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Protein

Reticulon-4 receptor

Gene

Rtn4r

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for RTN4, OMG and MAG (PubMed:12037567, PubMed:15673660, PubMed:19420245). Functions as receptor for the sialylated gangliosides GT1b and GM1. Besides, functions as receptor for chondroitin sulfate proteoglycans. Can also bind heparin. Intracellular signaling cascades are triggered via the coreceptor NGFR (By similarity). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:18411262). Mediates axonal growth inhibition (PubMed:12037567). 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 (By similarity). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated via interaction with MAG (PubMed:26335717). 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 (PubMed:22325200).By similarity5 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionReceptor

Enzyme and pathway databases

ReactomeiR-RNO-193634. Axonal growth inhibition (RHOA activation).

Names & Taxonomyi

Protein namesi
Recommended name:
Reticulon-4 receptor
Alternative name(s):
Nogo receptor
Short name:
NgR
Nogo-66 receptor
Gene namesi
Name:Rtn4r
Synonyms:Nogor
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi620810. Rtn4r.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000002225927 – 447Reticulon-4 receptorAdd BLAST421
PropeptideiPRO_0000022260448 – 473Removed in mature formSequence analysisAdd BLAST26

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 33Combined sources1 Publication
Disulfide bondi31 ↔ 43Combined sources1 Publication
Glycosylationi82N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi264 ↔ 287Combined sources1 Publication
Disulfide bondi266 ↔ 309By similarity
Glycosylationi372N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi447GPI-anchor amidated serineSequence analysis1

Post-translational modificationi

N-glycosylated. O-glycosylated. Contains terminal sialic acid groups on its glycan chains.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ99M75.

Expressioni

Tissue specificityi

Detected in embryonic cerebellum, in spinal cord motor neurons and in dorsal root ganglia (PubMed:12426574). Detected in adult brain, in neocortex, hippocampus, striatum, thalamus and dorsal root ganglion neurons (at protein level).1 Publication

Developmental stagei

Expression is high in adult, but very low in neonate dorsal root ganglion neurons (at protein level).1 Publication

Gene expression databases

BgeeiENSRNOG00000030920.
GenevisibleiQ99M75. RN.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with MAG (PubMed:15673660, PubMed:19420245). Interacts with RTN4 and OMG (PubMed:15673660, PubMed:19420245). Interacts with LINGO1 and NGFR (By similarity). Interacts with KIAA0319L (By similarity). Interacts with OLFM1; this inhibits interaction with LINGO1 and NGFR (By similarity).By similarity2 Publications

Protein-protein interaction databases

MINTiMINT-243866.
STRINGi10116.ENSRNOP00000041517.

Structurei

Secondary structure

1473
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 34Combined sources3
Beta strandi36 – 38Combined sources3
Beta strandi40 – 42Combined sources3
Beta strandi60 – 63Combined sources4
Beta strandi85 – 87Combined sources3
Beta strandi94 – 96Combined sources3
Turni98 – 103Combined sources6
Beta strandi109 – 111Combined sources3
Turni123 – 128Combined sources6
Beta strandi134 – 136Combined sources3
Turni147 – 152Combined sources6
Beta strandi158 – 160Combined sources3
Turni171 – 176Combined sources6
Beta strandi182 – 184Combined sources3
Turni195 – 200Combined sources6
Beta strandi206 – 208Combined sources3
Turni219 – 224Combined sources6
Beta strandi230 – 232Combined sources3
Beta strandi254 – 256Combined sources3
Helixi268 – 277Combined sources10
Helixi291 – 293Combined sources3
Helixi298 – 300Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KJ4X-ray3.10A/D27-312[»]
ProteinModelPortaliQ99M75.
SMRiQ99M75.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99M75.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 57LRRNTSequence analysisAdd BLAST31
Repeati56 – 79LRR 1Sequence analysisAdd BLAST24
Repeati80 – 103LRR 2Sequence analysisAdd BLAST24
Repeati105 – 128LRR 3Sequence analysisAdd BLAST24
Repeati129 – 152LRR 4Sequence analysisAdd BLAST24
Repeati153 – 176LRR 5Sequence analysisAdd BLAST24
Repeati178 – 200LRR 6Sequence analysisAdd BLAST23
Repeati202 – 224LRR 7Sequence analysisAdd BLAST23
Repeati225 – 248LRR 8Sequence analysisAdd BLAST24
Repeati250 – 273LRR 9Sequence analysisAdd BLAST24
Domaini260 – 310LRRCTSequence analysisAdd BLAST51

Sequence similaritiesi

Belongs to the Nogo receptor family.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118777.
HOGENOMiHOG000116109.
HOVERGENiHBG063707.
InParanoidiQ99M75.
KOiK16659.
OMAiNDSPFGT.
OrthoDBiEOG091G08II.
PhylomeDBiQ99M75.
TreeFamiTF330080.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiView protein in InterPro
IPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
PfamiView protein in Pfam
PF13855. LRR_8. 2 hits.
SMARTiView protein in SMART
SM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 1 hit.
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiView protein in PROSITE
PS51450. LRR. 8 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99M75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRASSGGSR LLAWVLWLQA WRVATPCPGA CVCYNEPKVT TSCPQQGLQA
60 70 80 90 100
VPTGIPASSQ RIFLHGNRIS YVPAASFQSC RNLTILWLHS NALAGIDAAA
110 120 130 140 150
FTGLTLLEQL DLSDNAQLRV VDPTTFRGLG HLHTLHLDRC GLQELGPGLF
160 170 180 190 200
RGLAALQYLY LQDNNLQALP DNTFRDLGNL THLFLHGNRI PSVPEHAFRG
210 220 230 240 250
LHSLDRLLLH QNHVARVHPH AFRDLGRLMT LYLFANNLSM LPAEVLVPLR
260 270 280 290 300
SLQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCNLP QRLAGRDLKR
310 320 330 340 350
LAASDLEGCA VASGPFRPFQ TNQLTDEELL GLPKCCQPDA ADKASVLEPG
360 370 380 390 400
RPASAGNALK GRVPPGDTPP GNGSGPRHIN DSPFGTLPGS AEPPLTALRP
410 420 430 440 450
GGSEPPGLPT TGPRRRPGCS RKNRTRSHCR LGQAGSGSSG TGDAEGSGAL
460 470
PALACSLAPL GLALVLWTVL GPC
Length:473
Mass (Da):50,851
Last modified:May 10, 2005 - v2
Checksum:i3DFD17EA4651FECB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12 – 13LA → PT in AAK20166 (Ref. 1) Curated2
Sequence conflicti43C → R in AAK20166 (Ref. 1) Curated1
Sequence conflicti53T → A in AAK20166 (Ref. 1) Curated1
Sequence conflicti284E → G in AAK20166 (Ref. 1) Curated1
Sequence conflicti287C → S in AAK20166 (Ref. 1) Curated1
Sequence conflicti303A → T in AAK20166 (Ref. 1) Curated1
Sequence conflicti355A → V in AAK20166 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028438 mRNA. Translation: AAK20166.1.
AF462390 mRNA. Translation: AAM46772.1.
RefSeqiNP_446065.1. NM_053613.1.
UniGeneiRn.229952.

Genome annotation databases

EnsembliENSRNOT00000051037; ENSRNOP00000041517; ENSRNOG00000030920.
GeneIDi113912.
KEGGirno:113912.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiRTN4R_RAT
AccessioniPrimary (citable) accession number: Q99M75
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 10, 2005
Last modified: July 5, 2017
This is version 131 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families