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

 RTN4R_RAT               Reviewed;         473 AA.
Q99M75;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
22-NOV-2017, entry version 134.
RecName: Full=Reticulon-4 receptor;
AltName: Full=Nogo receptor;
Short=NgR;
AltName: Full=Nogo-66 receptor;
Flags: Precursor;
Name=Rtn4r; Synonyms=Nogor;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Jin W.-L., Jia W., Long M., Ju G.;
"Identification and preparation of polyclonal antibody against rat
Nogo receptor.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Oertle T., van der Haar M.E., Bandtlow C.E., Huber A.B., Simonen M.,
Schnell L., Broesamle C., Schwab M.E.;
"Nogo-A: a molecule with two active sites and two membrane
topologies.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
INTERACTION WITH NGFR, TISSUE SPECIFICITY, 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).
[5]
FUNCTION.
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).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAG; RTN4 AND OMG,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15673660; DOI=10.1523/JNEUROSCI.4464-04.2005;
Venkatesh K., Chivatakarn O., Lee H., Joshi P.S., Kantor D.B.,
Newman B.A., Mage R., Rader C., Giger R.J.;
"The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent receptor
selective for myelin-associated glycoprotein.";
J. Neurosci. 25:808-822(2005).
[7]
FUNCTION.
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).
[8]
INTERACTION WITH MAG; RTN4 AND OMG, GLYCOSYLATION, AND SUBCELLULAR
LOCATION.
PubMed=19420245; DOI=10.1523/JNEUROSCI.4935-08.2009;
Robak L.A., Venkatesh K., Lee H., Raiker S.J., Duan Y.,
Lee-Osbourne J., Hofer T., Mage R.G., Rader C., Giger R.J.;
"Molecular basis of the interactions of the Nogo-66 receptor and its
homolog NgR2 with myelin-associated glycoprotein: development of
NgROMNI-Fc, a novel antagonist of CNS myelin inhibition.";
J. Neurosci. 29:5768-5783(2009).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[10]
FUNCTION.
PubMed=26335717; DOI=10.1038/cddis.2015.228;
Palandri A., Salvador V.R., Wojnacki J., Vivinetto A.L., Schnaar R.L.,
Lopez P.H.;
"Myelin-associated glycoprotein modulates apoptosis of motoneurons
during early postnatal development via NgR/p75(NTR) receptor-mediated
activation of RhoA signaling pathways.";
Cell Death Dis. 6:E1876-E1876(2015).
[11]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-312, AND DISULFIDE BONDS.
PubMed=20815818; DOI=10.1042/BA20100061;
Weinreb P.H., Wen D., Qian F., Wildes C.P., Garber E.A., Walus L.,
Jung M.Y., Wang J., Relton J.K., Amatucci J., Wang R., Porreca F.,
Silvian L., Meier W., Pepinsky R.B., Lee D.H.;
"Resolution of disulfide heterogeneity in Nogo receptor I fusion
proteins by molecular engineering.";
Biotechnol. Appl. Biochem. 57:31-45(2010).
-!- FUNCTION: Receptor for RTN4, OMG and MAG (PubMed:12037567,
PubMed:15673660, PubMed:19420245). Functions as receptor for the
sialylated gangliosides GT1b and GM1. Besides, functions as
receptor for chondroitin sulfate proteoglycans. Can also bind
heparin. Intracellular signaling cascades are triggered via the
coreceptor NGFR (By similarity). Signaling mediates activation of
Rho and downstream reorganization of the actin cytoskeleton
(PubMed:18411262). Mediates axonal growth inhibition
(PubMed:12037567). May play 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 (By similarity). Protects motoneurons against
apoptosis; protection against apoptosis is probably mediated via
interaction with MAG (PubMed:26335717). 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:0000250|UniProtKB:Q9BZR6, ECO:0000269|PubMed:12037567,
ECO:0000269|PubMed:15673660, ECO:0000269|PubMed:18411262,
ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:26335717}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with MAG
(PubMed:15673660, PubMed:19420245). Interacts with RTN4 and OMG
(PubMed:15673660, PubMed:19420245). Interacts with LINGO1 and NGFR
(By similarity). Interacts with KIAA0319L (By similarity).
Interacts with OLFM1; this inhibits interaction with LINGO1 and
NGFR (By similarity). {ECO:0000250|UniProtKB:Q99PI8,
ECO:0000250|UniProtKB:Q9BZR6, ECO:0000269|PubMed:15673660,
ECO:0000269|PubMed:19420245}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15673660,
ECO:0000269|PubMed:19420245, ECO:0000269|PubMed:22325200}; Lipid-
anchor, GPI-anchor {ECO:0000250|UniProtKB:Q99PI8}. Membrane raft
{ECO:0000269|PubMed:15673660}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q99PI8}. Perikaryon
{ECO:0000269|PubMed:15673660}. Cell projection, axon
{ECO:0000269|PubMed:12426574}. Note=Detected along dendrites and
axons, close to synapses, but clearly excluded from synapses.
{ECO:0000250|UniProtKB:Q99PI8}.
-!- TISSUE SPECIFICITY: Detected in embryonic cerebellum, in spinal
cord motor neurons and in dorsal root ganglia (PubMed:12426574).
Detected in adult brain, in neocortex, hippocampus, striatum,
thalamus and dorsal root ganglion neurons (at protein level).
{ECO:0000269|PubMed:15673660}.
-!- DEVELOPMENTAL STAGE: Expression is high in adult, but very low in
neonate dorsal root ganglion neurons (at protein level).
{ECO:0000269|PubMed:15673660}.
-!- PTM: N-glycosylated. O-glycosylated. Contains terminal sialic acid
groups on its glycan chains. {ECO:0000269|PubMed:19420245}.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AY028438; AAK20166.1; -; mRNA.
EMBL; AF462390; AAM46772.1; -; mRNA.
RefSeq; NP_446065.1; NM_053613.1.
UniGene; Rn.229952; -.
PDB; 3KJ4; X-ray; 3.10 A; A/D=27-312.
PDBsum; 3KJ4; -.
ProteinModelPortal; Q99M75; -.
SMR; Q99M75; -.
MINT; MINT-243866; -.
STRING; 10116.ENSRNOP00000041517; -.
iPTMnet; Q99M75; -.
PaxDb; Q99M75; -.
Ensembl; ENSRNOT00000051037; ENSRNOP00000041517; ENSRNOG00000030920.
GeneID; 113912; -.
KEGG; rno:113912; -.
CTD; 65078; -.
RGD; 620810; Rtn4r.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00900000140818; -.
HOGENOM; HOG000116109; -.
HOVERGEN; HBG063707; -.
InParanoid; Q99M75; -.
KO; K16659; -.
OMA; NDSPFGT; -.
OrthoDB; EOG091G08II; -.
PhylomeDB; Q99M75; -.
TreeFam; TF330080; -.
Reactome; R-RNO-193634; Axonal growth inhibition (RHOA activation).
EvolutionaryTrace; Q99M75; -.
PRO; PR:Q99M75; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000030920; -.
Genevisible; Q99M75; RN.
GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS: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; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0030426; C:growth cone; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA: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; ISO:RGD.
GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
GO; GO:1905573; F:ganglioside GM1 binding; ISS:UniProtKB.
GO; GO:1905576; F:ganglioside GT1b binding; ISS: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:0004872; F:receptor activity; IMP:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISO:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IMP: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:RGD.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP: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; ISS: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.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 8.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Complete proteome;
Disulfide bond; Glycoprotein; GPI-anchor; Leucine-rich repeat;
Lipoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 447 Reticulon-4 receptor.
/FTId=PRO_0000022259.
PROPEP 448 473 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000022260.
DOMAIN 27 57 LRRNT. {ECO:0000255}.
REPEAT 56 79 LRR 1. {ECO:0000255}.
REPEAT 80 103 LRR 2. {ECO:0000255}.
REPEAT 105 128 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}.
LIPID 447 447 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 33 {ECO:0000244|PDB:3KJ4,
ECO:0000269|PubMed:20815818}.
DISULFID 31 43 {ECO:0000244|PDB:3KJ4,
ECO:0000269|PubMed:20815818}.
DISULFID 264 287 {ECO:0000244|PDB:3KJ4,
ECO:0000269|PubMed:20815818}.
DISULFID 266 309 {ECO:0000250|UniProtKB:Q9BZR6}.
CONFLICT 12 13 LA -> PT (in Ref. 1; AAK20166).
{ECO:0000305}.
CONFLICT 43 43 C -> R (in Ref. 1; AAK20166).
{ECO:0000305}.
CONFLICT 53 53 T -> A (in Ref. 1; AAK20166).
{ECO:0000305}.
CONFLICT 284 284 E -> G (in Ref. 1; AAK20166).
{ECO:0000305}.
CONFLICT 287 287 C -> S (in Ref. 1; AAK20166).
{ECO:0000305}.
CONFLICT 303 303 A -> T (in Ref. 1; AAK20166).
{ECO:0000305}.
CONFLICT 355 355 A -> V (in Ref. 1; AAK20166).
{ECO:0000305}.
STRAND 32 34 {ECO:0000244|PDB:3KJ4}.
STRAND 36 38 {ECO:0000244|PDB:3KJ4}.
STRAND 40 42 {ECO:0000244|PDB:3KJ4}.
STRAND 60 63 {ECO:0000244|PDB:3KJ4}.
STRAND 85 87 {ECO:0000244|PDB:3KJ4}.
STRAND 94 96 {ECO:0000244|PDB:3KJ4}.
TURN 98 103 {ECO:0000244|PDB:3KJ4}.
STRAND 109 111 {ECO:0000244|PDB:3KJ4}.
TURN 123 128 {ECO:0000244|PDB:3KJ4}.
STRAND 134 136 {ECO:0000244|PDB:3KJ4}.
TURN 147 152 {ECO:0000244|PDB:3KJ4}.
STRAND 158 160 {ECO:0000244|PDB:3KJ4}.
TURN 171 176 {ECO:0000244|PDB:3KJ4}.
STRAND 182 184 {ECO:0000244|PDB:3KJ4}.
TURN 195 200 {ECO:0000244|PDB:3KJ4}.
STRAND 206 208 {ECO:0000244|PDB:3KJ4}.
TURN 219 224 {ECO:0000244|PDB:3KJ4}.
STRAND 230 232 {ECO:0000244|PDB:3KJ4}.
STRAND 254 256 {ECO:0000244|PDB:3KJ4}.
HELIX 268 277 {ECO:0000244|PDB:3KJ4}.
HELIX 291 293 {ECO:0000244|PDB:3KJ4}.
HELIX 298 300 {ECO:0000244|PDB:3KJ4}.
SEQUENCE 473 AA; 50851 MW; 3DFD17EA4651FECB CRC64;
MKRASSGGSR LLAWVLWLQA WRVATPCPGA CVCYNEPKVT TSCPQQGLQA VPTGIPASSQ
RIFLHGNRIS YVPAASFQSC RNLTILWLHS NALAGIDAAA FTGLTLLEQL DLSDNAQLRV
VDPTTFRGLG HLHTLHLDRC GLQELGPGLF RGLAALQYLY LQDNNLQALP DNTFRDLGNL
THLFLHGNRI PSVPEHAFRG LHSLDRLLLH QNHVARVHPH AFRDLGRLMT LYLFANNLSM
LPAEVLVPLR SLQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCNLP QRLAGRDLKR
LAASDLEGCA VASGPFRPFQ TNQLTDEELL GLPKCCQPDA ADKASVLEPG RPASAGNALK
GRVPPGDTPP GNGSGPRHIN DSPFGTLPGS AEPPLTALRP GGSEPPGLPT TGPRRRPGCS
RKNRTRSHCR LGQAGSGSSG TGDAEGSGAL PALACSLAPL GLALVLWTVL GPC


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