Search by BoMiProt ID - Bomi5799

Primary Information

BoMiProt ID Bomi5799
Protein Name Fibulin-5
Organism Bos taurus
Uniprot IDQ5EA62
Milk FractionWhey
Ref Sequence ID NP_001014946.1
Aminoacid Length 448
Molecular Weight 50164
FASTA Sequence Download
Gene Name FBLN5
Gene ID 535185
Protein Existence Status reviewed

Secondary Information

Presence in other biological fluids/tissue/cells rich in elastic fibers including developing arteries and the heart valves, lungs, and skin
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.
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.
Significance in milk Embryonic development
PTMs N linked Glycosylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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.
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.
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.