leucine-rich repeat & immunoglobulin-like domain-containing nogo receptor-interacting protein 1 (leucine-rich repeat & immunoglobilin-domain containing protein 1, leucine-rich repeat neuronal protein 6A, leucine-rich repeat neuronal protein 1, LINGO1, LERN1, LRRN6A, UNQ201/PRO227)

Function: - functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors - negative regulator of oligodentrocyte differentiation & axonal myelination - N-glycosylated. contains predominantly high-mannose glycans Structure: - homotetramer - forms ternary complex with RTN4R/NGFR & RTN4R/TNFRSF19 - contains 1 Ig-like C2-type domain (immunoglobulin-like) - contains 13 LRR repeats (leucine-rich repeats) Compartment: cell membrane Alternative splicing: named isoforms=2 Expression: - expressed exclusively in the central nervous system - highest level in the in amygdala, hippocampus, thalamus & cerebral cortex - in the rest of the brain a basal expression seems to be always present Pathology: - up-regulated in substantia nigra neurons from patients with Parkinson's disease

General

glycoprotein leucine-rich repeat & immunoglobulin-like domain-containing nogo receptor-interacting protein (LINGO) phosphoprotein

Properties

SIZE: entity length = 620 aa MW = 70 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-41} cysteine residue {C42} MODIFICATION: cysteine residue {C48} cysteine residue {C46} MODIFICATION: cysteine residue {C57} cysteine residue {C48} MODIFICATION: cysteine residue {C42} cysteine residue {C57} MODIFICATION: cysteine residue {C46} leucine-rich repeat SITE: 70-93 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 94-117 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 118-141 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 143-165 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N144} leucine-rich repeat SITE: 166-189 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 190-213 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N202} leucine-rich repeat SITE: 215-237 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 262-285 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N264} N-glycosylation site {N274} leucine-rich repeat SITE: 286-309 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N293} leucine-rich repeat SITE: 311-333 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 334-357 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N341} leucine-rich repeat SITE: 359-383 MOTIF: leucine residue (SEVERAL) cysteine residue {C373} MODIFICATION: cysteine residue {C396} cysteine residue {C375} MODIFICATION: cysteine residue {C421} cysteine residue {C396} MODIFICATION: cysteine residue {C373} immunoglobulin superfamily domain {411-513} MOTIF: cysteine residue {C421} MODIFICATION: cysteine residue {C375} cysteine residue {C446} MODIFICATION: cysteine residue {C497} leucine-rich repeat SITE: 459-484 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N492} cysteine residue {C497} MODIFICATION: cysteine residue {C446} N-glycosylation site {N505} N-glycosylation site {N526} N-glycosylation site {N542} transmembrane domain {562-582} Ser phosphorylation site {S602}

Database Correlations

UniProt Q96FE5 PFAM correlations Kegg hsa:8489

References

UniProt :accession Q96FE5