RTN4R_MACFA
ID RTN4R_MACFA Reviewed; 473 AA.
AC Q9N0E3;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Reticulon-4 receptor;
DE AltName: Full=Nogo receptor;
DE Short=NgR;
DE AltName: Full=Nogo-66 receptor;
DE Flags: Precursor;
GN Name=RTN4R; Synonyms=NOGOR; ORFNames=QccE-10286;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=11574149; DOI=10.1016/s0378-1119(01)00665-5;
RA Osada N., Hida M., Kususda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
RT "Assignment of 118 novel cDNAs of cynomolgus monkey brain to human
RT chromosomes.";
RL Gene 275:31-37(2001).
RN [2]
RP ERRATUM OF PUBMED:11574149.
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K., Kususda J.;
RL Gene 278:267-267(2001).
RN [3]
RP REVIEW.
RX PubMed=11891768; DOI=10.1002/jnr.10134;
RA Ng C.E.L., Tang B.L.;
RT "Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron
RT regeneration.";
RL J. Neurosci. Res. 67:559-565(2002).
CC -!- FUNCTION: Receptor for RTN4, OMG and MAG. Functions as receptor for the
CC sialylated gangliosides GT1b and GM1 (By similarity). Besides,
CC functions as receptor for chondroitin sulfate proteoglycans (By
CC similarity). Can also bind heparin (By similarity). Intracellular
CC signaling cascades are triggered via the coreceptor NGFR. Signaling
CC mediates activation of Rho and downstream reorganization of the actin
CC cytoskeleton. Mediates axonal growth inhibition (By similarity). May
CC play a role in regulating axon regeneration and neuronal plasticity in
CC the adult central nervous system. Plays a role in postnatal brain
CC development. Required for normal axon migration across the brain
CC midline and normal formation of the corpus callosum. Protects
CC motoneurons against apoptosis; protection against apoptosis is probably
CC mediated via interaction with MAG. Acts in conjunction with RTN4 and
CC LINGO1 in regulating neuronal precursor cell motility during cortical
CC development. Like other family members, plays a role in restricting the
CC number dendritic spines and the number of synapses that are formed
CC during brain development (By similarity). Interacts with OMG (By
CC similarity). {ECO:0000250|UniProtKB:Q99PI8,
CC ECO:0000250|UniProtKB:Q9BZR6}.
CC -!- SUBUNIT: Homodimer. Interacts with MAG (By similarity). Interacts with
CC RTN4 (By similarity). Interacts with NGFR. Interacts with LINGO1.
CC Interacts with KIAA0319L (By similarity). Interacts with OLFM1; this
CC inhibits interaction with LINGO1 and NGFR (By similarity).
CC {ECO:0000250|UniProtKB:Q99PI8, ECO:0000250|UniProtKB:Q9BZR6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BZR6};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9BZR6}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9BZR6}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q99PI8}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q99PI8}. Perikaryon
CC {ECO:0000250|UniProtKB:Q99M75}. Note=Detected along dendrites and
CC axons, close to synapses, but clearly excluded from synapses.
CC {ECO:0000250|UniProtKB:Q99PI8}.
CC -!- PTM: N-glycosylated. O-glycosylated. Contains terminal sialic acid
CC groups on its glycan chains. {ECO:0000250|UniProtKB:Q99M75}.
CC -!- SIMILARITY: Belongs to the Nogo receptor family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Nerve regrowth: nipped by a
CC no-go - Issue 69 of April 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/069";
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DR EMBL; AB045987; BAB01569.1; -; mRNA.
DR RefSeq; NP_001306507.1; NM_001319578.1.
DR AlphaFoldDB; Q9N0E3; -.
DR SMR; Q9N0E3; -.
DR STRING; 9541.XP_005567993.1; -.
DR GeneID; 102139327; -.
DR CTD; 65078; -.
DR eggNOG; KOG0619; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:1905573; F:ganglioside GM1 binding; ISS:UniProtKB.
DR GO; GO:1905576; F:ganglioside GT1b binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0038131; F:neuregulin receptor activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 7.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Disulfide bond; Glycoprotein; GPI-anchor;
KW Leucine-rich repeat; Lipoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..447
FT /note="Reticulon-4 receptor"
FT /id="PRO_0000022255"
FT PROPEP 448..473
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022256"
FT DOMAIN 27..55
FT /note="LRRNT"
FT REPEAT 56..79
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 81..103
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 104..128
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 129..152
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 153..176
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 178..200
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 202..224
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 225..248
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 250..273
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT DOMAIN 260..310
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT REGION 346..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 447
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..33
FT /evidence="ECO:0000250|UniProtKB:Q99PI8"
FT DISULFID 31..43
FT /evidence="ECO:0000250|UniProtKB:Q99PI8"
FT DISULFID 264..287
FT /evidence="ECO:0000250|UniProtKB:Q99PI8"
FT DISULFID 266..335
FT /evidence="ECO:0000250|UniProtKB:Q99PI8"
FT DISULFID 309..336
FT /evidence="ECO:0000250|UniProtKB:Q99PI8"
SQ 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
