Reeler domain (IPR002861)

Short name: Reeler_dom

Overlapping homologous superfamilies


Domain relationships



The reeler or reelin domain is a ~170 amino acid module, which has been identified in the amino terminus of the extracellular matrix proteins reelin and F-spondin (renamed Spon1) [PMID: 18602404, PMID: 19020352]. The reelin domain is found in association with other modules, such as the thrombospondin type I repeat (TSP1), the spondin domain, the fibronectin type III domain or the Kunitz trypsin protease inhibitor domain. Its function is not yet known [PMID: 9441663, PMID: 10409509].

Extracellular matrix (ECM) proteins play an important role in early cortical development, specifically in the formation of neural connections and in controlling the cyto-architecture of the central nervous system. The product of the reeler gene in mouse is reelin,a large extracellular protein secreted by pioneer neurons that coordinates cell positioning during neurodevelopment [PMID: 9338784]. F-spondin and mindin are a family of matrix-attached adhesion molecules that share structural similarities and overlapping domains of expression. Both F-spondin and mindin promote adhesion and outgrowth of hippocampal embryonic neurons and bind to a putative receptor(s) expressed on both hippocampal and sensory neurons [PMID: 10409509].

Contributing signatures

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