Primary Information |
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| BoMiProt ID | Bomi5799 |
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| Protein Name | Fibulin-5 |
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| Organism | Bos taurus |
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| Uniprot ID | Q5EA62 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001014946.1 |
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| Aminoacid Length | 448 |
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| Molecular Weight | 50164 |
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| FASTA Sequence |
Download |
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| Gene Name | FBLN5 |
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| Gene ID | 535185 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | rich in elastic fibers including developing arteries and the heart valves, lungs, and skin |
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| Protein Function | mediate binding to human umbilical vein endothelial cells (HUVECs) in a RGD-dependent manner elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN. Stabilizes and organizes elastic fibers in the skin, lung and vasculature. Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling. May act as an adapter that mediates the interaction between FBN1 and ELN. |
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| Biochemical Properties | Homodimer. Monomer, homodimerizes in presence of Ca2+.Fibulin-5 contains an evolutionally conserved RGD sequence in the first cbEGF domain.has an RGD integrin binding site. |
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| Significance in milk | Embryonic development |
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| PTMs | N linked Glycosylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q5EA62|FBLN5_BOVIN Fibulin-5 OS=Bos taurus OX=9913 GN=FBLN5 PE=2 SV=1
MPGFKRILTVTVLALCLPTPGNAQQQCTNGFDLDRSSGQCLDVDECRTIPEACRGDMMCV
NQNGGYLCIPRTNPVYRGPYSNPYSNPYSASYPAAAPPLSAPNYPTISRPLICRFGYQMD
ESNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQL
CANVPGSYSCTCNPGFTLNEDGRSCQDVNECATENPCVQTCVNTYGSFICRCDPGYELED
DGVHCSDMDECSFSEFLCQHECVNQPGTYFCSCPAGYILLDDN*283RSCQDINECEHRN*296HTCI
LQQTCYNLQGGFKCIDPIRCEEPYLRISDNRCMCPAENPGCRDQPFTILYRDMDVVSGRS
VPADIFQMQATTRYPGAYYIFQIKSGNDGREFYMRQTGPISATLVMTRPIKGPRDIQLDL
EMITVNTVINFRGSSVIRLRIYVSQYPF |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Proteolytic cleavage of fibulin-5 has been reported in its N-terminal linker region in aged mice.The resulting fibulin-5 fragment is no longer able to participate in elastogenesis, suggesting that fibulin-5 cleavage may be involved in the aging of elastic tissues. |
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| Additional Comments | Fibulin-5 can protect the ECM of chondrocytes and reduce the inflammatory response of chondrocytes by inhibiting the Wnt/β-catenin signaling pathway.Mice deficient in the fibulin-5 gene (Fbln5) exhibit systemic elastic fiber defects with manifestations of loose skin, tortuous aorta, emphysematous lung and genital prolapse. |
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| Bibliography | Yanagisawa H, Schluterman MK, Brekken RA. Fibulin-5, an integrin-binding matricellular protein: its function in development and disease. J Cell Commun Signal. 2009 Dec;3(3-4):337-47. doi: 10.1007/s12079-009-0065-3. Epub 2009 Oct 2. PMID: 19798595; PMCID: PMC2778585. |
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