-rich region {330-340} MOTIF: threonine residue (SEVERAL) EGF domain {341-382} MOTIF: cysteine residue {C345} MODIFICATION: cysteine residue {C359} N-glycosylation site {N346} cysteine residue {C353} MODIFICATION: cysteine residue {C370} cysteine residue {C359} MODIFICATION: cysteine residue {C345} cysteine residue {C370} MODIFICATION: cysteine residue {C353} cysteine residue {C372} MODIFICATION: cysteine residue {C381} cysteine residue {C381} MODIFICATION: cysteine residue {C372} transmembrane domain {406-426} proline-rich region SITE: 721-727 MOTIF: proline residue (SEVERAL) Ser phosphorylation site {S809}

Database Correlations

OMIM 603818 UniProt O14511 PFAM correlations Entrez Gene 9542 Kegg hsa:9542

References

UniProt :accession O14511