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Reticulon-4 receptor-like 2 (Nogo receptor-like 3) (Nogo-66 receptor homolog 1) (Nogo-66 receptor-related protein 2) (NgR2)

 R4RL2_MOUSE             Reviewed;         420 AA.
Q7M6Z0; A2RTJ0; Q3UQ62;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
20-JUN-2018, entry version 122.
RecName: Full=Reticulon-4 receptor-like 2;
AltName: Full=Nogo receptor-like 3;
AltName: Full=Nogo-66 receptor homolog 1;
AltName: Full=Nogo-66 receptor-related protein 2;
Short=NgR2 {ECO:0000303|PubMed:19367338};
Flags: Precursor;
Name=Rtn4rl2 {ECO:0000312|MGI:MGI:2669796};
Synonyms=Ngrl3 {ECO:0000312|EMBL:AAP82837.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAP82837.1}
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
TISSUE=Brain {ECO:0000269|PubMed:14664809};
PubMed=14664809; DOI=10.1016/S1044-7431(03)00199-4;
Lauren J., Airaksinen M.S., Saarma M., Timmusk T.;
"Two novel mammalian nogo receptor homologs differentially expressed
in the central and peripheral nervous systems.";
Mol. Cell. Neurosci. 24:581-594(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3] {ECO:0000305, ECO:0000312|EMBL:BAE25181.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 379-420.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25181.1};
TISSUE=Heart {ECO:0000312|EMBL:BAE25181.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4] {ECO:0000312|EMBL:DAA01386.1}
IDENTIFICATION.
PubMed=12839991; DOI=10.1093/emboj/cdg325;
Barton W.A., Liu B.P., Tzvetkova D., Jeffrey P.D., Fournier A.E.,
Sah D., Cate R., Strittmatter S.M., Nikolov D.B.;
"Structure and axon outgrowth inhibitor binding of the Nogo-66
receptor and related proteins.";
EMBO J. 22:3291-3302(2003).
[5]
DISRUPTION PHENOTYPE.
PubMed=15673660; DOI=10.1523/JNEUROSCI.4464-04.2005;
Venkatesh K., Chivatakarn O., Lee H., Joshi P.S., Kantor D.B.,
Newman B.A., Mage R., Rader C., Giger R.J.;
"The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent receptor
selective for myelin-associated glycoprotein.";
J. Neurosci. 25:808-822(2005).
[6]
DISRUPTION PHENOTYPE.
PubMed=19367338; DOI=10.1371/journal.pone.0005218;
Woerter V., Schweigreiter R., Kinzel B., Mueller M., Barske C.,
Boeck G., Frentzel S., Bandtlow C.E.;
"Inhibitory activity of myelin-associated glycoprotein on sensory
neurons is largely independent of NgR1 and NgR2 and resides within Ig-
Like domains 4 and 5.";
PLoS ONE 4:E5218-E5218(2009).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=22406547; DOI=10.1038/nn.3070;
Dickendesher T.L., Baldwin K.T., Mironova Y.A., Koriyama Y.,
Raiker S.J., Askew K.L., Wood A., Geoffroy C.G., Zheng B.,
Liepmann C.D., Katagiri Y., Benowitz L.I., Geller H.M., Giger R.J.;
"NgR1 and NgR3 are receptors for chondroitin sulfate proteoglycans.";
Nat. Neurosci. 15:703-712(2012).
[8]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22325200; DOI=10.1016/j.neuron.2011.11.029;
Wills Z.P., Mandel-Brehm C., Mardinly A.R., McCord A.E., Giger R.J.,
Greenberg M.E.;
"The Nogo receptor family restricts synapse number in the developing
hippocampus.";
Neuron 73:466-481(2012).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=26335717; DOI=10.1038/cddis.2015.228;
Palandri A., Salvador V.R., Wojnacki J., Vivinetto A.L., Schnaar R.L.,
Lopez P.H.;
"Myelin-associated glycoprotein modulates apoptosis of motoneurons
during early postnatal development via NgR/p75(NTR) receptor-mediated
activation of RhoA signaling pathways.";
Cell Death Dis. 6:E1876-E1876(2015).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=27339102; DOI=10.1002/cne.24064;
Yoo S.W., Motari M.G., Schnaar R.L.;
"Agenesis of the corpus callosum in Nogo receptor deficient mice.";
J. Comp. Neurol. 525:291-301(2017).
-!- FUNCTION: Cell surface receptor that plays a functionally
redundant role in the inhibition of neurite outgrowth mediated by
MAG (By similarity). Plays a functionally redundant role in
postnatal brain development (PubMed:27339102). Contributes to
normal axon migration across the brain midline and normal
formation of the corpus callosum (PubMed:27339102). Does not seem
to play a significant role in regulating axon regeneration in the
adult central nervous system (PubMed:22406547). 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). {ECO:0000250|UniProtKB:Q80WD1,
ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547,
ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27339102}.
-!- SUBUNIT: Interaction with MAG is controversial, and may be
indirect (Probable). Interacts with MAG. Does not interact with
OMG and RTN4 (By similarity). {ECO:0000250|UniProtKB:Q80WD1,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q86UN3}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:Q86UN3}. Membrane raft
{ECO:0000250|UniProtKB:Q80WD1}. Cell projection, dendrite
{ECO:0000269|PubMed:22325200}. Cell projection, axon
{ECO:0000269|PubMed:22325200}. Perikaryon
{ECO:0000250|UniProtKB:Q80WD1}. Note=Localized to the surface of
neurons, including axons. Detected close to synapses, but is
excluded from synapses. {ECO:0000269|PubMed:22325200}.
-!- TISSUE SPECIFICITY: Detected in brain (PubMed:22406547). Detected
in hippocampus neurons (at protein level) (PubMed:22325200).
{ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547}.
-!- DEVELOPMENTAL STAGE: At E13.5, strongly expressed in PNS ganglia
and developing heart, and weakly expressed in brain and spinal
cord. By postnatal day 1, strongly expressed in dorsal root
ganglia and in dorsal and gray matter areas of spinal cord.
Expressed in various adult brain structures including the
amygdala, cerebral cortex, cerebellum, hippocampus and olfactory
bulb. {ECO:0000269|PubMed:14664809}.
-!- PTM: 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.
{ECO:0000250|UniProtKB:Q86UN3}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q86UN3}.
-!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:19367338).
Mutant sensory neurons show no decrease of the inhibition of
neurite outgrowth by MAG (PubMed:19367338). Compared to wild-type
littermates, cultured hippocampus neurons from mutant mice display
an increased number of excitatory synapses (PubMed:22325200).
Likewise, mice lacking both Rtn4r and Rtn4rl2 display no visible
phenotype (PubMed:19367338). Sensory neurons from mice lacking
both Rtn4r and Rtn4rl2 show moderately decreased inhibition of
neurite outgrowth by MAG (PubMed:19367338). Mice with a triple
gene disruption that lack Rtn4r, Rtn4rl1 and Rtn4rl2 have no
visible phenotype, are healthy and viable (PubMed:22406547,
PubMed:22325200). Mice with a triple gene disruption that lack
Rtn4r, Rtn4rl1 and Rtn4rl2 have normal brain size and grossly
normal brain anatomy, but display disruption of medial brain
structures, including an absence of the fasciola cinereum, corpus
callosum agenesis and formation of bilateral Probst bundles
indicative of the failure of callosally projecting neurons to
extend across the midline (PubMed:27339102). Mice with a triple
gene disruption of Rtn4r, Rtn4rl1 and Rtn4rl2 display impaired
ability to stay on a rotarod and increased spontaneous locomotion
(PubMed:27339102). These mice display an increased number of
excitatory synapses in the apical dendritic regions of hippocampus
neurons, an increase in the complexity of dendrite structure and
increased total dendrite length (PubMed:22325200). One month after
birth, mice with a triple gene disruption that lack Rtn4r, Rtn4rl1
and Rtn4rl2 show a significant reduction in the survival of
motoneurons (PubMed:26335717). Compared to wild-type or single
mutants, cerebellar granule cells from mice lacking Rtn4r, Rtn4rl1
and Rtn4rl2 show decreased myelin-mediated inhibition of neurite
outgrowth, an inhibition that is strongly decreased on myelin
deficient in Mag, Rtn4 and Omg (PubMed:22406547). Mice lacking
both Rtn4r and Rtn4rl1 show increased axon regeneration after
injury; the same effect is observed when Rtn4r, Rtn4rl1 and
Rtn4rl2 are disrupted (PubMed:22406547). Combined disruption of
Rtn4r, Rtn4rl1 and Ptprs further increases axon regeneration after
injury (PubMed:22406547). Single gene disruption of Rtn4r, Rtn4rl1
and Rtn4rl2 and combined disruption of Rtn4r and Rtn4rl2 have no
effect on axon regeneration (PubMed:22406547).
{ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:22325200,
ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:26335717,
ECO:0000269|PubMed:27339102}.
-!- SIMILARITY: Belongs to the Nogo receptor family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE25181.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY250220; AAP82837.1; -; mRNA.
EMBL; BC132523; AAI32524.1; -; mRNA.
EMBL; BC138154; AAI38155.1; -; mRNA.
EMBL; AK142743; BAE25181.1; ALT_SEQ; mRNA.
EMBL; BK001303; DAA01386.1; -; mRNA.
CCDS; CCDS16197.1; -.
RefSeq; NP_954693.1; NM_199223.1.
UniGene; Mm.389289; -.
UniGene; Mm.86447; -.
ProteinModelPortal; Q7M6Z0; -.
SMR; Q7M6Z0; -.
STRING; 10090.ENSMUSP00000057725; -.
iPTMnet; Q7M6Z0; -.
PhosphoSitePlus; Q7M6Z0; -.
PaxDb; Q7M6Z0; -.
PRIDE; Q7M6Z0; -.
Ensembl; ENSMUST00000054514; ENSMUSP00000057725; ENSMUSG00000050896.
GeneID; 269295; -.
KEGG; mmu:269295; -.
UCSC; uc008kjm.1; mouse.
CTD; 349667; -.
MGI; MGI:2669796; Rtn4rl2.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00920000148971; -.
HOGENOM; HOG000116109; -.
HOVERGEN; HBG063707; -.
InParanoid; Q7M6Z0; -.
KO; K16661; -.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
PRO; PR:Q7M6Z0; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000050896; -.
CleanEx; MM_RTN4RL2; -.
ExpressionAtlas; Q7M6Z0; baseline and differential.
Genevisible; Q7M6Z0; MM.
GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
GO; GO:0031103; P:axon regeneration; TAS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0022038; P:corpus callosum development; IMP:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF13855; LRR_8; 2.
SMART; SM00369; LRR_TYP; 8.
SMART; SM00082; LRRCT; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome; Disulfide bond;
Glycoprotein; GPI-anchor; Leucine-rich repeat; Lipoprotein; Membrane;
Receptor; Reference proteome; Repeat; Signal.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 398 Reticulon-4 receptor-like 2.
/FTId=PRO_0000046050.
PROPEP 399 420 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000046051.
DOMAIN 31 60 LRRNT.
REPEAT 61 82 LRR 1.
REPEAT 83 104 LRR 2.
REPEAT 107 129 LRR 3.
REPEAT 132 153 LRR 4.
REPEAT 156 177 LRR 5.
REPEAT 180 201 LRR 6.
REPEAT 204 225 LRR 7.
REPEAT 228 249 LRR 8.
DOMAIN 261 312 LRRCT.
REGION 315 327 Important for interaction with MAG.
{ECO:0000250|UniProtKB:Q80WD1}.
LIPID 398 398 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q80WD1}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q80WD1}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q80WD1}.
DISULFID 31 37 {ECO:0000250|UniProtKB:Q80WD1}.
DISULFID 35 46 {ECO:0000250|UniProtKB:Q80WD1}.
DISULFID 265 288 {ECO:0000250|UniProtKB:Q80WD1}.
DISULFID 267 310 {ECO:0000250|UniProtKB:Q80WD1}.
SEQUENCE 420 AA; 46075 MW; 412500FEE8154B47 CRC64;
MLPGLRRLLQ GPASACLLLT LLALPSVTPS CPMLCTCYSS PPTVSCQANN FSSVPLSLPP
STQRLFLQNN LIRSLRPGTF GPNLLTLWLF SNNLSTIHPG TFRHLQALEE LDLGDNRHLR
SLEPDTFQGL ERLQSLHLYR CQLSSLPGNI FRGLVSLQYL YLQENSLLHL QDDLFADLAN
LSHLFLHGNR LRLLTEHVFR GLGSLDRLLL HGNRLQGVHR AAFHGLSRLT ILYLFNNSLA
SLPGEALADL PALEFLRLNA NPWACDCRAR PLWAWFQRAR VSSSDVTCAT PPERQGRDLR
ALRDSDFQAC PPPTPTRPGS RARGNSSSNH LYGVAEAGAP PADPSTLYRD LPAEDSRGRQ
GGDAPTEDDY WGGYGGEDQR GEQTCPGAAC QAPADSRGPA LSAGLRTPLL CLLPLALHHL


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