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Reticulon-4 receptor (Nogo receptor) (NgR) (Nogo-66 receptor)

 RTN4R_HUMAN             Reviewed;         473 AA.
Q9BZR6; D3DX28;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
10-OCT-2018, entry version 171.
RecName: Full=Reticulon-4 receptor;
AltName: Full=Nogo receptor;
Short=NgR;
AltName: Full=Nogo-66 receptor;
Flags: Precursor;
Name=RTN4R; Synonyms=NOGOR; ORFNames=UNQ330/PRO526;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=11201742; DOI=10.1038/35053072;
Fournier A.E., GrandPre T., Strittmatter S.M.;
"Identification of a receptor mediating Nogo-66 inhibition of axonal
regeneration.";
Nature 409:341-346(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 27-41.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[9]
FUNCTION, INTERACTION WITH NGR, AND SUBCELLULAR LOCATION.
PubMed=12426574; DOI=10.1038/nn975;
Wong S.T., Henley J.R., Kanning K.C., Huang K.H., Bothwell M.,
Poo M.M.;
"A p75(NTR) and Nogo receptor complex mediates repulsive signaling by
myelin-associated glycoprotein.";
Nat. Neurosci. 5:1302-1308(2002).
[10]
FUNCTION, AND INTERACTION WITH RTN4.
PubMed=12037567; DOI=10.1038/417547a;
GrandPre T., Li S., Strittmatter S.M.;
"Nogo-66 receptor antagonist peptide promotes axonal regeneration.";
Nature 417:547-551(2002).
[11]
INTERACTION WITH OMG, AND FUNCTION.
PubMed=12068310; DOI=10.1038/nature00867;
Wang K.C., Koprivica V., Kim J.A., Sivasankaran R., Guo Y., Neve R.L.,
He Z.;
"Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that
inhibits neurite outgrowth.";
Nature 417:941-944(2002).
[12]
INTERACTION WITH MAG, AND FUNCTION.
PubMed=12089450; DOI=10.1126/science.1073031;
Liu B.P., Fournier A., GrandPre T., Strittmatter S.M.;
"Myelin-associated glycoprotein as a functional ligand for the Nogo-66
receptor.";
Science 297:1190-1193(2002).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12694398;
Pignot V., Hein A.E., Barske C., Wiessner C., Walmsley A.R.,
Kaupmann K., Mayeur H., Sommer B., Mir A.K., Frentzel S.;
"Characterization of two novel proteins, NgRH1 and NgRH2, structurally
and biochemically homologous to the Nogo-66 receptor.";
J. Neurochem. 85:717-728(2003).
[14]
INVOLVEMENT IN SCZD, AND VARIANTS SCZD TRP-119 AND HIS-196.
PubMed=15532024; DOI=10.1002/humu.9292;
Sinibaldi L., De Luca A., Bellacchio E., Conti E., Pasini A.,
Paloscia C., Spalletta G., Caltagirone C., Pizzuti A.,
Dallapiccola B.;
"Mutations of the Nogo-66 receptor (RTN4R) gene in schizophrenia.";
Hum. Mutat. 24:534-535(2004).
[15]
FUNCTION, AND INTERACTION WITH LINGO1.
PubMed=14966521; DOI=10.1038/nn1188;
Mi S., Lee X., Shao Z., Thill G., Ji B., Relton J., Levesque M.,
Allaire N., Perrin S., Sands B., Crowell T., Cate R.L., McCoy J.M.,
Pepinsky R.B.;
"LINGO-1 is a component of the Nogo-66 receptor/p75 signaling
complex.";
Nat. Neurosci. 7:221-228(2004).
[16]
REVIEW.
PubMed=12183616; DOI=10.1126/science.1076247;
Woolf C.J., Bloechlinger S.;
"It takes more than two to Nogo.";
Science 297:1132-1134(2002).
[17]
REVIEW.
PubMed=11891768; DOI=10.1002/jnr.10134;
Ng C.E.L., Tang B.L.;
"Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron
regeneration.";
J. Neurosci. Res. 67:559-565(2002).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16712417; DOI=10.1089/adt.2006.4.133;
Teusch N., Kiefer C.;
"A high-content screening assay for the Nogo receptor based on
cellular Rho activation.";
Assay Drug Dev. Technol. 4:133-141(2006).
[19]
INTERACTION WITH GANGLIOSIDE GT1B; GANGLIOSIDE GM1; NGFR; RTN4 AND
MAG, SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF
ARG-151; ARG-199; LYS-277 AND ARG-279.
PubMed=18411262; DOI=10.1074/jbc.M802067200;
Williams G., Wood A., Williams E.J., Gao Y., Mercado M.L., Katz A.,
Joseph-McCarthy D., Bates B., Ling H.P., Aulabaugh A., Zaccardi J.,
Xie Y., Pangalos M.N., Walsh F.S., Doherty P.;
"Ganglioside inhibition of neurite outgrowth requires Nogo receptor
function: identification of interaction sites and development of novel
antagonists.";
J. Biol. Chem. 283:16641-16652(2008).
[20]
FUNCTION, INTERACTION WITH MAG; RTN4; OMG; NGFR AND LINGO1,
INVOLVEMENT IN SCZD, VARIANTS MET-53; HIS-68; SER-141; HIS-227;
MET-263; SER-314; LEU-329 AND MET-363, VARIANTS SCZD TRP-119; HIS-196;
CYS-227; GLN-377; TRP-377 AND TRP-399, AND CHARACTERIZATION OF
VARIANTS SCZD TRP-119; HIS-196; GLN-377 AND TRP-377.
PubMed=19052207; DOI=10.1523/JNEUROSCI.3828-08.2008;
Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
Strittmatter S.M.;
"Genetic variants of Nogo-66 receptor with possible association to
schizophrenia block myelin inhibition of axon growth.";
J. Neurosci. 28:13161-13172(2008).
[21]
INTERACTION WITH KIAA0319L.
PubMed=20697954; DOI=10.1007/s10571-010-9549-1;
Poon M.W., Tsang W.H., Chan S.O., Li H.M., Ng H.K., Waye M.M.;
"Dyslexia-associated kiaa0319-like protein interacts with axon
guidance receptor nogo receptor 1.";
Cell. Mol. Neurobiol. 31:27-35(2011).
[22]
FUNCTION.
PubMed=22325200; DOI=10.1016/j.neuron.2011.11.029;
Wills Z.P., Mandel-Brehm C., Mardinly A.R., McCord A.E., Giger R.J.,
Greenberg M.E.;
"The Nogo receptor family restricts synapse number in the developing
hippocampus.";
Neuron 73:466-481(2012).
[23]
FUNCTION, VARIANTS HIS-68; ASN-259 AND MET-363, INVOLVEMENT IN SCZD,
VARIANT SCZD HIS-292, AND CHARACTERIZATION OF VARIANT SCZD HIS-292.
PubMed=28892071; DOI=10.1038/tp.2017.170;
Kimura H., Fujita Y., Kawabata T., Ishizuka K., Wang C., Iwayama Y.,
Okahisa Y., Kushima I., Morikawa M., Uno Y., Okada T., Ikeda M.,
Inada T., Branko A., Mori D., Yoshikawa T., Iwata N., Nakamura H.,
Yamashita T., Ozaki N.;
"A novel rare variant R292H in RTN4R affects growth cone formation and
possibly contributes to schizophrenia susceptibility.";
Transl. Psychiatry 7:E1214-E1214(2017).
[24]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 27-311, FUNCTION, INTERACTION
WITH MAG; OMG AND RTN4, SUBCELLULAR LOCATION, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-82 AND ASN-179.
PubMed=12839991; DOI=10.1093/emboj/cdg325;
Barton W.A., Liu B.P., Tzvetkova D., Jeffrey P.D., Fournier A.E.,
Sah D., Cate R., Strittmatter S.M., Nikolov D.B.;
"Structure and axon outgrowth inhibitor binding of the Nogo-66
receptor and related proteins.";
EMBO J. 22:3291-3302(2003).
[25]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 26-310, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-82 AND ASN-179.
PubMed=12718853; DOI=10.1016/S0896-6273(03)00232-0;
He X.L., Bazan J.F., McDermott G., Park J.B., Wang K.,
Tessier-Lavigne M., He Z., Garcia K.C.;
"Structure of the Nogo receptor ectodomain: a recognition module
implicated in myelin inhibition.";
Neuron 38:177-185(2003).
-!- FUNCTION: Receptor for RTN4, OMG and MAG (PubMed:12037567,
PubMed:12068310, PubMed:12426574, PubMed:12089450,
PubMed:16712417, PubMed:18411262, PubMed:12839991,
PubMed:19052207). Functions as receptor for the sialylated
gangliosides GT1b and GM1 (PubMed:18411262). Besides, functions as
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}.
-!- SUBUNIT: Homodimer (PubMed:18411262). Interacts with MAG
(PubMed:12089450, PubMed:12839991, PubMed:18411262,
PubMed:19052207). Interacts with RTN4 (PubMed:12839991,
PubMed:19052207). Interacts with NGFR (PubMed:12426574,
PubMed:18411262, PubMed:19052207). Interacts with LINGO1
(PubMed:14966521, PubMed:19052207). Interacts with KIAA0319L
(PubMed:20697954). Interacts with OLFM1; this inhibits interaction
with LINGO1 and NGFR (By similarity). Interacts with OMG
(PubMed:12068310, PubMed:12839991, PubMed:19052207).
{ECO:0000250|UniProtKB:Q99PI8, ECO:0000269|PubMed:12068310,
ECO:0000269|PubMed:12089450, ECO:0000269|PubMed:12426574,
ECO:0000269|PubMed:12839991, ECO:0000269|PubMed:14966521,
ECO:0000269|PubMed:18411262, ECO:0000269|PubMed:19052207,
ECO:0000269|PubMed:20697954}.
-!- INTERACTION:
Q8IZA0:KIAA0319L; NbExp=4; IntAct=EBI-5240240, EBI-5240269;
-!- 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}.
-!- TISSUE SPECIFICITY: Widespread in the brain but highest levels in
the gray matter. Low levels in heart and kidney; not expressed in
oligodendrocytes (white matter). {ECO:0000269|PubMed:12694398}.
-!- PTM: N-glycosylated. O-glycosylated. Contains terminal sialic acid
groups on its glycan chains. {ECO:0000250|UniProtKB:Q99M75}.
-!- 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 variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the Nogo receptor family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Nerve regrowth: nipped
by a no-go - Issue 69 of April 2006;
URL="https://web.expasy.org/spotlight/back_issues/069";
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EMBL; AF283463; AAG53612.1; -; mRNA.
EMBL; AL834449; CAD39109.1; -; mRNA.
EMBL; AY358297; AAQ88664.1; -; mRNA.
EMBL; CR456360; CAG30246.1; -; mRNA.
EMBL; AC058790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471176; EAX02975.1; -; Genomic_DNA.
EMBL; CH471176; EAX02976.1; -; Genomic_DNA.
EMBL; BC011787; AAH11787.1; -; mRNA.
CCDS; CCDS13777.1; -.
RefSeq; NP_075380.1; NM_023004.5.
UniGene; Hs.30868; -.
PDB; 1OZN; X-ray; 1.52 A; A=26-310.
PDB; 1P8T; X-ray; 3.20 A; A=27-311.
PDBsum; 1OZN; -.
PDBsum; 1P8T; -.
ProteinModelPortal; Q9BZR6; -.
SMR; Q9BZR6; -.
BioGrid; 122388; 7.
CORUM; Q9BZR6; -.
IntAct; Q9BZR6; 3.
STRING; 9606.ENSP00000043402; -.
iPTMnet; Q9BZR6; -.
BioMuta; RTN4R; -.
EPD; Q9BZR6; -.
PaxDb; Q9BZR6; -.
PeptideAtlas; Q9BZR6; -.
PRIDE; Q9BZR6; -.
ProteomicsDB; 79894; -.
DNASU; 65078; -.
Ensembl; ENST00000043402; ENSP00000043402; ENSG00000040608.
GeneID; 65078; -.
KEGG; hsa:65078; -.
UCSC; uc002zrv.4; human.
CTD; 65078; -.
DisGeNET; 65078; -.
EuPathDB; HostDB:ENSG00000040608.13; -.
GeneCards; RTN4R; -.
HGNC; HGNC:18601; RTN4R.
HPA; CAB012443; -.
MalaCards; RTN4R; -.
MIM; 181500; phenotype.
MIM; 605566; gene.
neXtProt; NX_Q9BZR6; -.
OpenTargets; ENSG00000040608; -.
PharmGKB; PA38600; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00920000148971; -.
HOGENOM; HOG000116109; -.
HOVERGEN; HBG063707; -.
InParanoid; Q9BZR6; -.
KO; K16659; -.
PhylomeDB; Q9BZR6; -.
TreeFam; TF330080; -.
Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
ChiTaRS; RTN4R; human.
EvolutionaryTrace; Q9BZR6; -.
GeneWiki; Reticulon_4_receptor; -.
GenomeRNAi; 65078; -.
PRO; PR:Q9BZR6; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000040608; Expressed in 109 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_RTN4R; -.
ExpressionAtlas; Q9BZR6; baseline and differential.
Genevisible; Q9BZR6; HS.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IMP:UniProtKB.
GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098793; C:presynapse; IEA:Ensembl.
GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
GO; GO:1905573; F:ganglioside GM1 binding; IDA:UniProtKB.
GO; GO:1905576; F:ganglioside GT1b binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0038131; F:neuregulin receptor activity; ISS:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
GO; GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:UniProtKB.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF13855; LRR_8; 2.
SMART; SM00369; LRR_TYP; 8.
SMART; SM00082; LRRCT; 1.
PROSITE; PS51450; LRR; 6.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; GPI-anchor; Leucine-rich repeat; Lipid-binding;
Lipoprotein; Membrane; Polymorphism; Receptor; Reference proteome;
Repeat; Schizophrenia; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:15340161}.
CHAIN 27 447 Reticulon-4 receptor.
/FTId=PRO_0000022253.
PROPEP 448 473 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000022254.
DOMAIN 27 54 LRRNT.
REPEAT 55 79 LRR 1. {ECO:0000255}.
REPEAT 81 103 LRR 2. {ECO:0000255}.
REPEAT 104 128 LRR 3. {ECO:0000255}.
REPEAT 129 152 LRR 4. {ECO:0000255}.
REPEAT 153 176 LRR 5. {ECO:0000255}.
REPEAT 178 200 LRR 6. {ECO:0000255}.
REPEAT 202 224 LRR 7. {ECO:0000255}.
REPEAT 225 248 LRR 8. {ECO:0000255}.
REPEAT 250 273 LRR 9. {ECO:0000255}.
DOMAIN 260 310 LRRCT. {ECO:0000255}.
COMPBIAS 435 442 Poly-Gly.
LIPID 447 447 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1OZN,
ECO:0000269|PubMed:12718853,
ECO:0000269|PubMed:12839991}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12718853,
ECO:0000269|PubMed:12839991}.
DISULFID 27 33 {ECO:0000244|PDB:1OZN,
ECO:0000244|PDB:1P8T,
ECO:0000269|PubMed:12718853,
ECO:0000269|PubMed:12839991}.
DISULFID 31 43 {ECO:0000244|PDB:1OZN,
ECO:0000244|PDB:1P8T,
ECO:0000269|PubMed:12718853,
ECO:0000269|PubMed:12839991}.
DISULFID 264 287 {ECO:0000244|PDB:1OZN,
ECO:0000244|PDB:1P8T,
ECO:0000269|PubMed:12718853,
ECO:0000269|PubMed:12839991}.
DISULFID 266 335 {ECO:0000250|UniProtKB:Q99PI8}.
DISULFID 309 336 {ECO:0000250|UniProtKB:Q99PI8}.
VARIANT 53 53 V -> M (in dbSNP:rs145292678).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079224.
VARIANT 68 68 R -> H (in dbSNP:rs145773589).
{ECO:0000269|PubMed:19052207,
ECO:0000269|PubMed:28892071}.
/FTId=VAR_079225.
VARIANT 119 119 R -> W (in SCZD; associated with disease
susceptibility; unable to mediate down-
regulation of axonal growth; decreased
interaction with MAG and OMG; no effect
on interaction with RTN4;
dbSNP:rs74315508).
{ECO:0000269|PubMed:15532024,
ECO:0000269|PubMed:19052207}.
/FTId=VAR_079154.
VARIANT 141 141 G -> S (in dbSNP:rs760855779).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079226.
VARIANT 196 196 R -> H (in SCZD; associated with disease
susceptibility; unable to mediate down-
regulation of axonal growth; does not
affect interaction with MAG, RTN4 and
OMG; dbSNP:rs74315509).
{ECO:0000269|PubMed:15532024,
ECO:0000269|PubMed:19052207}.
/FTId=VAR_079155.
VARIANT 227 227 R -> C (in SCZD; unknown pathological
significance; dbSNP:rs754793885).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079227.
VARIANT 227 227 R -> H (in dbSNP:rs576939822).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079228.
VARIANT 259 259 D -> N (in dbSNP:rs3747073).
{ECO:0000269|PubMed:28892071}.
/FTId=VAR_079229.
VARIANT 263 263 V -> M (in dbSNP:rs752810777).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079230.
VARIANT 292 292 R -> H (in SCZD; associated with disease
susceptibility; unable to mediate down-
regulation of axonal growth).
{ECO:0000269|PubMed:28892071}.
/FTId=VAR_079231.
VARIANT 314 314 G -> S (in dbSNP:rs112151786).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079232.
VARIANT 329 329 P -> L (in dbSNP:rs757507039).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079233.
VARIANT 363 363 V -> M (in dbSNP:rs149231717).
{ECO:0000269|PubMed:19052207,
ECO:0000269|PubMed:28892071}.
/FTId=VAR_079234.
VARIANT 377 377 R -> Q (in SCZD; associated with disease
susceptibility; unable to mediate down-
regulation of axonal growth; does not
affect interaction with MAG, RTN4, OMG,
NGFR and LINGO1; dbSNP:rs779384862).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079235.
VARIANT 377 377 R -> W (in SCZD; associated with disease
susceptibility; unable to mediate down-
regulation of axonal growth; does not
affect interaction with MAG, RTN4, OMG,
NGFR and LINGO1; dbSNP:rs748655075).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079236.
VARIANT 399 399 R -> W (in SCZD; unknown pathological
significance; dbSNP:rs200119628).
{ECO:0000269|PubMed:19052207}.
/FTId=VAR_079237.
MUTAGEN 151 151 R->E: Impaired ganglioside binding.
{ECO:0000269|PubMed:18411262}.
MUTAGEN 199 199 R->E: Impaired ganglioside binding.
{ECO:0000269|PubMed:18411262}.
MUTAGEN 277 277 K->A: No effect on interaction with MAG.
{ECO:0000269|PubMed:18411262}.
MUTAGEN 277 277 K->D: Decreases interaction with MAG;
when associated with D-279.
{ECO:0000269|PubMed:18411262}.
MUTAGEN 279 279 R->A: Mildly decreases interaction with
MAG. {ECO:0000269|PubMed:18411262}.
MUTAGEN 279 279 R->D: Decreases interaction with MAG;
when associated with D-277.
{ECO:0000269|PubMed:18411262}.
MUTAGEN 279 279 R->E: Impaired ganglioside binding.
{ECO:0000269|PubMed:18411262}.
STRAND 32 34 {ECO:0000244|PDB:1OZN}.
STRAND 36 38 {ECO:0000244|PDB:1OZN}.
STRAND 40 42 {ECO:0000244|PDB:1OZN}.
STRAND 60 63 {ECO:0000244|PDB:1OZN}.
TURN 74 79 {ECO:0000244|PDB:1OZN}.
STRAND 85 87 {ECO:0000244|PDB:1OZN}.
TURN 98 103 {ECO:0000244|PDB:1OZN}.
STRAND 109 111 {ECO:0000244|PDB:1OZN}.
TURN 123 128 {ECO:0000244|PDB:1OZN}.
STRAND 134 136 {ECO:0000244|PDB:1OZN}.
TURN 147 152 {ECO:0000244|PDB:1OZN}.
STRAND 158 160 {ECO:0000244|PDB:1OZN}.
TURN 171 176 {ECO:0000244|PDB:1OZN}.
STRAND 182 184 {ECO:0000244|PDB:1OZN}.
TURN 195 200 {ECO:0000244|PDB:1OZN}.
STRAND 206 208 {ECO:0000244|PDB:1OZN}.
TURN 219 224 {ECO:0000244|PDB:1OZN}.
STRAND 230 232 {ECO:0000244|PDB:1OZN}.
HELIX 243 246 {ECO:0000244|PDB:1OZN}.
STRAND 254 256 {ECO:0000244|PDB:1OZN}.
HELIX 266 268 {ECO:0000244|PDB:1OZN}.
HELIX 269 277 {ECO:0000244|PDB:1OZN}.
STRAND 280 282 {ECO:0000244|PDB:1OZN}.
STRAND 286 290 {ECO:0000244|PDB:1OZN}.
HELIX 291 293 {ECO:0000244|PDB:1OZN}.
HELIX 298 300 {ECO:0000244|PDB:1OZN}.
HELIX 303 305 {ECO:0000244|PDB:1OZN}.
SEQUENCE 473 AA; 50708 MW; CA5624B24C584702 CRC64;
MKRASAGGSR LLAWVLWLQA WQVAAPCPGA CVCYNEPKVT TSCPQQGLQA VPVGIPAASQ
RIFLHGNRIS HVPAASFRAC RNLTILWLHS NVLARIDAAA FTGLALLEQL DLSDNAQLRS
VDPATFHGLG RLHTLHLDRC GLQELGPGLF RGLAALQYLY LQDNALQALP DDTFRDLGNL
THLFLHGNRI SSVPERAFRG LHSLDRLLLH QNRVAHVHPH AFRDLGRLMT LYLFANNLSA
LPTEALAPLR ALQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCSLP QRLAGRDLKR
LAANDLQGCA VATGPYHPIW TGRATDEEPL GLPKCCQPDA ADKASVLEPG RPASAGNALK
GRVPPGDSPP GNGSGPRHIN DSPFGTLPGS AEPPLTAVRP EGSEPPGFPT SGPRRRPGCS
RKNRTRSHCR LGQAGSGGGG TGDSEGSGAL PSLTCSLTPL GLALVLWTVL GPC


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