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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. Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton. Mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system. Acts in conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell motility during cortical development.By similarity1 Publication

GO - Molecular functioni

  • neuregulin receptor activity Source: UniProtKB
  • protein kinase inhibitor activity Source: GO_Central
  • receptor activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi620810. Rtn4r.

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 447421Reticulon-4 receptorPRO_0000022259Add
BLAST
Propeptidei448 – 47326Removed in mature formSequence analysisPRO_0000022260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 331 Publication
Disulfide bondi31 ↔ 431 Publication
Glycosylationi82 – 821N-linked (GlcNAc...)By similarity
Glycosylationi179 – 1791N-linked (GlcNAc...)By similarity
Disulfide bondi264 ↔ 2871 Publication
Disulfide bondi266 ↔ 309By similarity
Lipidationi447 – 4471GPI-anchor amidated serineSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ99M75.

Expressioni

Gene expression databases

ExpressionAtlasiQ99M75. baseline and differential.
GenevisibleiQ99M75. RN.

Interactioni

Subunit structurei

Homomultimer (By similarity). 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 similarity

Protein-protein interaction databases

MINTiMINT-243866.
STRINGi10116.ENSRNOP00000041517.

Structurei

Secondary structure

1
473
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343Combined sources
Beta strandi36 – 383Combined sources
Beta strandi40 – 423Combined sources
Beta strandi60 – 634Combined sources
Beta strandi85 – 873Combined sources
Beta strandi94 – 963Combined sources
Turni98 – 1036Combined sources
Beta strandi109 – 1113Combined sources
Turni123 – 1286Combined sources
Beta strandi134 – 1363Combined sources
Turni147 – 1526Combined sources
Beta strandi158 – 1603Combined sources
Turni171 – 1766Combined sources
Beta strandi182 – 1843Combined sources
Turni195 – 2006Combined sources
Beta strandi206 – 2083Combined sources
Turni219 – 2246Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi254 – 2563Combined sources
Helixi268 – 27710Combined sources
Helixi291 – 2933Combined sources
Helixi298 – 3003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KJ4X-ray3.10A/D27-312[»]
ProteinModelPortaliQ99M75.
SMRiQ99M75. Positions 27-311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99M75.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 5731LRRNTAdd
BLAST
Repeati58 – 7922LRR 1Add
BLAST
Repeati82 – 10322LRR 2Add
BLAST
Repeati106 – 12823LRR 3Add
BLAST
Repeati131 – 15222LRR 4Add
BLAST
Repeati155 – 17622LRR 5Add
BLAST
Repeati179 – 20022LRR 6Add
BLAST
Repeati203 – 22422LRR 7Add
BLAST
Repeati227 – 24822LRR 8Add
BLAST
Domaini260 – 31152LRRCTAdd
BLAST

Sequence similaritiesi

Belongs to the Nogo receptor family.Curated
Contains 8 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000116109.
HOVERGENiHBG063707.
InParanoidiQ99M75.
KOiK16659.
OrthoDBiEOG7CZK5N.
PhylomeDBiQ99M75.
TreeFamiTF330080.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 132LA → PT in AAK20166 (Ref. 1) Curated
Sequence conflicti43 – 431C → R in AAK20166 (Ref. 1) Curated
Sequence conflicti53 – 531T → A in AAK20166 (Ref. 1) Curated
Sequence conflicti284 – 2841E → G in AAK20166 (Ref. 1) Curated
Sequence conflicti287 – 2871C → S in AAK20166 (Ref. 1) Curated
Sequence conflicti303 – 3031A → T in AAK20166 (Ref. 1) Curated
Sequence conflicti355 – 3551A → V in AAK20166 (Ref. 1) Curated

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.

Cross-referencesi

Web resourcesi

Protein Spotlight

Nerve regrowth: nipped by a no-go - Issue 69 of April 2006

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KJ4X-ray3.10A/D27-312[»]
ProteinModelPortaliQ99M75.
SMRiQ99M75. Positions 27-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-243866.
STRINGi10116.ENSRNOP00000041517.

Proteomic databases

PaxDbiQ99M75.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi65078.
RGDi620810. Rtn4r.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000116109.
HOVERGENiHBG063707.
InParanoidiQ99M75.
KOiK16659.
OrthoDBiEOG7CZK5N.
PhylomeDBiQ99M75.
TreeFamiTF330080.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ99M75.
PROiQ99M75.

Gene expression databases

ExpressionAtlasiQ99M75. baseline and differential.
GenevisibleiQ99M75. RN.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification and preparation of polyclonal antibody against rat Nogo receptor."
    Jin W.-L., Jia W., Long M., Ju G.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Nogo-A: a molecule with two active sites and two membrane topologies."
    Oertle T., van der Haar M.E., Bandtlow C.E., Huber A.B., Simonen M., Schnell L., Broesamle C., Schwab M.E.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron regeneration."
    Ng C.E.L., Tang B.L.
    J. Neurosci. Res. 67:559-565(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "Nogo-66 receptor antagonist peptide promotes axonal regeneration."
    GrandPre T., Li S., Strittmatter S.M.
    Nature 417:547-551(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-312, DISULFIDE BONDS.

Entry informationi

Entry nameiRTN4R_RAT
AccessioniPrimary (citable) accession number: Q99M75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 10, 2005
Last modified: July 6, 2016
This is version 123 of the entry and version 2 of the sequence. [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

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.