RTN4R_MOUSE
ID RTN4R_MOUSE Reviewed; 473 AA.
AC Q99PI8; Q80WQ1;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Reticulon-4 receptor;
DE AltName: Full=Nogo receptor;
DE Short=NgR {ECO:0000303|PubMed:15504325};
DE AltName: Full=Nogo-66 receptor {ECO:0000303|PubMed:15504325};
DE AltName: Full=Nogo66 receptor-1 {ECO:0000303|PubMed:22406547};
DE Short=NgR1 {ECO:0000303|PubMed:22406547};
DE Flags: Precursor;
GN Name=Rtn4r; Synonyms=Ngr1, Nogor;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Swiss Webster;
RX PubMed=11201742; DOI=10.1038/35053072;
RA Fournier A.E., GrandPre T., Strittmatter S.M.;
RT "Identification of a receptor mediating Nogo-66 inhibition of axonal
RT regeneration.";
RL Nature 409:341-346(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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).
RN [4]
RP INTERACTION WITH MAG, AND FUNCTION.
RX PubMed=12089450; DOI=10.1126/science.1073031;
RA Liu B.P., Fournier A., GrandPre T., Strittmatter S.M.;
RT "Myelin-associated glycoprotein as a functional ligand for the Nogo-66
RT receptor.";
RL Science 297:1190-1193(2002).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH RTN4, AND TISSUE
RP SPECIFICITY.
RX PubMed=15504325; DOI=10.1016/j.neuron.2004.10.015;
RA Kim J.E., Liu B.P., Park J.H., Strittmatter S.M.;
RT "Nogo-66 receptor prevents raphespinal and rubrospinal axon regeneration
RT and limits functional recovery from spinal cord injury.";
RL Neuron 44:439-451(2004).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=15647357; DOI=10.1073/pnas.0409026102;
RA Zheng B., Atwal J., Ho C., Case L., He X.L., Garcia K.C., Steward O.,
RA Tessier-Lavigne M.;
RT "Genetic deletion of the Nogo receptor does not reduce neurite inhibition
RT in vitro or promote corticospinal tract regeneration in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1205-1210(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18411262; DOI=10.1074/jbc.m802067200;
RA Williams G., Wood A., Williams E.J., Gao Y., Mercado M.L., Katz A.,
RA Joseph-McCarthy D., Bates B., Ling H.P., Aulabaugh A., Zaccardi J., Xie Y.,
RA Pangalos M.N., Walsh F.S., Doherty P.;
RT "Ganglioside inhibition of neurite outgrowth requires Nogo receptor
RT function: identification of interaction sites and development of novel
RT antagonists.";
RL J. Biol. Chem. 283:16641-16652(2008).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=19052207; DOI=10.1523/jneurosci.3828-08.2008;
RA Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
RA Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
RA Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
RA Strittmatter S.M.;
RT "Genetic variants of Nogo-66 receptor with possible association to
RT schizophrenia block myelin inhibition of axon growth.";
RL J. Neurosci. 28:13161-13172(2008).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=19367338; DOI=10.1371/journal.pone.0005218;
RA Woerter V., Schweigreiter R., Kinzel B., Mueller M., Barske C., Boeck G.,
RA Frentzel S., Bandtlow C.E.;
RT "Inhibitory activity of myelin-associated glycoprotein on sensory neurons
RT is largely independent of NgR1 and NgR2 and resides within Ig-Like domains
RT 4 and 5.";
RL PLoS ONE 4:E5218-E5218(2009).
RN [10]
RP FUNCTION.
RX PubMed=20093372; DOI=10.1093/cercor/bhp307;
RA Mathis C., Schroeter A., Thallmair M., Schwab M.E.;
RT "Nogo-a regulates neural precursor migration in the embryonic mouse
RT cortex.";
RL Cereb. Cortex 20:2380-2390(2010).
RN [11]
RP FUNCTION, INTERACTION WITH MAG; OLFM1; LINGO1 AND NGFR, AND TISSUE
RP SPECIFICITY.
RX PubMed=22923615; DOI=10.1074/jbc.m112.389916;
RA Nakaya N., Sultana A., Lee H.S., Tomarev S.I.;
RT "Olfactomedin 1 interacts with the Nogo A receptor complex to regulate axon
RT growth.";
RL J. Biol. Chem. 287:37171-37184(2012).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22406547; DOI=10.1038/nn.3070;
RA Dickendesher T.L., Baldwin K.T., Mironova Y.A., Koriyama Y., Raiker S.J.,
RA Askew K.L., Wood A., Geoffroy C.G., Zheng B., Liepmann C.D., Katagiri Y.,
RA Benowitz L.I., Geller H.M., Giger R.J.;
RT "NgR1 and NgR3 are receptors for chondroitin sulfate proteoglycans.";
RL Nat. Neurosci. 15:703-712(2012).
RN [13]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22325200; DOI=10.1016/j.neuron.2011.11.029;
RA Wills Z.P., Mandel-Brehm C., Mardinly A.R., McCord A.E., Giger R.J.,
RA Greenberg M.E.;
RT "The Nogo receptor family restricts synapse number in the developing
RT hippocampus.";
RL Neuron 73:466-481(2012).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=26335717; DOI=10.1038/cddis.2015.228;
RA Palandri A., Salvador V.R., Wojnacki J., Vivinetto A.L., Schnaar R.L.,
RA Lopez P.H.;
RT "Myelin-associated glycoprotein modulates apoptosis of motoneurons during
RT early postnatal development via NgR/p75(NTR) receptor-mediated activation
RT of RhoA signaling pathways.";
RL Cell Death Dis. 6:E1876-E1876(2015).
RN [15]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=27339102; DOI=10.1002/cne.24064;
RA Yoo S.W., Motari M.G., Schnaar R.L.;
RT "Agenesis of the corpus callosum in Nogo receptor deficient mice.";
RL J. Comp. Neurol. 525:291-301(2017).
RN [16] {ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L, ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N, ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P, ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 26-337, SUBUNIT, GLYCOSYLATION AT
RP ASN-82; ASN-179 AND ASN-372, AND DISULFIDE BONDS.
RX PubMed=29095159; DOI=10.1107/s2059798317013791;
RA Pronker M.F., Tas R.P., Vlieg H.C., Janssen B.J.C.;
RT "Nogo Receptor crystal structures with a native disulfide pattern suggest a
RT novel mode of self-interaction.";
RL Acta Crystallogr. D 73:860-876(2017).
CC -!- FUNCTION: Receptor for RTN4, OMG and MAG (PubMed:11201742,
CC PubMed:12089450, PubMed:15504325, PubMed:18411262, PubMed:22923615).
CC Functions as receptor for the sialylated gangliosides GT1b and GM1
CC (PubMed:18411262). Besides, functions as receptor for chondroitin
CC sulfate proteoglycans (PubMed:22406547). Can also bind heparin
CC (PubMed:22406547). Intracellular signaling cascades are triggered via
CC the coreceptor NGFR (By similarity). Signaling mediates activation of
CC Rho and downstream reorganization of the actin cytoskeleton
CC (PubMed:22325200). Mediates axonal growth inhibition (By similarity).
CC Mediates axonal growth inhibition and plays a role in regulating axon
CC regeneration and neuronal plasticity in the adult central nervous
CC system (PubMed:11201742, PubMed:12089450, PubMed:15504325,
CC PubMed:22923615). Plays a role in postnatal brain development
CC (PubMed:27339102). Required for normal axon migration across the brain
CC midline and normal formation of the corpus callosum (PubMed:27339102).
CC Protects motoneurons against apoptosis; protection against apoptosis is
CC probably mediated via interaction with MAG (PubMed:26335717). Acts in
CC conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell
CC motility during cortical development (PubMed:20093372). Like other
CC family members, plays a role in restricting the number dendritic spines
CC and the number of synapses that are formed during brain development
CC (PubMed:22325200). {ECO:0000250|UniProtKB:Q9BZR6,
CC ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:12089450,
CC ECO:0000269|PubMed:15504325, ECO:0000269|PubMed:20093372,
CC ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547,
CC ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26335717,
CC ECO:0000269|PubMed:27339102}.
CC -!- SUBUNIT: Homodimer (PubMed:29095159). Interacts with MAG
CC (PubMed:12089450). Interacts with RTN4 (PubMed:15504325). Interacts
CC with NGFR(PubMed:22923615). Interacts with LINGO1(PubMed:22923615).
CC Interacts with KIAA0319L (By similarity). Interacts with OLFM1; this
CC inhibits interaction with LINGO1 and NGFR (PubMed:22923615). Interacts
CC with OMG (By similarity). {ECO:0000250|UniProtKB:Q99M75,
CC ECO:0000250|UniProtKB:Q9BZR6, ECO:0000269|PubMed:12089450,
CC ECO:0000269|PubMed:15504325, ECO:0000269|PubMed:22923615,
CC ECO:0000269|PubMed:29095159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11201742,
CC ECO:0000269|PubMed:22325200}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:11201742}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9BZR6}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22325200}. Cell projection, axon
CC {ECO:0000269|PubMed:22325200}. Perikaryon
CC {ECO:0000250|UniProtKB:Q99M75}. Note=Detected along dendrites and
CC axons, close to synapses, but clearly excluded from synapses.
CC {ECO:0000269|PubMed:22325200}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic hippocampus neurons
CC (PubMed:22325200). Detected in brain (at protein level)
CC (PubMed:15504325, PubMed:22406547). Detected in neurons in the
CC neocortex, in hippocampus, dorsal thalamus, cerebellum granule cell
CC layer and the mitral cell layer in the olfactory bulb
CC (PubMed:15647357). Detected in brain, dorsal root ganglion and heart.
CC {ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:15504325,
CC ECO:0000269|PubMed:15647357, ECO:0000269|PubMed:22325200,
CC ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:22923615}.
CC -!- PTM: N-glycosylated (PubMed:29095159). O-glycosylated. Contains
CC terminal sialic acid groups on its glycan chains (By similarity).
CC {ECO:0000250|UniProtKB:Q99M75, ECO:0000269|PubMed:29095159}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, are
CC viable and fertile (PubMed:15504325, PubMed:15647357). They display
CC subtle changes in exploratory behavior, manifest deficits in spatial
CC working memory performance, and show impaired ability to stay on a
CC rotarod (PubMed:15504325 and PubMed:19052207). Compared to wild-type
CC littermates, cultured hippocampus neurons from mutant mice display an
CC increased number of excitatory synapses (PubMed:22325200). Effects on
CC neurite outgrowth are controversial and may depend on the mouse strain,
CC cell type, and the experimental conditions (PubMed:15504325,
CC PubMed:15647357, PubMed:18411262, PubMed:19367338). Cultured neurons
CC display impaired axon growth cone collapse in response to myelin, MAG
CC and RTN4 (PubMed:15504325). Mutant cerebellar and dorsal root ganglion
CC neurons show no decrease of the inhibition of neurite outgrowth by
CC myelin or RTN4 (PubMed:15647357). Mutant cerebellar neurons display
CC decreased inhibition of neurite outgrowth mediated by MAG and by cross-
CC linking ganglioside GT1b (in vitro) (PubMed:18411262). Likewise, mutant
CC sensory neurons show no decrease of the inhibition of neurite outgrowth
CC by MAG (PubMed:19367338). Mutant mice have improved functional recovery
CC and increased regeneration of rubrospinal and raphespinal fibers after
CC spinal cord transection. Still, there is no regeneration of
CC corticospinal fibers (PubMed:15504325, PubMed:15647357). Mice lacking
CC both Rtn4r and Rtn4rl2 display no visible phenotype (PubMed:19367338).
CC Sensory neurons from mice lacking both Rtn4r and Rtn4rl2 show
CC moderately decreased inhibition of neurite outgrowth by MAG
CC (PubMed:19367338). Mice with a triple gene disruption that lack Rtn4r,
CC Rtn4rl1 and Rtn4rl2 have no visible phenotype, are healthy and viable
CC (PubMed:22406547). Mice with a triple gene disruption that lack Rtn4r,
CC Rtn4rl1 and Rtn4rl2 have normal brain size and grossly normal brain
CC anatomy, but display disruption of medial brain structures, including
CC an absence of the fasciola cinereum, corpus callosum agenesis and
CC formation of bilateral Probst bundles indicative of the failure of
CC callosally projecting neurons to extend across the midline
CC (PubMed:27339102). Mice with a triple gene disruption of Rtn4r, Rtn4rl1
CC and Rtn4rl2 display impaired ability to stay on a rotarod and increased
CC spontaneous locomotion (PubMed:27339102). These mice display an
CC increased number of excitatory synapses in the apical dendritic regions
CC of hippocampus neurons, an increase in the complexity of dendrite
CC structure and increased total dendrite length (PubMed:22325200). One
CC month after birth, mice with a triple gene disruption that lack Rtn4r,
CC Rtn4rl1 and Rtn4rl2 show a significant reduction in the survival of
CC motoneurons (PubMed:26335717). Compared to wild-type or single mutants,
CC cerebellar granule cells from mice lacking Rtn4r, Rtn4rl1 and Rtn4rl2
CC show decreased myelin-mediated inhibition of neurite outgrowth, an
CC inhibition that is strongly decreased on myelin deficient in Mag, Rtn4
CC and Omg (PubMed:22406547). Mice lacking both Rtn4r and Rtn4rl1 show
CC increased axon regeneration after injury; the same effect is observed
CC when Rtn4r, Rtn4rl1 and Rtn4rl2 are disrupted (PubMed:22406547).
CC Combined disruption of Rtn4r, Rtn4rl1 and Ptprs further increases axon
CC regeneration after injury (PubMed:22406547). Single gene disruption of
CC Rtn4r, Rtn4rl1 and Rtn4rl2 and combined disruption of Rtn4r and Rtn4rl2
CC have no effect on axon regeneration (PubMed:22406547).
CC {ECO:0000269|PubMed:15504325, ECO:0000269|PubMed:15647357,
CC ECO:0000269|PubMed:18411262, ECO:0000269|PubMed:19052207,
CC ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:22325200,
CC ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:26335717,
CC ECO:0000269|PubMed:27339102}.
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; AF283462; AAG53611.1; -; mRNA.
DR EMBL; BC052317; AAH52317.2; -; mRNA.
DR EMBL; BC058381; AAH58381.1; -; mRNA.
DR CCDS; CCDS37279.1; -.
DR RefSeq; NP_075358.1; NM_022982.2.
DR PDB; 5O0K; X-ray; 2.30 A; A/B=27-337.
DR PDB; 5O0L; X-ray; 2.51 A; A/B=27-337.
DR PDB; 5O0M; X-ray; 1.90 A; A/B=26-337.
DR PDB; 5O0N; X-ray; 2.50 A; A=27-337.
DR PDB; 5O0O; X-ray; 2.20 A; A/B/C/D/E/F/G/H=27-337.
DR PDB; 5O0P; X-ray; 2.00 A; A/B=26-348.
DR PDB; 5O0Q; X-ray; 2.50 A; A/B/C/D=26-348.
DR PDB; 5O0R; X-ray; 2.50 A; A/B=26-348.
DR PDB; 7R86; X-ray; 1.65 A; A/B=27-309.
DR PDBsum; 5O0K; -.
DR PDBsum; 5O0L; -.
DR PDBsum; 5O0M; -.
DR PDBsum; 5O0N; -.
DR PDBsum; 5O0O; -.
DR PDBsum; 5O0P; -.
DR PDBsum; 5O0Q; -.
DR PDBsum; 5O0R; -.
DR PDBsum; 7R86; -.
DR AlphaFoldDB; Q99PI8; -.
DR SMR; Q99PI8; -.
DR BioGRID; 211123; 2.
DR CORUM; Q99PI8; -.
DR IntAct; Q99PI8; 1.
DR MINT; Q99PI8; -.
DR STRING; 10090.ENSMUSP00000062924; -.
DR GlyConnect; 2681; 1 N-Linked glycan (2 sites).
DR GlyGen; Q99PI8; 4 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q99PI8; -.
DR PhosphoSitePlus; Q99PI8; -.
DR PaxDb; Q99PI8; -.
DR PeptideAtlas; Q99PI8; -.
DR PRIDE; Q99PI8; -.
DR ProteomicsDB; 256638; -.
DR ABCD; Q99PI8; 1 sequenced antibody.
DR Antibodypedia; 23162; 336 antibodies from 34 providers.
DR DNASU; 65079; -.
DR Ensembl; ENSMUST00000059589; ENSMUSP00000062924; ENSMUSG00000043811.
DR GeneID; 65079; -.
DR KEGG; mmu:65079; -.
DR UCSC; uc007ymv.1; mouse.
DR CTD; 65078; -.
DR MGI; MGI:2136886; Rtn4r.
DR VEuPathDB; HostDB:ENSMUSG00000043811; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160711; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; Q99PI8; -.
DR OMA; MWLNLLP; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q99PI8; -.
DR TreeFam; TF330080; -.
DR BioGRID-ORCS; 65079; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q99PI8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q99PI8; protein.
DR Bgee; ENSMUSG00000043811; Expressed in primary visual cortex and 109 other tissues.
DR Genevisible; Q99PI8; MM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0035374; F:chondroitin sulfate binding; IDA: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; IDA:UniProtKB.
DR GO; GO:0038131; F:neuregulin receptor activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0048495; F:Roundabout binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0022038; P:corpus callosum development; IMP:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0023041; P:neuronal signal transduction; IDA:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
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 PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Disulfide bond; Glycoprotein;
KW GPI-anchor; Heparin-binding; Leucine-rich repeat; Lipoprotein; Membrane;
KW Receptor; Reference proteome; Repeat; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..447
FT /note="Reticulon-4 receptor"
FT /id="PRO_0000022257"
FT PROPEP 448..473
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022258"
FT DOMAIN 27..57
FT /note="LRRNT"
FT REPEAT 58..79
FT /note="LRR 1"
FT REPEAT 82..103
FT /note="LRR 2"
FT REPEAT 106..128
FT /note="LRR 3"
FT REPEAT 131..152
FT /note="LRR 4"
FT REPEAT 155..176
FT /note="LRR 5"
FT REPEAT 179..200
FT /note="LRR 6"
FT REPEAT 203..224
FT /note="LRR 7"
FT REPEAT 227..248
FT /note="LRR 8"
FT DOMAIN 260..311
FT /note="LRRCT"
FT REGION 346..446
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:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT DISULFID 27..33
FT /evidence="ECO:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT DISULFID 31..43
FT /evidence="ECO:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT DISULFID 264..287
FT /evidence="ECO:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT DISULFID 266..335
FT /evidence="ECO:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT DISULFID 309..336
FT /evidence="ECO:0000269|PubMed:29095159,
FT ECO:0007744|PDB:5O0K, ECO:0007744|PDB:5O0L,
FT ECO:0007744|PDB:5O0M, ECO:0007744|PDB:5O0N,
FT ECO:0007744|PDB:5O0O, ECO:0007744|PDB:5O0P,
FT ECO:0007744|PDB:5O0Q, ECO:0007744|PDB:5O0R"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:7R86"
FT TURN 74..79
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7R86"
FT TURN 98..103
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7R86"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5O0K"
FT TURN 147..152
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7R86"
FT TURN 171..176
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7R86"
FT TURN 195..200
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:7R86"
FT TURN 219..224
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:7R86"
FT TURN 243..248
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:7R86"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:7R86"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7R86"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:7R86"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:7R86"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:7R86"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:7R86"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5O0O"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:5O0O"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5O0M"
SQ SEQUENCE 473 AA; 50987 MW; 14C5270EBF557E7C CRC64;
MKRASSGGSR LLAWVLWLQA WRVATPCPGA CVCYNEPKVT TSCPQQGLQA VPTGIPASSQ
RIFLHGNRIS HVPAASFQSC RNLTILWLHS NALARIDAAA FTGLTLLEQL DLSDNAQLHV
VDPTTFHGLG HLHTLHLDRC GLRELGPGLF RGLAALQYLY LQDNNLQALP DNTFRDLGNL
THLFLHGNRI PSVPEHAFRG LHSLDRLLLH QNHVARVHPH AFRDLGRLMT LYLFANNLSM
LPAEVLMPLR SLQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCNLP QRLADRDLKR
LAASDLEGCA VASGPFRPIQ TSQLTDEELL SLPKCCQPDA ADKASVLEPG RPASAGNALK
GRVPPGDTPP GNGSGPRHIN DSPFGTLPSS AEPPLTALRP GGSEPPGLPT TGPRRRPGCS
RKNRTRSHCR LGQAGSGASG TGDAEGSGAL PALACSLAPL GLALVLWTVL GPC
