Q9D1T0 · LIGO1_MOUSE
- ProteinLeucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
- GeneLingo1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids614 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination (By similarity).
Acts in conjunction with RTN4 and RTN4R in regulating neuronal precursor cell motility during cortical development
Acts in conjunction with RTN4 and RTN4R in regulating neuronal precursor cell motility during cortical development
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Cellular Component | glutamatergic synapse | |
Cellular Component | plasma membrane | |
Cellular Component | presynapse | |
Molecular Function | epidermal growth factor receptor binding | |
Biological Process | central nervous system neuron development | |
Biological Process | negative regulation of oligodendrocyte differentiation | |
Biological Process | negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | |
Biological Process | neuron projection development | |
Biological Process | oligodendrocyte differentiation |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLeucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D1T0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 36-555 | Extracellular | ||||
Sequence: CPPRCECSAQDRAVLCHRKRFVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTPNCLYGLNLTSLSITHCNLTAVPYLAVRHLVYLRFLNLSYNPIGTIEGSMLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESAFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQPTCATPEFVQGKEFKDFPDVLLPNYFTCRRAHIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHVRSYSPDWPHQPNKTFAFISNQPGEGEANSTRATVPFPFDIKTLIIAT | ||||||
Transmembrane | 556-576 | Helical | ||||
Sequence: TMGFISFLGVVLFCLVLLFLW | ||||||
Topological domain | 577-614 | Cytoplasmic | ||||
Sequence: SRGKGNTKHNIEIEYVPRKSDAGISSADAPRKFNMKMI |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
In mice lacking Lingo1 and MPTP-intoxicated, a model for Parkinson disease, the dopaminergic neurons survival is increased and behavioral abnormalities reduced.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 41 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, disulfide bond, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-35 | |||||
Sequence: MLAGGMRSMPSPLLACWQPILLLVLGSVLSGSATG | ||||||
Disulfide bond | 36↔42 | |||||
Sequence: CPPRCEC | ||||||
Chain | PRO_0000328643 | 36-614 | Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 | |||
Sequence: CPPRCECSAQDRAVLCHRKRFVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTPNCLYGLNLTSLSITHCNLTAVPYLAVRHLVYLRFLNLSYNPIGTIEGSMLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESAFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQPTCATPEFVQGKEFKDFPDVLLPNYFTCRRAHIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHVRSYSPDWPHQPNKTFAFISNQPGEGEANSTRATVPFPFDIKTLIIATTMGFISFLGVVLFCLVLLFLWSRGKGNTKHNIEIEYVPRKSDAGISSADAPRKFNMKMI | ||||||
Disulfide bond | 40↔51 | |||||
Sequence: CECSAQDRAVLC | ||||||
Glycosylation | 138 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 196 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 268 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 287 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 335 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 367↔390 | |||||
Sequence: CDCRLLWVFRRRWRLNFNRQQPTC | ||||||
Disulfide bond | 369↔415 | |||||
Sequence: CRLLWVFRRRWRLNFNRQQPTCATPEFVQGKEFKDFPDVLLPNYFTC | ||||||
Disulfide bond | 440↔491 | |||||
Sequence: CRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLC | ||||||
Glycosylation | 486 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 536 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 596 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N-glycosylated. Contains predominantly high-mannose glycans (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly specific expression in the central nervous system. Predominant expression in neocortex, amygdala, hippocampus, thalamus and entorhinal cortex, with lower levels in cerebellum and basal nuclei.
Induction
Up-regulated in brain from MPTP-intoxicated mice, a model for Parkinson disease.
Developmental stage
Expressed broadly at high levels in the whole embryo and becomes progressively restricted to the central nervous system by 14.5 dpc. Extensively expressed across the central nervous system through late embryogenesis and during postnatal development, with a peak of expression around the first week after birth.
Gene expression databases
Interaction
Subunit
Homotetramer. Forms a ternary complex with RTN4R/NGFR and RTN4R/TNFRSF19 (By similarity).
Interacts with NGRF and MYT1L (PubMed:18186492).
Interacts with RTN4R (PubMed:18186492, PubMed:22923615).
Interacts with NGRF and MYT1L (PubMed:18186492).
Interacts with RTN4R (PubMed:18186492, PubMed:22923615).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9D1T0 | App P12023 | 2 | EBI-2012981, EBI-78814 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-65 | LRRNT | ||||
Sequence: CPPRCECSAQDRAVLCHRKRFVAVPEGIPT | ||||||
Repeat | 66-87 | LRR 1 | ||||
Sequence: ETRLLDLGKNRIKTLNQDEFAS | ||||||
Repeat | 90-111 | LRR 2 | ||||
Sequence: HLEELELNENIVSAVEPGAFNN | ||||||
Repeat | 114-135 | LRR 3 | ||||
Sequence: NLRTLGLRSNRLKLIPLGVFTG | ||||||
Repeat | 138-159 | LRR 4 | ||||
Sequence: NLTKLDISENKIVILLDYMFQD | ||||||
Repeat | 162-183 | LRR 5 | ||||
Sequence: NLKSLEVGDNDLVYISHRAFSG | ||||||
Repeat | 186-207 | LRR 6 | ||||
Sequence: SLEQLTLEKCNLTSIPTEALSH | ||||||
Repeat | 210-231 | LRR 7 | ||||
Sequence: GLIVLRLRHLNINAIRDYSFKR | ||||||
Repeat | 258-279 | LRR 8 | ||||
Sequence: NLTSLSITHCNLTAVPYLAVRH | ||||||
Repeat | 282-303 | LRR 9 | ||||
Sequence: YLRFLNLSYNPIGTIEGSMLHE | ||||||
Repeat | 306-327 | LRR 10 | ||||
Sequence: RLQEIQLVGGQLAVVEPYAFRG | ||||||
Repeat | 330-351 | LRR 11 | ||||
Sequence: YLRVLNVSGNQLTTLEESAFHS | ||||||
Domain | 363-417 | LRRCT | ||||
Sequence: NPLACDCRLLWVFRRRWRLNFNRQQPTCATPEFVQGKEFKDFPDVLLPNYFTCRR | ||||||
Domain | 405-507 | Ig-like C2-type | ||||
Sequence: PDVLLPNYFTCRRAHIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLH |
Domain
The intracellular domain of LINGO1 interacts with MYT1L.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length614
- Mass (Da)69,101
- Last updated2001-06-01 v1
- Checksum41CFF40C21335681
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A9DA50 | A9DA50_MOUSE | Lingo1 | 620 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 491 | in Ref. 3; AAQ97219 | ||||
Sequence: C → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK027262 EMBL· GenBank· DDBJ | BAB32403.1 EMBL· GenBank· DDBJ | mRNA | ||
AK163538 EMBL· GenBank· DDBJ | BAE37388.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052384 EMBL· GenBank· DDBJ | AAH52384.2 EMBL· GenBank· DDBJ | mRNA | ||
BC065696 EMBL· GenBank· DDBJ | AAH65696.1 EMBL· GenBank· DDBJ | mRNA | ||
AY324324 EMBL· GenBank· DDBJ | AAQ97219.1 EMBL· GenBank· DDBJ | mRNA |