Fibulin-2 (IPR037286)

Short name: Fibulin-2

Overlapping homologous superfamilies


Family relationships



Fibulins are a family of ECM glycoproteins characterized by a fibulin-type C-terminal domain preceded by tandem calcium-binding epidermal growth factor (EGF)-like modules. They are involved in protein-protein interaction with the components of basement membrane and extracellular matrix proteins. There are five fibulins, which can be classified into two subgroups. Fibulin-1 and -2 constitute one subgroup. These fibulins are larger than the others due to the presence of a higher number of EGF modules and an extra domain with three anaphylatoxin modules [PMID: 17324935]. Members of the second subgroup, fibulin-3, -4, and -5, are similarly small in size and highly homologous to one another in modular structure. They consist of a modified cbEGF domain at the N terminus followed by five tandem cbEGF modules and the fibulin-type C-terminal region.

Fibulin-2 is the largest of all the fibulins, because it possesses an additional N-terminal domain not found in other fibulins. Fibulin-2 and fibulin-1 overlap in their binding patterns, which ligands that include fibronectin, proteoglycans, tropoelastin, and various elastic fibre and basement membrane proteins. Only a couple of ligands are specific for fibulin-1 (fibrinogen and laminin-1) and for fibulin-2 (fibrillin-1 and perlecan) [PMID: 12778127]. Expression of the fibulin-2 initiates later than fibulin-1 during embryonic development and is distributed in a more restricted manner.

GO terms

Biological Process

GO:0030198 extracellular matrix organization

Molecular Function

GO:0005515 protein binding

Cellular Component

GO:0062023 collagen-containing extracellular matrix

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.