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

 RTN4R_MACFA             Reviewed;         473 AA.
Q9N0E3;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 98.
RecName: Full=Reticulon-4 receptor;
AltName: Full=Nogo receptor;
Short=NgR;
AltName: Full=Nogo-66 receptor;
Flags: Precursor;
Name=RTN4R; Synonyms=NOGOR; ORFNames=QccE-10286;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
PubMed=11574149; DOI=10.1016/S0378-1119(01)00665-5;
Osada N., Hida M., Kususda J., Tanuma R., Iseki K., Hirata M.,
Suto Y., Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
"Assignment of 118 novel cDNAs of cynomolgus monkey brain to human
chromosomes.";
Gene 275:31-37(2001).
[2]
ERRATUM.
Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K., Kususda J.;
Gene 278:267-267(2001).
[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).
-!- FUNCTION: Receptor for RTN4, OMG and MAG. Functions as receptor
for the sialylated gangliosides GT1b and GM1 (By similarity).
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. Signaling mediates activation of Rho and
downstream reorganization of the actin cytoskeleton. Mediates
axonal growth inhibition (By similarity). 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. 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 (By
similarity). Interacts with OMG (By similarity).
{ECO:0000250|UniProtKB:Q99PI8, ECO:0000250|UniProtKB:Q9BZR6}.
-!- SUBUNIT: Homodimer. Interacts with MAG (By similarity). Interacts
with RTN4 (By similarity). Interacts with NGFR. Interacts with
LINGO1. 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}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q9BZR6}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:Q9BZR6}. Membrane raft
{ECO:0000250|UniProtKB:Q9BZR6}. 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}.
-!- PTM: N-glycosylated. O-glycosylated. Contains terminal sialic acid
groups on its glycan chains. {ECO:0000250|UniProtKB:Q99M75}.
-!- 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; AB045987; BAB01569.1; -; mRNA.
RefSeq; NP_001306507.1; NM_001319578.1.
UniGene; Mfa.6428; -.
ProteinModelPortal; Q9N0E3; -.
SMR; Q9N0E3; -.
PRIDE; Q9N0E3; -.
GeneID; 102139327; -.
KEGG; mcf:102139327; -.
CTD; 65078; -.
HOVERGEN; HBG063707; -.
KO; K16659; -.
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; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
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: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:0038023; F:signaling receptor activity; ISS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
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.
PROSITE; PS51450; LRR; 7.
2: Evidence at transcript level;
Cell membrane; Cell projection; Disulfide bond; Glycoprotein;
GPI-anchor; Leucine-rich repeat; Lipoprotein; Membrane; Receptor;
Repeat; Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 447 Reticulon-4 receptor.
/FTId=PRO_0000022255.
PROPEP 448 473 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000022256.
DOMAIN 27 55 LRRNT.
REPEAT 56 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:0000255}.
DISULFID 27 33 {ECO:0000250|UniProtKB:Q99PI8}.
DISULFID 31 43 {ECO:0000250|UniProtKB:Q99PI8}.
DISULFID 264 287 {ECO:0000250|UniProtKB:Q99PI8}.
DISULFID 266 335 {ECO:0000250|UniProtKB:Q99PI8}.
DISULFID 309 336 {ECO:0000250|UniProtKB:Q99PI8}.
SEQUENCE 473 AA; 50645 MW; 53290DE83DB12CB3 CRC64;
MKRASAGGSR LLAWVLWLQA WRVAAPCPGA CVCYNEPKVT TSCPQQGLQA VPAGIPASSQ
RIFLHGNRIS HVPAASFRAC RNLTILWLHS NVLARIDAAA FAGLALLEQL DLSDNAQLRS
VDPATFHGLG RLHTLHLDRC GLQELGPGLF RGLAALQYLY LQDNALQALP DDTFRDLGNL
THLFLHGNRI SSVPERAFRG LHSLDRLLLH QNRVAHVHPH AFRDLGRLMT LYLFRNNLSA
LPAEALAPLR ALQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCSLP QRLAGRDLKR
LAANDLQGCA VATGPCHPIW TGRATDEELL GLPKCCQPDA ADKASVLEPG RPASAGNALK
GRVPPGDSPP GNGSGPRHIN DSPFGTLPGS AEPPLTAVRP EGSEPPGFPT SGPRRRPGCS
RKNRTRSHCR LGQAGSGGGG TGDSEGSGAL PSLACSLAPL GLALVLWTVL GPC


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