RTN4R
entrez
65078
canonical
uniprot
Q9BZR6
canonical
ensembl
ENSG00000040608
resolver
ensp
ENSP00000043402
resolver
enst
ENST00000043402
resolver
genesymbol
RTN4R
resolver
genesymbol_syn
NOGOR
resolver
hgnc
HGNC:18601
resolver
uniprot
D3DX28
resolver
uniprot_entry
RTN4R_HUMAN
resolver
uniprot_sec
D3DX28
resolver
amino_acid_sequence
MKRASAGGSRLLAWVLWLQAWQVAAPCPGACVCYNEPKVTTSCPQQGLQAVPVGIPAASQRIFLHGNRISHVPAASFRACRNLTILWLHSNVLARIDAAAFTGLALLEQLDLSDNAQLRSVDPATFHGLGRLHTLHLDRCGLQELGPGLFRGLAALQYLYLQDNALQALPDDTFRDLGNLTHLFLHGNRISSVPERAFRGLHSLDRLLLHQNRVAHVHPHAFRDLGRLMTLYLFANNLSALPTEALAPLRALQYLRLNDNPWVCDCRARPLWAWLQKFRGSSSEVPCSLPQRLAGRDLKRLAANDLQGCAVATGPYHPIWTGRATDEEPLGLPKCCQPDAADKASVLEPGRPASAGNALKGRVPPGDSPPGNGSGPRHINDSPFGTLPGSAEPPLTAVRPEGSEPPGFPTSGPRRRPGCSRKNRTRSHCRLGQAGSGGGGTGDSEGSGALPSLTCSLTPLGLALVLWTVLGPC
uniprot
proteins
disease_involvement
DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:15532024, ECO:0000269|PubMed:19052207, ECO:0000269|PubMed:28892071}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Receptor for RTN4, OMG and MAG (PubMed:12037567, PubMed:12068310, PubMed:12089450, PubMed:12426574, PubMed:12839991, PubMed:16712417, PubMed:18411262, PubMed:19052207). Functions as a receptor for the sialylated gangliosides GT1b and GM1 (PubMed:18411262). Besides, functions as a receptor for chondroitin sulfate proteoglycans (By similarity). Can also bind heparin (By similarity). Intracellular signaling cascades are triggered via the coreceptor NGFR (PubMed:12426574). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:16712417, PubMed:22325200). Mediates axonal growth inhibition (PubMed:12839991, PubMed:19052207, PubMed:28892071). Plays a role in regulating axon regeneration and neuronal plasticity in the adult central nervous system. Plays a role in postnatal brain development. Required for normal axon migration across the brain midline and normal formation of the corpus callosum. Protects motoneurons against apoptosis; protection against apoptosis is probably mediated via interaction with MAG. Acts in conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell motility during cortical development. Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). {ECO:0000250|UniProtKB:Q99PI8, ECO:0000269|PubMed:12037567, ECO:0000269|PubMed:12426574, ECO:0000269|PubMed:12839991, ECO:0000269|PubMed:14966521, ECO:0000269|PubMed:16712417, ECO:0000269|PubMed:18411262, ECO:0000269|PubMed:19052207, ECO:0000269|PubMed:28892071}.; FUNCTION: (Microbial infection) Acts as a receptor for Reovirus type 3. {ECO:0000269|PubMed:37276413}.
uniprot
proteins
mass_dalton
50708
uniprot
proteins
mutagenesis
MUTAGEN 151; /note="R->E: Impaired ganglioside binding."; /evidence="ECO:0000269|PubMed:18411262"; MUTAGEN 160; /note="Y->R: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 162; /note="Q->R: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 184; /note="F->R: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 189; /note="R->E: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 199; /note="R->E: Impaired ganglioside binding."; /evidence="ECO:0000269|PubMed:18411262"; MUTAGEN 206; /note="R->E: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 208; /note="L->R: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 235; /note="A->R: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 256; /note="R->E: Complete loss of binding to Reovirus type 3 outer capsid protein sigma-3. Complete loss of infectivity."; /evidence="ECO:0000269|PubMed:37276413"; MUTAGEN 277; /note="K->A: No effect on interaction with MAG."; /evidence="ECO:0000269|PubMed:18411262"; MUTAGEN 277; /note="K->D: Decreases interaction with MAG; when associated with D-279."; /evidence="ECO:0000269|PubMed:18411262"; MUTAGEN 279; /note="R->A: Mildly decreases interaction with MAG."; /evidence="ECO:0000269|PubMed:18411262"; MUTAGEN 279; /note="R->D: Decreases interaction with MAG; when associated with D-277."; /evidence="ECO:0000269|PubMed:18411262"; MUTAGEN 279; /note="R->E: Impaired ganglioside binding."; /evidence="ECO:0000269|PubMed:18411262
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. O-glycosylated. Contains terminal sialic acid groups on its glycan chains. {ECO:0000250|UniProtKB:Q99M75}.
uniprot
proteins
protein_family
Nogo receptor family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
11201742
uniprot
proteins
pubmed
11891768
uniprot
proteins
pubmed
12037567
uniprot
proteins
pubmed
12068310
uniprot
proteins
pubmed
12089450
uniprot
proteins
pubmed
12183616
uniprot
proteins
pubmed
12426574
uniprot
proteins
pubmed
12694398
uniprot
proteins
pubmed
12718853
uniprot
proteins
pubmed
12839991
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14966521
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15532024
uniprot
proteins
pubmed
16712417
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18411262
uniprot
proteins
pubmed
19052207
uniprot
proteins
pubmed
20697954
uniprot
proteins
pubmed
22325200
uniprot
proteins
pubmed
28892071
uniprot
proteins
pubmed
37276413
uniprot
proteins
sequence_length
473
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12426574, ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:12839991, ECO:0000269|PubMed:16712417, ECO:0000269|PubMed:18411262}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12694398}. Membrane raft {ECO:0000269|PubMed:12694398}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99PI8}. Cell projection, axon {ECO:0000250|UniProtKB:Q99PI8}. Perikaryon {ECO:0000250|UniProtKB:Q99M75}. Note=Detected along dendrites and axons, close to synapses, but clearly excluded from synapses. {ECO:0000250|UniProtKB:Q99PI8}.
uniprot
proteins