描述：
Osteoactivin (also GPNMB and DC-HIL) is a variably glycosylated 75 -125 kDa member of the
NMB/pMEL-17 family of molecules. It is found in multiple subcellular sites, but is most often
associated with the endosomal/lysosomal compartment. Human Osteoactivin is a 560 amino
acid (aa) type I transmembrane protein. Its precursor contains a 21 aa signal sequence, a 465
aa luminal/extracellular domain, a 21 aa transmembrane segment and a 53 aa cytoplasmic tail.
The luminal region contains an N-terminal heparin-binding motif (aa 23-26), multiple
glycosylation sites, an RGD motif (aa 64-66) and an 88 aa PKD domain (aa 240-327). The
intracellular tail has an ITAM (Y-x-x-I) and lysosomal targeting (LL) motif. The extracellular/
luminal region shares 74% and 77% aa identity with the equivalent regions in mouse and canine,
respectively. Multiple isoforms would appear to exist. There is one alternate splice form known
that shows a 12 aa insert between aa 339-340. An addtional 206 aa isoform shows a mutation
at position # 181 that results in a 26 aa substitution for the C-terminal 380 amino acids. This has
the potential to be soluble and may represent a counterpart to a secreted isoform of rat
Osteoactivin. Cells known to express Osteoactivin include macrophages/Kupffer cells, fibroblasts,
osteoblasts, myeloid dendritic cells, retinal pigment epithelial cells and melanocytes, plus fetal
chondrocytes and stratum basale keratinocytes. In mice, Osteoactivin is reported to bind to
heparan sulfateproteoglycan, possibly on the surface of endothelial cells and may also interact
with integrins. It also appears to act as an inflammatory suppressor gene, as its expression
downregulates the macrophage inflammatory response by inhibiting IL-6 and IL-12p40
production.
原厂资料：
Osteoactivin (also GPNMB and DC-HIL) is a variably glycosylated 75 -125 kDa member of the
NMB/pMEL-17 family of molecules. It is found in multiple subcellular sites, but is most often
associated with the endosomal/lysosomal compartment. Human Osteoactivin is a 560 amino
acid (aa) type I transmembrane protein. Its precursor contains a 21 aa signal sequence, a 465
aa luminal/extracellular domain, a 21 aa transmembrane segment and a 53 aa cytoplasmic tail.
The luminal region contains an N-terminal heparin-binding motif (aa 23-26), multiple
glycosylation sites, an RGD motif (aa 64-66) and an 88 aa PKD domain (aa 240-327). The
intracellular tail has an ITAM (Y-x-x-I) and lysosomal targeting (LL) motif. The extracellular/
luminal region shares 74% and 77% aa identity with the equivalent regions in mouse and canine,
respectively. Multiple isoforms would appear to exist. There is one alternate splice form known
that shows a 12 aa insert between aa 339-340. An addtional 206 aa isoform shows a mutation
at position # 181 that results in a 26 aa substitution for the C-terminal 380 amino acids. This has
the potential to be soluble and may represent a counterpart to a secreted isoform of rat
Osteoactivin. Cells known to express Osteoactivin include macrophages/Kupffer cells, fibroblasts,
osteoblasts, myeloid dendritic cells, retinal pigment epithelial cells and melanocytes, plus fetal
chondrocytes and stratum basale keratinocytes. In mice, Osteoactivin is reported to bind to
heparan sulfateproteoglycan, possibly on the surface of endothelial cells and may also interact
with integrins. It also appears to act as an inflammatory suppressor gene, as its expression
downregulates the macrophage inflammatory response by inhibiting IL-6 and IL-12p40
production.
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