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Q9BZR6

- RTN4R_HUMAN

UniProt

Q9BZR6 - RTN4R_HUMAN

Protein

Reticulon-4 receptor

Gene

RTN4R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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

    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

    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

    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 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.
    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.
    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.
    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

    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: October 1, 2014
    This is version 134 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