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Protein

Reticulon-4 receptor-like 2

Gene

Rtn4rl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface receptor that plays a functionally redundant role in the inhibition of neurite outgrowth mediated by MAG (PubMed:15673660). Plays a functionally redundant role in postnatal brain development. Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum. Does not seem to play a significant role in regulating axon regeneration in the adult central nervous system (By similarity). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG (PubMed:26335717). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:22325200).By similarity3 Publications

GO - Molecular functioni

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

GO - Biological processi

  • cell surface receptor signaling pathway Source: UniProtKB
  • corpus callosum development Source: RGD
  • cytokine-mediated signaling pathway Source: GO_Central
  • negative regulation of JAK-STAT cascade Source: GO_Central
  • negative regulation of neuron projection development Source: UniProtKB
  • negative regulation of protein kinase activity Source: GO_Central

Keywordsi

Molecular functionReceptor

Enzyme and pathway databases

ReactomeiR-RNO-163125. Post-translational modification: synthesis of GPI-anchored proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Reticulon-4 receptor-like 2
Alternative name(s):
Nogo receptor-like 3
Nogo-66 receptor homolog 11 Publication
Nogo-66 receptor-related protein 2
Short name:
NgR21 Publication
Gene namesi
Name:Rtn4rl2Imported
Synonyms:Ngrh11 PublicationImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi727797. Rtn4rl2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000004605231 – 390Reticulon-4 receptor-like 2Add BLAST360
PropeptideiPRO_0000046053391 – 420Removed in mature formSequence analysisAdd BLAST30

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 37Combined sources1 Publication
Disulfide bondi35 ↔ 46Combined sources1 Publication
Glycosylationi50N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi93N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi236N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi265 ↔ 288Combined sources1 Publication
Disulfide bondi267 ↔ 310Combined sources1 Publication
Lipidationi390GPI-anchor amidated cysteineSequence analysis1

Post-translational modificationi

Undergoes zinc metalloproteinase-mediated ectodomain shedding in neuroblastoma cells; is released both as a full-length ectodomain and an N-terminal fragment containing the leucine-rich repeat (LRR) region of the protein.By similarity
N-glycosylated (PubMed:19420245, PubMed:21308849). O-glycosylated (PubMed:19420245). Contains terminal sialic acid groups on its glycan chains (PubMed:19420245).2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ80WD1.
PRIDEiQ80WD1.

Expressioni

Tissue specificityi

Detected in adult brain, in neocortex, hippocampus, striatum and dorsal root ganglion neurons, and in retina (at protein level) (PubMed:15673660). In brain, detected in cerebral cortex and hippocampus. Weak or no expression detected in the cerebellum, thalamus or striatum (PubMed:12694398).2 Publications

Developmental stagei

Expression is high in adult, but very low in neonate dorsal root ganglion neurons (at protein level).1 Publication

Gene expression databases

BgeeiENSRNOG00000021513.

Interactioni

Subunit structurei

Interaction with MAG is controversial, and may be indirect (Probable). Interacts with MAG (PubMed:15673660, PubMed:19420245, PubMed:21308849). Does not interact with OMG and RTN4 (PubMed:15673660).Curated3 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000032922.

Structurei

Secondary structure

1420
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Turni39 – 42Combined sources4
Beta strandi43 – 45Combined sources3
Beta strandi64 – 66Combined sources3
Beta strandi85 – 88Combined sources4
Turni99 – 104Combined sources6
Beta strandi110 – 112Combined sources3
Turni124 – 129Combined sources6
Beta strandi135 – 137Combined sources3
Turni148 – 153Combined sources6
Beta strandi159 – 161Combined sources3
Turni172 – 177Combined sources6
Beta strandi183 – 185Combined sources3
Turni196 – 201Combined sources6
Beta strandi207 – 209Combined sources3
Turni220 – 225Combined sources6
Beta strandi231 – 233Combined sources3
Helixi244 – 248Combined sources5
Beta strandi255 – 257Combined sources3
Helixi267 – 269Combined sources3
Helixi270 – 278Combined sources9
Beta strandi287 – 291Combined sources5
Helixi292 – 294Combined sources3
Helixi299 – 301Combined sources3
Helixi304 – 307Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4P8SX-ray1.80A29-310[»]
4P91X-ray2.10A29-330[»]
ProteinModelPortaliQ80WD1.
SMRiQ80WD1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 60LRRNTAdd BLAST30
Repeati61 – 82LRR 1Add BLAST22
Repeati83 – 104LRR 2Add BLAST22
Repeati107 – 129LRR 3Add BLAST23
Repeati132 – 153LRR 4Add BLAST22
Repeati156 – 177LRR 5Add BLAST22
Repeati180 – 201LRR 6Add BLAST22
Repeati204 – 225LRR 7Add BLAST22
Repeati228 – 249LRR 8Add BLAST22
Domaini261 – 312LRRCTAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni315 – 327Important for interaction with MAG1 PublicationAdd BLAST13

Sequence similaritiesi

Belongs to the Nogo receptor family.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00900000140818.
HOGENOMiHOG000116109.
HOVERGENiHBG063707.
InParanoidiQ80WD1.
KOiK16661.
OMAiPTEDDYW.
OrthoDBiEOG091G08II.
PhylomeDBiQ80WD1.
TreeFamiTF330080.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiView protein in InterPro
IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR032675. LRR_dom_sf.
PfamiView protein in Pfam
PF13855. LRR_8. 2 hits.
SMARTiView protein in SMART
SM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 1 hit.
SUPFAMiSSF52058. SSF52058. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q80WD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPGLRRLLQ GPASACLLLT LLALPPVTPS CPMLCTCYSS PPTVSCQANN
60 70 80 90 100
FSSVPLSLPP STQRLFLQNN LIRSLRPGTF GPNLLTLWLF SNNLSTIYPG
110 120 130 140 150
TFRHLQALEE LDLGDNRHLR SLEPDTFQGL ERLQSLHLYR CQLSSLPGNI
160 170 180 190 200
FRGLVSLQYL YLQENSLLHL QDDLFADLAN LSHLFLHGNR LRLLTEHVFR
210 220 230 240 250
GLGSLDRLLL HGNRLQGVHR AAFHGLSRLT ILYLFNNSLA SLPGEALADL
260 270 280 290 300
PALEFLRLNA NPWACDCRAR PLWAWFQRAR VSSSDVTCAT PPERQGRDLR
310 320 330 340 350
TLRDTDFQAC PPPTPTRPGS RARGNSSSNH LYGVAEAGAP PADPSTLYRD
360 370 380 390 400
LPAEDSRGRQ GGDAPTEDDY WGGYGGEDQR GEQTCPGAAC QAPADSRGPV
410 420
LSAGLRTPLL CLLLLAPHHL
Length:420
Mass (Da):46,184
Last modified:June 1, 2003 - v1
Checksum:i27536A80B4E34EF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF532860 mRNA. Translation: AAP21837.1.
RefSeqiNP_852045.1. NM_181380.2.
UniGeneiRn.162683.

Genome annotation databases

EnsembliENSRNOT00000038250; ENSRNOP00000032922; ENSRNOG00000021513.
GeneIDi311169.
KEGGirno:311169.
UCSCiRGD:727797. rat.

Similar proteinsi

Entry informationi

Entry nameiR4RL2_RAT
AccessioniPrimary (citable) accession number: Q80WD1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: June 1, 2003
Last modified: November 22, 2017
This is version 109 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families