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Q9BZR6 (RTN4R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reticulon-4 receptor
Alternative name(s):
Nogo receptor
Short name=NgR
Nogo-66 receptor
Gene names
Name:RTN4R
Synonyms:NOGOR
ORF Names:UNQ330/PRO526
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.12

Subunit structure

Homomultimer. Interacts with LINGO1. Interacts with KIAA0319L. Ref.10 Ref.11 Ref.12 Ref.15

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

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

Sequence similarities

Belongs to the Nogo receptor family.

Contains 8 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KIAA0319LQ8IZA04EBI-5240240,EBI-5240269

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.8
Chain27 – 447421Reticulon-4 receptor
PRO_0000022253
Propeptide448 – 47326Removed in mature form Potential
PRO_0000022254

Regions

Domain27 – 5731LRRNT
Repeat58 – 7922LRR 1
Repeat82 – 10322LRR 2
Repeat106 – 12823LRR 3
Repeat131 – 15222LRR 4
Repeat155 – 17622LRR 5
Repeat179 – 20022LRR 6
Repeat203 – 22422LRR 7
Repeat227 – 24822LRR 8
Domain260 – 31152LRRCT
Compositional bias435 – 4428Poly-Gly

Amino acid modifications

Lipidation4471GPI-anchor amidated serine Potential
Glycosylation821N-linked (GlcNAc...) Ref.17
Glycosylation1791N-linked (GlcNAc...) Ref.17
Disulfide bond27 ↔ 33 Ref.16 Ref.17
Disulfide bond31 ↔ 43 Ref.16 Ref.17
Disulfide bond264 ↔ 287 Ref.16 Ref.17
Disulfide bond266 ↔ 309 Ref.16 Ref.17

Secondary structure

..................................................... 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BZR6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: CA5624B24C584702

FASTA47350,708
        10         20         30         40         50         60 
MKRASAGGSR LLAWVLWLQA WQVAAPCPGA CVCYNEPKVT TSCPQQGLQA VPVGIPAASQ 

        70         80         90        100        110        120 
RIFLHGNRIS HVPAASFRAC RNLTILWLHS NVLARIDAAA FTGLALLEQL DLSDNAQLRS 

       130        140        150        160        170        180 
VDPATFHGLG RLHTLHLDRC GLQELGPGLF RGLAALQYLY LQDNALQALP DDTFRDLGNL 

       190        200        210        220        230        240 
THLFLHGNRI SSVPERAFRG LHSLDRLLLH QNRVAHVHPH AFRDLGRLMT LYLFANNLSA 

       250        260        270        280        290        300 
LPTEALAPLR ALQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCSLP QRLAGRDLKR 

       310        320        330        340        350        360 
LAANDLQGCA VATGPYHPIW TGRATDEEPL GLPKCCQPDA ADKASVLEPG RPASAGNALK 

       370        380        390        400        410        420 
GRVPPGDSPP GNGSGPRHIN DSPFGTLPGS AEPPLTAVRP EGSEPPGFPT SGPRRRPGCS 

       430        440        450        460        470 
RKNRTRSHCR LGQAGSGGGG TGDSEGSGAL PSLTCSLTPL GLALVLWTVL GPC 

« Hide

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"LINGO-1 is a component of the Nogo-66 receptor/p75 signaling complex."
Mi S., Lee X., Shao Z., Thill G., Ji B., Relton J., Levesque M., Allaire N., Perrin S., Sands B., Crowell T., Cate R.L., McCoy J.M., Pepinsky R.B.
Nat. Neurosci. 7:221-228(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LINGO1.
[13]"It takes more than two to Nogo."
Woolf C.J., Bloechlinger S.
Science 297:1132-1134(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Protein Spotlight

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13777.1.
RefSeqNP_075380.1. NM_023004.5.
UniGeneHs.30868.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZNX-ray1.52A26-310[»]
1P8TX-ray3.20A27-311[»]
ProteinModelPortalQ9BZR6.
SMRQ9BZR6. Positions 26-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122388. 1 interaction.
IntActQ9BZR6. 1 interaction.
MINTMINT-3064550.
STRING9606.ENSP00000043402.

Proteomic databases

PaxDbQ9BZR6.
PRIDEQ9BZR6.

Protocols and materials databases

DNASU65078.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000043402; ENSP00000043402; ENSG00000040608.
GeneID65078.
KEGGhsa:65078.
UCSCuc002zru.3. human.

Organism-specific databases

CTD65078.
GeneCardsGC22M020234.
HGNCHGNC:18601. RTN4R.
HPACAB012443.
MIM605566. gene.
neXtProtNX_Q9BZR6.
PharmGKBPA38600.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000116109.
HOVERGENHBG063707.
InParanoidQ9BZR6.
KOK16659.
PhylomeDBQ9BZR6.
TreeFamTF330080.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeQ9BZR6.
CleanExHS_RTN4R.
GenevestigatorQ9BZR6.

Family and domain databases

InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BZR6.
GeneWikiReticulon_4_receptor.
GenomeRNAi65078.
NextBio67268.
PROQ9BZR6.
SOURCESearch...

Entry information

Entry nameRTN4R_HUMAN
AccessionPrimary (citable) accession number: Q9BZR6
Secondary accession number(s): D3DX28
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM