motifs/domains
| invariant cysteine residues, 12 N terminal, 6 C terminal, a N terminal IGFBP motif (containing only one high-affinity binding site for IGF) |
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divided in 3 parts which are N-, L- and C- region (L-region is composed of a flexible linker structure and N- and C-regions closely contact for stabilizing their charge) |
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a central domain lacking cysteine residue, with a RGD motif |
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a 13kDa C terminal fragment (with intrinsic biological functions) |
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also a nuclear localization signal (NLS) |
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one thyroglobulin type-I domain |
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a mini-IGFBP5 (AAs 40–92 of the N domain) containing a hydrophobic IGF-binding site within a novel protein fold, and mutations of key hydrophobic AAs within this region of IGFBP5 and the equivalent region of IGFBP3 dramatically reduces the affinity for IGF binding |
basic FUNCTION
| insulin-like growth factor binding protein 5, high affinity, involved in regulation of cell growth |
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having an important role in controlling cell survival, differentiation and apoptosis |
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having IGF-independent actions during development |
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activates GNAI3 and regulates smooth muscle growth, IGF1 production, and collagen production via the alpha-subunit of GNAI3, independently of IGF1, in normal human intestinal muscle cells) |
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role in the control of growth and metabolism |
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induces formation of a FLNA-based nuclear shuttle that recruits transcription factors and regulates transcription of IGFBP5 target genes |
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has an effect on human hair shape |
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play an important role in breast cancer biology, especially in breast cancer metastasis |
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SRC and IL6 inhibit osteoblast differentiation and integrate IGFBP5 signalling |