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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