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Q9BZR6

- RTN4R_HUMAN

UniProt

Q9BZR6 - RTN4R_HUMAN

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Protein

Reticulon-4 receptor

Gene
RTN4R, NOGOR, UNQ330/PRO526
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. receptor activity Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: UniProtKB
  2. negative regulation of axonogenesis Source: Reactome
  3. neurotrophin TRK receptor signaling pathway Source: Reactome
  4. regulation of axonogenesis Source: Reactome
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: Chromosome 22

Organism-specific databases

HGNCiHGNC:18601. RTN4R.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: DFLAT
  3. endoplasmic reticulum Source: LIFEdb
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38600.

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 form Reviewed predictionPRO_0000022254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 332 Publications
Disulfide bondi31 ↔ 432 Publications
Glycosylationi82 – 821N-linked (GlcNAc...)1 Publication
Glycosylationi179 – 1791N-linked (GlcNAc...)1 Publication
Disulfide bondi264 ↔ 2872 Publications
Disulfide bondi266 ↔ 3092 Publications
Lipidationi447 – 4471GPI-anchor amidated serine Reviewed prediction

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.
GenevestigatoriQ9BZR6.

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. 1 interaction.
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 – 343
Beta strandi36 – 383
Beta strandi40 – 423
Beta strandi60 – 634
Turni74 – 796
Beta strandi85 – 873
Turni98 – 1036
Beta strandi109 – 1113
Turni123 – 1286
Beta strandi134 – 1363
Turni147 – 1526
Beta strandi158 – 1603
Turni171 – 1766
Beta strandi182 – 1843
Turni195 – 2006
Beta strandi206 – 2083
Turni219 – 2246
Beta strandi230 – 2323
Helixi243 – 2464
Beta strandi254 – 2563
Helixi266 – 2683
Helixi269 – 2779
Beta strandi280 – 2823
Beta strandi286 – 2905
Helixi291 – 2933
Helixi298 – 3003
Helixi303 – 3053

3D structure databases

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

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.
Contains 1 LRRCT domain.
Contains 1 LRRNT domain.

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiCOG4886.
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

MKRASAGGSR LLAWVLWLQA WQVAAPCPGA CVCYNEPKVT TSCPQQGLQA    50
VPVGIPAASQ RIFLHGNRIS HVPAASFRAC RNLTILWLHS NVLARIDAAA 100
FTGLALLEQL DLSDNAQLRS VDPATFHGLG RLHTLHLDRC GLQELGPGLF 150
RGLAALQYLY LQDNALQALP DDTFRDLGNL THLFLHGNRI SSVPERAFRG 200
LHSLDRLLLH QNRVAHVHPH AFRDLGRLMT LYLFANNLSA LPTEALAPLR 250
ALQYLRLNDN PWVCDCRARP LWAWLQKFRG SSSEVPCSLP QRLAGRDLKR 300
LAANDLQGCA VATGPYHPIW TGRATDEEPL GLPKCCQPDA ADKASVLEPG 350
RPASAGNALK GRVPPGDSPP GNGSGPRHIN DSPFGTLPGS AEPPLTAVRP 400
EGSEPPGFPT SGPRRRPGCS RKNRTRSHCR LGQAGSGGGG TGDSEGSGAL 450
PSLTCSLTPL GLALVLWTVL GPC 473
Length:473
Mass (Da):50,708
Last modified:June 1, 2001 - v1
Checksum:iCA5624B24C584702
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13777.1.
RefSeqi NP_075380.1. NM_023004.5.
UniGenei Hs.30868.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OZN X-ray 1.52 A 26-310 [» ]
1P8T X-ray 3.20 A 27-311 [» ]
ProteinModelPortali Q9BZR6.
SMRi Q9BZR6. Positions 26-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122388. 1 interaction.
IntActi Q9BZR6. 1 interaction.
MINTi MINT-3064550.
STRINGi 9606.ENSP00000043402.

Proteomic databases

PaxDbi Q9BZR6.
PRIDEi Q9BZR6.

Protocols and materials databases

DNASUi 65078.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000043402 ; ENSP00000043402 ; ENSG00000040608 .
GeneIDi 65078.
KEGGi hsa:65078.
UCSCi uc002zru.3. human.

Organism-specific databases

CTDi 65078.
GeneCardsi GC22M020234.
HGNCi HGNC:18601. RTN4R.
HPAi CAB012443.
MIMi 605566. gene.
neXtProti NX_Q9BZR6.
PharmGKBi PA38600.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000116109.
HOVERGENi HBG063707.
InParanoidi Q9BZR6.
KOi K16659.
PhylomeDBi Q9BZR6.
TreeFami TF330080.

Enzyme and pathway databases

Reactomei REACT_13815. Axonal growth inhibition (RHOA activation).

Miscellaneous databases

EvolutionaryTracei Q9BZR6.
GeneWikii Reticulon_4_receptor.
GenomeRNAii 65078.
NextBioi 67268.
PROi Q9BZR6.
SOURCEi Search...

Gene expression databases

Bgeei Q9BZR6.
CleanExi HS_RTN4R.
Genevestigatori Q9BZR6.

Family and domain databases

InterProi IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view ]
Pfami PF13855. LRR_8. 2 hits.
[Graphical view ]
SMARTi SM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 6 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 133 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

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