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A disintegrin & metalloproteinase domain 9; metalloprotease/disintegrin/cysteine-rich protein 9; myeloma cell metalloproteinase; meltrin gamma (ADAM9, KIAA0021, MCMP, MDC9, MLTNG)

Function: - probable Zn+2 protease - may mediate cell-cell or cell-matrix interactions - isoform 2 displays alpha-secretase activity for APP - interacts with MAD2L2 - cytoplasmic domain interacts with SH3 domain of endophilin 1 & protein kinase C Cofactor: binds 1 Zn+2 per subunit (probable) Structure: - contains 1 disintegrin domain - contains 1 EGF-like domain - contains 1 peptidase M12B domain Compartment: - isoform 1: cell membrane - isoform 2: secreted Alternative splicing: named isoforms=2 Expression: - widely expressed - expressed in chondrocytes - highest expression of isoform 2 found in liver & heart Note: has sometimes been referred to as ADAM-12

General

ADAM (A disintegrin & metalloproteinase domain); MDC (metalloproteinase, disintegrin, cysteine-rich) protein glycoprotein phosphoprotein

Properties

SIZE: entity length = 819 aa MW = 91 kD MOTIF: signal sequence {1-28} N-glycosylation site {N125} N-glycosylation site {N144} N-glycosylation site {N154} Peptidase M12B {212-406} MOTIF: N-glycosylation site {N231} cysteine residue {C322} MODIFICATION: cysteine residue {C401} Zn+2-binding site SITE: 347-347 glutamate residue {E348} Zn+2-binding site SITE: 351-351 Zn+2-binding site SITE: 357-357 cysteine residue {C363} MODIFICATION: cysteine residue {C385} cysteine residue {C365} MODIFICATION: cysteine residue {C370} cysteine residue {C370} MODIFICATION: cysteine residue {C365} N-glycosylation site {N381} cysteine residue {C385} MODIFICATION: cysteine residue {C363} cysteine residue {C401} MODIFICATION: cysteine residue {C322} disintegrin domain {414-501} MOTIF: cysteine residue {C473} MODIFICATION: cysteine residue {C493} N-glycosylation site {N487} cysteine residue {C493} MODIFICATION: cysteine residue {C473} cysteine-rich region {505-634} EGF domain {644-698} MOTIF: cysteine residue {C644} MODIFICATION: cysteine residue {C656} cysteine residue {C650} MODIFICATION: cysteine residue {C662} cysteine residue {C656} MODIFICATION: cysteine residue {C644} cysteine residue {C662} MODIFICATION: cysteine residue {C650} cysteine residue {C664} MODIFICATION: cysteine residue {C673} cysteine residue {C673} MODIFICATION: cysteine residue {C664} transmembrane domain {698-718} Ser phosphorylation site {S758} Thr phosphorylation site {T761} proline-rich region SITE: 790-795 MOTIF: proline residue (SEVERAL) Tyr phosphorylation site {Y815}

Database Correlations

OMIM 602713 UniProt Q13443 PFAM correlations Entrez Gene 8754 Kegg hsa:8754

References

  1. OMIM :accession 602713
  2. Yong VW et al Metalloproteinases in biology and pathology of the nervous system. Nat Rev Neurosci. 2001 Jul;2(7):502-11. Review. PMID: 11433375
  3. UniProt :accession Q13443