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 24-JAN-2024, entry version 180. 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 a receptor for the sialylated gangliosides GT1b and GM1 CC (PubMed:18411262). Besides, functions as a 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, 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q99PI8; 3 sites, 1 glycan. DR GlyGen; Q99PI8; 4 sites, 1 N-linked glycan (2 sites). DR iPTMnet; Q99PI8; -. DR PhosphoSitePlus; Q99PI8; -. DR SwissPalm; Q99PI8; -. DR PaxDb; 10090-ENSMUSP00000062924; -. DR PeptideAtlas; Q99PI8; -. DR ProteomicsDB; 256638; -. DR ABCD; Q99PI8; 1 sequenced antibody. DR Antibodypedia; 23162; 414 antibodies from 34 providers. DR DNASU; 65079; -. DR Ensembl; ENSMUST00000059589.6; ENSMUSP00000062924.6; ENSMUSG00000043811.6. DR GeneID; 65079; -. DR KEGG; mmu:65079; -. DR UCSC; uc007ymv.1; mouse. DR AGR; MGI:2136886; -. 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; HPHAFHD; -. DR OrthoDB; 5394956at2759; -. DR PhylomeDB; Q99PI8; -. DR TreeFam; TF330080; -. DR BioGRID-ORCS; 65079; 2 hits in 79 CRISPR screens. DR PRO; PR:Q99PI8; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q99PI8; Protein. DR Bgee; ENSMUSG00000043811; Expressed in primary visual cortex and 112 other cell types or tissues. 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:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0030426; C:growth cone; IDA:MGI. 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:UniProtKB. 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; Ribonuclease Inhibitor; 1. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR PANTHER; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1. DR PANTHER; PTHR24369:SF174; RETICULON-4 RECEPTOR; 1. DR Pfam; PF13855; LRR_8; 2. DR SMART; SM00369; LRR_TYP; 8. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 8. DR Genevisible; Q99PI8; MM. 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 //