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Description

Neural cell adhesion molecule L1-like protein (UniProt: P70232, also known as Cell adhesion molecule with homology to L1CAM, NCAM-L1, Chl1-like protein, Close homolog of L1) is encoded by the Chl1 (also known as Call) gene (Gene ID: in murine species. NCAM-L1 is a single-pass type I membrane protein that is synthesized with a signal peptide (aa 1-25), which is subsequently cleaved off in the mature form. It is expressed in neurons and glial cells in the brain and the spinal cord and has also been detected in the retina and the optic nerve. It is not detectable in mouse forebrain at E11 and becomes weakly detectable at E13 with highest detection at E18 to postnatal day 7. It is down-regulated at postnatal day 15 and is further reduced in four-week-old animals. NCAM-L1 is heavily N-glycosylated and contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1. NCAM-L1 contains an extracellular domain (aa 26-1083), a transmembrane domain (aa 1084-1104), and a cytoplasmic domain (aa 1105-1209). It also has six Ig-like C2 type domains and four fibronectin type -III domains. NCAM-L1 is an extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. It 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.