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A disintegrin & metalloproteinase domain 19; meltrin-beta; metalloprotease & disintegrin dendritic antigen marker; MADDAM (ADAM19, MLTNB, FKSG34)
Function:
- role in proteolytic processing of beta neuregulin isoforms
- possible regulatory role in glial cells
- also cleaves alpha-2 macroglobulin
- may be involved in osteoblast differentiation &/or osteoblast activity in bone
- interacts with SH3PXD2A
- precursor is cleaved by a furin endopeptidase
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure:
- the conserved Cys present in the cysteine-switch motif binds the catalytic Zn+2, thus inhibiting the enzyme
- dissociation of Cys from the Zn+2 upon the activation- peptide release activates the enzyme
- contains 1 disintegrin domain
- contains 1 EGF-like domain
- contains 1 peptidase M12B domain
Compartment: membrane
Alternative splicing: named isoforms=2; A, B
Expression:
- expressed in many normal organ tissues & several cancer cell lines
- induced by calcitriol in monocytes
General
ADAM (A disintegrin & metalloproteinase domain); MDC (metalloproteinase, disintegrin, cysteine-rich) protein
glycoprotein
Properties
SIZE: entity length = 956 aa
MW = 105 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-25}
Cysteine switch {131-138}
MOTIF: Zn+2-binding site
SITE: 133-133
N-glycosylation site {N145}
Peptidase M12B {211-409}
MOTIF: cysteine residue {C321}
MODIFICATION: cysteine residue {C404}
Zn+2-binding site
SITE: 346-346
glutamate residue {E347}
Zn+2-binding site
SITE: 350-350
Zn+2-binding site
SITE: 356-356
cysteine residue {C361}
MODIFICATION: cysteine residue {C388}
cysteine residue {C362}
MODIFICATION: cysteine residue {C371}
cysteine residue {C371}
MODIFICATION: cysteine residue {C362}
cysteine residue {C388}
MODIFICATION: cysteine residue {C361}
cysteine residue {C404}
MODIFICATION: cysteine residue {C321}
disintegrin domain {417-503}
MOTIF: glutamate-rich region {435-438}
MOTIF: glutamate residue (SEVERAL)
N-glycosylation site {N445}
N-glycosylation site {N448}
cysteine residue {C475}
MODIFICATION: cysteine residue {C495}
cysteine residue {C495}
MODIFICATION: cysteine residue {C475}
cysteine-rich region {503-650}
MOTIF: N-glycosylation site {N646}
EGF domain {651-683}
MOTIF: cysteine residue {C655}
MODIFICATION: cysteine residue {C665}
cysteine residue {C659}
MODIFICATION: cysteine residue {C671}
cysteine residue {C665}
MODIFICATION: cysteine residue {C655}
cysteine residue {C671}
MODIFICATION: cysteine residue {C659}
cysteine residue {C673}
MODIFICATION: cysteine residue {C682}
cysteine residue {C682}
MODIFICATION: cysteine residue {C673}
transmembrane domain {701-721}
SH3-binding site
NAME: SH3-binding site
SITE: 834-840
SH3-binding site
NAME: SH3-binding site
SITE: 839-845
Database Correlations
OMIM 603640
UniProt Q9H013
PFAM correlations
Entrez Gene 8728
Kegg hsa:8728
References
UniProt :accession Q9H013