Not detectable in the forebrain at 11 dpc, weakly detectable at 13 dpc with highest detection at 18 dpc to postnatal day 7. Down-regulated at postnatal day 15 and further reduced in four-week-old animals.
The FIG[AQ]Y motif seems to be an ankyrin recruitment region.
The DGEA motif seems to be a recognition site for integrin.
Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane.
Cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is inhibited by metalloprotease inhibitors. In brain extracts, these two soluble forms are also present and are dramatically reduced in mice lacking ADAM8 (PubMed:14761956). Cleaved by BACE1 (PubMed:29325091).
N-glycosylated. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc).
O-glycosylated.
Belongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family.
Expressed in the brain, in the cerebellum and in the spinal cord. Detected in the retina and the optic nerve. Expressed in neurons and glial cells in the central nervous system and by Schwann cells in the peripheral nervous system.
Call, Chl1, Neural cell adhesion molecule L1-like protein, Cell adhesion molecule with homology to L1CAM, Chl1-like protein, Close homolog of L1
Proteins
Neuroscience
135074Da
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