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neural cell adhesion molecule L1-like protein (close homolog of L1, CHL1, CALL)
Function:
1) extracellular matrix & cell adhesion protein
2) nervous system development
3) synaptic plasticity
4) both soluble & membranous forms
a) promote neurite outgrowth of cerebellar & hippocampal neurons
b) suppress neuronal cell death
5) neuronal positioning of pyramidal neurons
6) regulation of both the number of interneurons & the efficacy of GABAergic synapses
7) regulation of cell migration in nerve regeneration & cortical development
8) potentiation of integrin-dependent cell migration towards extracellular matrix proteins
- DGEA motif seems to be a recognition site for integrin
9) recruits ANK3 to the plasma membrane
- FIG[AQ]Y motif seems to be an ankyrin recruitment
10) may interact with L1CAM, ITGB1/ITGA1, ITGB1/ITGA2, ANK3
11) cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kD, 165 kD) in vitro
Structure:
- N-glycosylated
- contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc)
- O-glycosylated
Compartment: membrane
Alternative splicing: named isoforms=2
Expression:
- expressed in the fetal & adult brain, Schwann cell culture
- also detected in adult peripheral tissues
Pathology:
- deletion of 1 copy of the CHL1 gene may be responsible for mental defects in patients with 3p deletion syndrome
General
adhesion receptor
glycoprotein
Properties
SIZE: MW = 135 kD
entity length = 1208 aa
COMPARTMENT: plasma membrane
MOTIF: signal sequence {1-24}
immunoglobulin superfamily domain {35-124}
MOTIF: cysteine residue {C57}
MODIFICATION: cysteine residue {C109}
cysteine residue {C109}
MODIFICATION: cysteine residue {C57}
immunoglobulin superfamily domain {128-223}
MOTIF: cysteine residue {C153}
MODIFICATION: cysteine residue {C204}
cysteine residue {C204}
MODIFICATION: cysteine residue {C153}
immunoglobulin superfamily domain {235-328}
MOTIF: cysteine residue {C262}
MODIFICATION: cysteine residue {C310}
N-glycosylation site {N299}
cysteine residue {C310}
MODIFICATION: cysteine residue {C262}
immunoglobulin superfamily domain {331-417}
MOTIF: cysteine residue {C352}
MODIFICATION: cysteine residue {C401}
cysteine residue {C401}
MODIFICATION: cysteine residue {C352}
immunoglobulin superfamily domain {423-510}
MOTIF: cysteine residue {C445}
MODIFICATION: cysteine residue {C494}
N-glycosylation site {N476}
N-glycosylation site {N482}
cysteine residue {C494}
MODIFICATION: cysteine residue {C445}
immunoglobulin superfamily domain {515-607}
MOTIF: cysteine residue {C536}
MODIFICATION: cysteine residue {C591}
N-glycosylation site {N562}
N-glycosylation site {N580}
cysteine residue {C591}
MODIFICATION: cysteine residue {C536}
fibronectin type III domain or F3 module {612-704}
fibronectin type III domain or F3 module {711-804}
MOTIF: proteolytic site {753-754}
N-glycosylation site {N767}
fibronectin type III domain or F3 module {809-911}
MOTIF: N-glycosylation site {N822}
fibronectin type III domain or F3 module {916-1011}
MOTIF: N-glycosylation site {N945}
N-glycosylation site {N1026}
proteolytic site {1039-1040}
transmembrane domain {1083-1103}
Database Correlations
OMIM 607416
UniProt O00533
PFAM correlations
References
UniProt :accession O00533