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A disintegrin & metalloproteinase domain 30 (ADAM30)
Function:
- may be involved in spermatogenesis & fertilization
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure:
- conserved Cys present in the cysteine-switch motif binds the catalytic Zn+2, thus inhibiting the enzyme
- dissociation of Cys from 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; alpha, beta
Expression: expressed specifically in testis
General
ADAM (A disintegrin & metalloproteinase domain); MDC (metalloproteinase, disintegrin, cysteine-rich) protein
glycoprotein
testis-specific protein
Properties
SIZE: MW = 89 kD
entity length = 790 aa
COMPARTMENT: cellular compartment
CELL: unspecified cell type
WITHIN: testis
MOTIF: metalloprotease domain {199-393}
MOTIF: N-glycosylation site {N222}
cysteine residue {C313}
MODIFICATION: cysteine residue {C388}
active site
SITE: E339
cysteine residue {C353}
MODIFICATION: cysteine residue {C373}
N-glycosylation site {N372}
cysteine residue {C373}
MODIFICATION: cysteine residue {C353}
cysteine residue {C388}
MODIFICATION: cysteine residue {C313}
disintegrin domain {399-485}
MOTIF: N-glycosylation site {N438}
cysteine residue {C457}
MODIFICATION: cysteine residue {C470}
cysteine residue {C470}
MODIFICATION: cysteine residue {C457}
N-glycosylation site {N473}
cysteine-rich region {486-632}
MOTIF: N-glycosylation site {N625}
EGF domain {629-663}
MOTIF: cysteine residue {C633}
MODIFICATION: cysteine residue {C644}
cysteine residue {C638}
MODIFICATION: cysteine residue {C650}
cysteine residue {C644}
MODIFICATION: cysteine residue {C633}
cysteine residue {C650}
MODIFICATION: cysteine residue {C638}
cysteine residue {C652}
MODIFICATION: cysteine residue {C661}
cysteine residue {C661}
MODIFICATION: cysteine residue {C652}
transmembrane domain {688-708}
Database Correlations
OMIM 604779
UniProt Q9UKF2
PFAM correlations
Entrez Gene 11085
Kegg hsa:11085
References
UniProt :accession Q9UKF2