R4RL1_RAT
ID R4RL1_RAT Reviewed; 445 AA.
AC Q80WD0; A1L1I9; Q7TQ96;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Reticulon-4 receptor-like 1;
DE AltName: Full=Nogo receptor-like 2;
DE AltName: Full=Nogo-66 receptor homolog 2 {ECO:0000303|PubMed:12694398};
DE AltName: Full=Nogo-66 receptor-related protein 3;
DE Short=NgR3 {ECO:0000303|PubMed:15673660};
DE Flags: Precursor;
GN Name=Rtn4rl1 {ECO:0000312|RGD:727812};
GN Synonyms=Ngrh2 {ECO:0000303|PubMed:12694398, ECO:0000312|EMBL:AAP21838.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP21838.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAP21838.1};
RX PubMed=12694398; DOI=10.1046/j.1471-4159.2003.01710.x;
RA Pignot V., Hein A.E., Barske C., Wiessner C., Walmsley A.R., Kaupmann K.,
RA Mayeur H., Sommer B., Mir A.K., Frentzel S.;
RT "Characterization of two novel proteins, NgRH1 and NgRH2, structurally and
RT biochemically homologous to the Nogo-66 receptor.";
RL J. Neurochem. 85:717-728(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAP74960.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAP74960.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAP74960.1};
RA Jin W.-L., Long M., Ju G.;
RT "Cloning and expression of rat NGRH1 and NGRH2.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND LACK OF INTERACTION WITH MAG;
RP OMG AND RTN4.
RX PubMed=15673660; DOI=10.1523/jneurosci.4464-04.2005;
RA Venkatesh K., Chivatakarn O., Lee H., Joshi P.S., Kantor D.B., Newman B.A.,
RA Mage R., Rader C., Giger R.J.;
RT "The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent receptor
RT selective for myelin-associated glycoprotein.";
RL J. Neurosci. 25:808-822(2005).
RN [5]
RP FUNCTION.
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).
CC -!- FUNCTION: Cell surface receptor. Plays a functionally redundant role in
CC postnatal brain development and in regulating axon regeneration in the
CC adult central nervous system. Contributes to normal axon migration
CC across the brain midline and normal formation of the corpus callosum.
CC Protects motoneurons against apoptosis; protection against apoptosis is
CC probably mediated by MAG. Plays a role in inhibiting neurite outgrowth
CC and axon regeneration via its binding to neuronal chondroitin sulfate
CC proteoglycans. Binds heparin (By similarity). Like other family
CC members, plays a role in restricting the number dendritic spines and
CC the number of synapses that are formed during brain development
CC (PubMed:22325200). Signaling mediates activation of Rho and downstream
CC reorganization of the actin cytoskeleton (PubMed:22325200).
CC {ECO:0000250|UniProtKB:Q8K0S5, ECO:0000269|PubMed:22325200}.
CC -!- SUBUNIT: Identified in a complex that contains RTN4R, RTN4RL1 and NGFR;
CC the interaction depends on the presence of chondroitin sulfate
CC proteoglycans (By similarity). Does not interact with MAG, OMG and RTN4
CC (PubMed:15673660). {ECO:0000250|UniProtKB:Q8K0S5,
CC ECO:0000269|PubMed:15673660}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15673660};
CC Lipid-anchor, GPI-anchor {ECO:0000305}. Membrane raft
CC {ECO:0000250|UniProtKB:Q86UN2}. Perikaryon
CC {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:15673660}. Cell
CC projection {ECO:0000269|PubMed:15673660}. Note=Localized to the surface
CC of neurons, including axons. {ECO:0000269|PubMed:12694398,
CC ECO:0000269|PubMed:15673660}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12694398};
CC IsoId=Q80WD0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.2};
CC IsoId=Q80WD0-2; Sequence=VSP_051945, VSP_051946;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:15673660). Expressed in various regions of the brain, including
CC the cerebral cortex, hippocampus, striatum, thalamus and cerebellum
CC (PubMed:12694398). {ECO:0000269|PubMed:12694398,
CC ECO:0000269|PubMed:15673660}.
CC -!- SIMILARITY: Belongs to the Nogo receptor family. {ECO:0000305}.
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DR EMBL; AF532861; AAP21838.1; -; mRNA.
DR EMBL; AY311478; AAP74960.1; -; mRNA.
DR EMBL; BC129084; AAI29085.1; -; mRNA.
DR RefSeq; NP_852042.1; NM_181377.3. [Q80WD0-1]
DR AlphaFoldDB; Q80WD0; -.
DR SMR; Q80WD0; -.
DR STRING; 10116.ENSRNOP00000058866; -.
DR PaxDb; Q80WD0; -.
DR Ensembl; ENSRNOT00000067414; ENSRNOP00000058866; ENSRNOG00000003121. [Q80WD0-1]
DR GeneID; 303311; -.
DR KEGG; rno:303311; -.
DR CTD; 146760; -.
DR RGD; 727812; Rtn4rl1.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157112; -.
DR InParanoid; Q80WD0; -.
DR OMA; HRKPGKN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q80WD0; -.
DR TreeFam; TF330080; -.
DR PRO; PR:Q80WD0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003121; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q80WD0; RN.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:RGD.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0048495; F:Roundabout binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:RGD.
DR GO; GO:0022038; P:corpus callosum development; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
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 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; 3.
DR SMART; SM00369; LRR_TYP; 7.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Glycoprotein;
KW GPI-anchor; Leucine-rich repeat; Lipoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..424
FT /note="Reticulon-4 receptor-like 1"
FT /id="PRO_0000046046"
FT PROPEP 425..445
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000046047"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 25..54
FT /note="LRRNT"
FT REPEAT 55..76
FT /note="LRR 1"
FT REPEAT 77..98
FT /note="LRR 2"
FT REPEAT 101..123
FT /note="LRR 3"
FT REPEAT 126..147
FT /note="LRR 4"
FT REPEAT 150..171
FT /note="LRR 5"
FT REPEAT 174..195
FT /note="LRR 6"
FT REPEAT 198..219
FT /note="LRR 7"
FT REPEAT 222..243
FT /note="LRR 8"
FT DOMAIN 255..306
FT /note="LRRCT"
FT REGION 304..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 424
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_051945"
FT VAR_SEQ 8
FT /note="V -> M (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_051946"
SQ SEQUENCE 445 AA; 49775 MW; 013FA4F1CE24A87C CRC64;
MLRKGCCVEL LLLLLAGELP LSGGCPRDCV CYPSPMTVSC QAHNFAAIPE GIPEDSERIF
LQNNHITFLQ QGHFSPAMVT LWIYSNNITF IAPNTFEGFV HLEELDLGDN RQLRTLAPET
FQGLVKLHAL YLYKCGLSSL PAGIFGGLHS LQYLYLQDNH IEYLQDDIFV DLVNLSHLFL
HGNKLWSLGQ GIFRGLVNLD RLLLHENQLQ WVHHKAFHDL HRLTTLFLFN NSLTELQGDC
LAPLVALEFL RLNGNAWDCG CRARSLWEWL RRFRGSSSVV PCATPELRQG QDLKSLRVED
FRNCTGPASP HQIKSHTLST SDRAARKEHH PSHGASRDKG HPHGHLPGSR SGSKKPGKNC
TSHRNRNQIS KGSAGKELPE LQDYAPDYQH KFSFDIMPTA RPKRKGKCAR RTPIRAPSGV
QQASSGTALG VSLLAWILGL VVSLR
