| Relevance | ADAM19, is a member of the ADAM (a disintegrin and metalloprotease-like domain) family. It has been cloned from mouse and human. ADAM19 was first described in muscle cells as a protein with homology to the fertilins (ADAMs 1 and 2). Initial observations indicated a role for ADAM19 in myoblast fusion, similar to sperm-egg fusion aided by ADAMs 1 and 2. Later works describe ADAM19 in the bone, muscle, lung, heart, brain, kidney, and a wide range of tissues.
The Cytoplasmic domain of ADAM19, like ADAMs 9, 12 and 15, contains SH3 ligand domains, which are thought to interact with PKC-d, suggesting specific regulation routes for ADAM19. Also reported is a sequence of ADAM19 lacking the transmembrane and cytoplasmic domains, suggesting that a soluble form is produced.
ADAM-19 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active. Other ADAMs family members (ADAM-10, ADAM-17) have been more thoroughly studied, and are known to play key roles in inflammation, growth factor maturation and release, and a wide range of other functions. The full length ADAM19 sequence codes for a 956 amino acid protein, containing a Type-I transmembrane domain, with a predicted mass is 105 kD. Two shorter sequences have been reported: a 918 amino acid sequence that differs at the carboxyterminal end, and the soluble form, a 538 amino acid version with predicted mass of 59.9 kD. Mouse ADAM19 sequence is 920 AA, predicted at 100.86 kD.
ADAM19 may be important in osteoblast differentiation, as a marker for dendritic cell differentiation, and in the intracellular processing of neuregulin. The ADAMs proteins are structurally similar, possessing a signal sequence, metalloprotease domain (inactive in some ADAMs), disintegrin domain, cysteinrich domain, EGF-like repeat, type-I transmembrane domain, and cytoplasmic domain. The function of ADAM-19 is still poorly understood.
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