FLRT2

This gene encodes a member of the fibronectin leucine rich transmembrane (FLRT) family of cell adhesion molecules, which regulate early embryonic vascular and neural development. The encoded type I transmembrane protein has an extracellular region consisting of an N-terminal leucine-rich repeat domain and a type 3 fibronectin domain, followed by a transmembrane domain and a short C-terminal cytoplasmic tail domain. It functions as both a homophilic cell adhesion molecule and a heterophilic chemorepellent through its interaction with members of the uncoordinated-5 receptor family. Proteolytic removal of the extracellular region controls the migration of neurons in the developing cortex. Alternative splicing results in multiple transcript variants.

Fibronectin Leucine Rich Transmembrane Protein 2

Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis.

Axon guidance Source: Ensembl
Basement membrane organization Source: UniProtKB
Cell adhesion involved in heart morphogenesis Source: UniProtKB
Fibroblast growth factor receptor signaling pathway Source: UniProtKB
Heart morphogenesis Source: UniProtKB
Positive regulation of synapse assembly Source: Ensembl
Regulation of neuron migration Source: Ensembl

Endoplasmic reticulum membrane; Microsome membrane; Cell membrane; Extracellular matrix; Secreted; Focal adhesion; Synaptosome. Proteolytic cleavage gives rise to a shedded ectodomain.

Extracellular: 36-541
Helical: 542-562
Cytoplasmic: 563-660

N-glycosylated.
Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease.