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Protein

Reticulon-4 receptor

Gene

RTN4R

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for RTN4, OMG and MAG. 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 LIGO1 in regulating neuronal precursor cell motility during cortical development (By similarity).By similarity

GO - Molecular functioni

  • receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_13815. 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
ORF Names:UNQ330/PRO526
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:18601. RTN4R.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cell surface Source: DFLAT
  • endoplasmic reticulum Source: LIFEdb
  • extracellular exosome Source: UniProtKB
  • growth cone Source: Ensembl
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38600.

Polymorphism and mutation databases

BioMutaiRTN4R.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 447421Reticulon-4 receptorPRO_0000022253Add
BLAST
Propeptidei448 – 47326Removed in mature formSequence AnalysisPRO_0000022254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 33
Disulfide bondi31 ↔ 43
Glycosylationi82 – 821N-linked (GlcNAc...)1 Publication
Glycosylationi179 – 1791N-linked (GlcNAc...)1 Publication
Disulfide bondi264 ↔ 287
Disulfide bondi266 ↔ 309
Lipidationi447 – 4471GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9BZR6.
PRIDEiQ9BZR6.

Expressioni

Tissue specificityi

Widespread in the brain but highest levels in the gray matter. Low levels in heart and kidney not expressed in oligodendrocytes (white matter).

Gene expression databases

BgeeiQ9BZR6.
CleanExiHS_RTN4R.
ExpressionAtlasiQ9BZR6. baseline and differential.
GenevisibleiQ9BZR6. HS.

Organism-specific databases

HPAiCAB012443.

Interactioni

Subunit structurei

Homomultimer. Interacts with LINGO1. Interacts with KIAA0319L.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KIAA0319LQ8IZA04EBI-5240240,EBI-5240269

Protein-protein interaction databases

BioGridi122388. 5 interactions.
IntActiQ9BZR6. 1 interaction.
MINTiMINT-3064550.
STRINGi9606.ENSP00000043402.

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
Turni74 – 796Combined sources
Beta strandi85 – 873Combined 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
Helixi243 – 2464Combined sources
Beta strandi254 – 2563Combined sources
Helixi266 – 2683Combined sources
Helixi269 – 2779Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi286 – 2905Combined sources
Helixi291 – 2933Combined sources
Helixi298 – 3003Combined sources
Helixi303 – 3053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZNX-ray1.52A26-310[»]
1P8TX-ray3.20A27-311[»]
ProteinModelPortaliQ9BZR6.
SMRiQ9BZR6. Positions 26-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZR6.

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi435 – 4428Poly-Gly

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

eggNOGiCOG4886.
GeneTreeiENSGT00760000118777.
HOGENOMiHOG000116109.
HOVERGENiHBG063707.
InParanoidiQ9BZR6.
KOiK16659.
PhylomeDBiQ9BZR6.
TreeFamiTF330080.

Family and domain databases

InterProiIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BZR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRASAGGSR LLAWVLWLQA WQVAAPCPGA CVCYNEPKVT TSCPQQGLQA
60 70 80 90 100
VPVGIPAASQ RIFLHGNRIS HVPAASFRAC RNLTILWLHS NVLARIDAAA
110 120 130 140 150
FTGLALLEQL DLSDNAQLRS VDPATFHGLG RLHTLHLDRC GLQELGPGLF
160 170 180 190 200
RGLAALQYLY LQDNALQALP DDTFRDLGNL THLFLHGNRI SSVPERAFRG
210 220 230 240 250
LHSLDRLLLH QNRVAHVHPH AFRDLGRLMT LYLFANNLSA LPTEALAPLR
260 270 280 290 300
ALQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCSLP QRLAGRDLKR
310 320 330 340 350
LAANDLQGCA VATGPYHPIW TGRATDEEPL GLPKCCQPDA ADKASVLEPG
360 370 380 390 400
RPASAGNALK GRVPPGDSPP GNGSGPRHIN DSPFGTLPGS AEPPLTAVRP
410 420 430 440 450
EGSEPPGFPT SGPRRRPGCS RKNRTRSHCR LGQAGSGGGG TGDSEGSGAL
460 470
PSLTCSLTPL GLALVLWTVL GPC
Length:473
Mass (Da):50,708
Last modified:June 1, 2001 - v1
Checksum:iCA5624B24C584702
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF283463 mRNA. Translation: AAG53612.1.
AL834449 mRNA. Translation: CAD39109.1.
AY358297 mRNA. Translation: AAQ88664.1.
CR456360 mRNA. Translation: CAG30246.1.
AC058790 Genomic DNA. No translation available.
AC007663 Genomic DNA. No translation available.
CH471176 Genomic DNA. Translation: EAX02975.1.
CH471176 Genomic DNA. Translation: EAX02976.1.
BC011787 mRNA. Translation: AAH11787.1.
CCDSiCCDS13777.1.
RefSeqiNP_075380.1. NM_023004.5.
UniGeneiHs.30868.

Genome annotation databases

EnsembliENST00000043402; ENSP00000043402; ENSG00000040608.
GeneIDi65078.
KEGGihsa:65078.
UCSCiuc002zru.3. human.

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
AF283463 mRNA. Translation: AAG53612.1.
AL834449 mRNA. Translation: CAD39109.1.
AY358297 mRNA. Translation: AAQ88664.1.
CR456360 mRNA. Translation: CAG30246.1.
AC058790 Genomic DNA. No translation available.
AC007663 Genomic DNA. No translation available.
CH471176 Genomic DNA. Translation: EAX02975.1.
CH471176 Genomic DNA. Translation: EAX02976.1.
BC011787 mRNA. Translation: AAH11787.1.
CCDSiCCDS13777.1.
RefSeqiNP_075380.1. NM_023004.5.
UniGeneiHs.30868.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZNX-ray1.52A26-310[»]
1P8TX-ray3.20A27-311[»]
ProteinModelPortaliQ9BZR6.
SMRiQ9BZR6. Positions 26-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122388. 5 interactions.
IntActiQ9BZR6. 1 interaction.
MINTiMINT-3064550.
STRINGi9606.ENSP00000043402.

Polymorphism and mutation databases

BioMutaiRTN4R.

Proteomic databases

PaxDbiQ9BZR6.
PRIDEiQ9BZR6.

Protocols and materials databases

DNASUi65078.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000043402; ENSP00000043402; ENSG00000040608.
GeneIDi65078.
KEGGihsa:65078.
UCSCiuc002zru.3. human.

Organism-specific databases

CTDi65078.
GeneCardsiGC22M020234.
HGNCiHGNC:18601. RTN4R.
HPAiCAB012443.
MIMi605566. gene.
neXtProtiNX_Q9BZR6.
PharmGKBiPA38600.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118777.
HOGENOMiHOG000116109.
HOVERGENiHBG063707.
InParanoidiQ9BZR6.
KOiK16659.
PhylomeDBiQ9BZR6.
TreeFamiTF330080.

Enzyme and pathway databases

ReactomeiREACT_13815. Axonal growth inhibition (RHOA activation).

Miscellaneous databases

EvolutionaryTraceiQ9BZR6.
GeneWikiiReticulon_4_receptor.
GenomeRNAii65078.
NextBioi67268.
PROiQ9BZR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZR6.
CleanExiHS_RTN4R.
ExpressionAtlasiQ9BZR6. baseline and differential.
GenevisibleiQ9BZR6. HS.

Family and domain databases

InterProiIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration."
    Fournier A.E., GrandPre T., Strittmatter S.M.
    Nature 409:341-346(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  8. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.
  9. "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.
  10. "Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that inhibits neurite outgrowth."
    Wang K.C., Koprivica V., Kim J.A., Sivasankaran R., Guo Y., Neve R.L., He Z.
    Nature 417:941-944(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OMG.
  11. "Myelin-associated glycoprotein as a functional ligand for the Nogo-66 receptor."
    Liu B.P., Fournier A., GrandPre T., Strittmatter S.M.
    Science 297:1190-1193(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAG.
  12. Cited for: FUNCTION, INTERACTION WITH LINGO1.
  13. Cited for: REVIEW.
  14. "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.
  15. "Dyslexia-associated kiaa0319-like protein interacts with axon guidance receptor nogo receptor 1."
    Poon M.W., Tsang W.H., Chan S.O., Li H.M., Ng H.K., Waye M.M.
    Cell. Mol. Neurobiol. 31:27-35(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIAA0319L.
  16. "Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins."
    Barton W.A., Liu B.P., Tzvetkova D., Jeffrey P.D., Fournier A.E., Sah D., Cate R., Strittmatter S.M., Nikolov D.B.
    EMBO J. 22:3291-3302(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 27-311, DISULFIDE BONDS.
  17. "Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition."
    He X.L., Bazan J.F., McDermott G., Park J.B., Wang K., Tessier-Lavigne M., He Z., Garcia K.C.
    Neuron 38:177-185(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 26-310, DISULFIDE BONDS, GLYCOSYLATION AT ASN-82 AND ASN-179.

Entry informationi

Entry nameiRTN4R_HUMAN
AccessioniPrimary (citable) accession number: Q9BZR6
Secondary accession number(s): D3DX28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.