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Reticulon-4 (Neurite outgrowth inhibitor) (Nogo protein)

 RTN4_MOUSE              Reviewed;        1162 AA.
Q99P72; Q5DTK9; Q7TNB7; Q80W95; Q8BGK7; Q8BGM9; Q8K290; Q8K3G8;
Q9CTE3;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 2.
28-MAR-2018, entry version 157.
RecName: Full=Reticulon-4;
AltName: Full=Neurite outgrowth inhibitor;
Short=Nogo protein;
Name=Rtn4; Synonyms=Kiaa0886, Nogo;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
STRAIN=129/Sv;
PubMed=12488097; DOI=10.1016/S0022-2836(02)01179-8;
Oertle T., Huber C., van der Putten H., Schwab M.E.;
"Genomic structure and functional characterisation of the promoters of
human and mouse nogo/rtn4.";
J. Mol. Biol. 325:299-323(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Adipocyte;
Coulson A.C., Craggs P.D., Morris N.J.;
"Mouse vp20/RTN4C cDNA.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
Jin W., Long M., Li R., Ju G.;
"Cloning and expression of the mouse Nogo-A protein.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 585-1162.
Tozaki H., Hirata T.;
"The partial sequence of mouse nogo-A cDNA clone#4109.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 975-982; 1061-1074 AND 1079-1090, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1133-1162.
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[10]
INTERACTION WITH RTN4IP1.
PubMed=12067236; DOI=10.1046/j.1471-4159.2002.00788.x;
Hu W.-H., Hausmann O.N., Yan M.-S., Walters W.M., Wong P.K.Y.,
Bethea J.R.;
"Identification and characterization of a novel Nogo-interacting
mitochondrial protein (NIMP).";
J. Neurochem. 81:36-45(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-690, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-344 AND
SER-489, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-105, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-344;
THR-348; SER-489; SER-690; SER-727; SER-768 AND SER-857, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=20093372; DOI=10.1093/cercor/bhp307;
Mathis C., Schroeter A., Thallmair M., Schwab M.E.;
"Nogo-a regulates neural precursor migration in the embryonic mouse
cortex.";
Cereb. Cortex 20:2380-2390(2010).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20573699; DOI=10.1242/dev.048371;
Petrinovic M.M., Duncan C.S., Bourikas D., Weinman O., Montani L.,
Schroeter A., Maerki D., Sommer L., Stoeckli E.T., Schwab M.E.;
"Neuronal Nogo-A regulates neurite fasciculation, branching and
extension in the developing nervous system.";
Development 137:2539-2550(2010).
-!- FUNCTION: Developmental neurite growth regulatory factor with a
role as a negative regulator of axon-axon adhesion and growth, and
as a facilitator of neurite branching. Regulates neurite
fasciculation, branching and extension in the developing nervous
system. Involved in down-regulation of growth, stabilization of
wiring and restriction of plasticity in the adult CNS. Regulates
the radial migration of cortical neurons via an RTN4R-LINGO1
containing receptor complex. May inhibit BACE1 activity and
amyloid precursor protein processing. Induces the formation and
stabilization of endoplasmic reticulum (ER) tubules. Regulates
membrane morphogenesis in the ER by promoting tubular ER
production. Influences NE expansion, nuclear pore complex
formation and proper localization of inner nuclear membrane
proteins (By similarity). {ECO:0000250|UniProtKB:Q9NQC3,
ECO:0000269|PubMed:20093372, ECO:0000269|PubMed:20573699}.
-!- SUBUNIT: Binds to RTN4R. Interacts with Bcl-xl and Bcl-2.
Interacts in trans with CNTNAP1. Interacts with ATL1 (By
similarity). Interacts with RTN4IP1. Interacts with TMEM170A and
TMEM33 (By similarity). {ECO:0000250|UniProtKB:Q9NQC3,
ECO:0000269|PubMed:12067236}.
-!- INTERACTION:
P48722:Hspa4l; NbExp=4; IntAct=EBI-3869532, EBI-8314699;
P52592:S1pr2; NbExp=2; IntAct=EBI-3869532, EBI-16091339;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9NQC3}; Multi-pass membrane protein
{ECO:0000255}. Note=Anchored to the membrane of the endoplasmic
reticulum through 2 putative transmembrane domains. Localizes
throughout the ER tubular network. Co-localizes with TMEM33 at the
ER sheets. {ECO:0000250|UniProtKB:Q9NQC3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q99P72-2; Sequence=Displayed;
Name=2;
IsoId=Q99P72-3; Sequence=VSP_018089, VSP_018090;
Name=3;
IsoId=Q99P72-1; Sequence=VSP_018088, VSP_018091;
-!- DEVELOPMENTAL STAGE: Expressed in radial glial cells, migrating
postmitotic as well as postmigratory neurons of the embryonic
cortex. {ECO:0000269|PubMed:20093372}.
-!- DOMAIN: Three regions, residues 59-172, 544-725 and the loop 66
amino acids, between the two transmembrane domains, known as Nogo-
66 loop, appear to be responsible for the inhibitory effect on
neurite outgrowth and the spreading of neurons. This Nogo-66 loop,
mediates also the binding of RTN4 to its receptor (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryos show defects in the development of
fore- and hindlimb innervation. Increased fasciculation and
decreased branching of nerves innervating fore- and hindlimbs
seen. Disturbances of the radial migration pattern of neuronal
precursor cells seen in embryonic cortex.
{ECO:0000269|PubMed:20093372, ECO:0000269|PubMed:20573699}.
-!- SEQUENCE CAUTION:
Sequence=AAH32192.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BC056373; Type=Erroneous termination; Positions=721; Note=Translated as Glu.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Nerve regrowth: nipped
by a no-go - Issue 69 of April 2006;
URL="https://web.expasy.org/spotlight/back_issues/069";
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EMBL; AY102280; AAM73502.1; -; mRNA.
EMBL; AY102284; AAM73506.1; -; mRNA.
EMBL; AY102286; AAM73507.1; -; Genomic_DNA.
EMBL; AY102286; AAM73511.1; -; Genomic_DNA.
EMBL; AF326337; AAK08076.1; -; mRNA.
EMBL; AY114152; AAM77068.1; -; mRNA.
EMBL; AK220511; BAD90301.1; -; mRNA.
EMBL; AL929371; CAI24273.1; -; Genomic_DNA.
EMBL; AL929371; CAI24274.1; -; Genomic_DNA.
EMBL; BC032192; AAH32192.1; ALT_INIT; mRNA.
EMBL; BC056373; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB073672; BAC75974.1; -; mRNA.
EMBL; AK003859; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS24501.1; -. [Q99P72-2]
CCDS; CCDS24502.1; -. [Q99P72-3]
CCDS; CCDS24503.1; -. [Q99P72-1]
RefSeq; NP_077188.1; NM_024226.4. [Q99P72-1]
RefSeq; NP_918940.1; NM_194051.3. [Q99P72-3]
RefSeq; NP_918943.1; NM_194054.3. [Q99P72-2]
UniGene; Mm.192580; -.
UniGene; Mm.440639; -.
UniGene; Mm.488364; -.
PDB; 2KO2; NMR; -; A=1025-1090.
PDBsum; 2KO2; -.
ProteinModelPortal; Q99P72; -.
SMR; Q99P72; -.
BioGrid; 212938; 7.
CORUM; Q99P72; -.
DIP; DIP-41976N; -.
IntAct; Q99P72; 7.
MINT; Q99P72; -.
STRING; 10090.ENSMUSP00000099907; -.
iPTMnet; Q99P72; -.
PhosphoSitePlus; Q99P72; -.
SwissPalm; Q99P72; -.
EPD; Q99P72; -.
MaxQB; Q99P72; -.
PaxDb; Q99P72; -.
PeptideAtlas; Q99P72; -.
PRIDE; Q99P72; -.
Ensembl; ENSMUST00000060992; ENSMUSP00000053754; ENSMUSG00000020458. [Q99P72-1]
Ensembl; ENSMUST00000102841; ENSMUSP00000099905; ENSMUSG00000020458. [Q99P72-3]
Ensembl; ENSMUST00000102843; ENSMUSP00000099907; ENSMUSG00000020458. [Q99P72-2]
GeneID; 68585; -.
KEGG; mmu:68585; -.
UCSC; uc007ihk.2; mouse. [Q99P72-2]
UCSC; uc007ihn.2; mouse. [Q99P72-3]
CTD; 57142; -.
MGI; MGI:1915835; Rtn4.
eggNOG; KOG1792; Eukaryota.
eggNOG; ENOG410XPKH; LUCA.
GeneTree; ENSGT00390000009934; -.
HOVERGEN; HBG023134; -.
InParanoid; Q99P72; -.
KO; K20720; -.
OMA; PLLEDHT; -.
OrthoDB; EOG091G0TIO; -.
PhylomeDB; Q99P72; -.
TreeFam; TF105431; -.
Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation).
ChiTaRS; Rtn4; mouse.
EvolutionaryTrace; Q99P72; -.
PRO; PR:Q99P72; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020458; -.
CleanEx; MM_RTN4; -.
ExpressionAtlas; Q99P72; baseline and differential.
Genevisible; Q99P72; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0044294; C:dendritic growth cone; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:MGI.
GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0007413; P:axonal fasciculation; IMP:UniProtKB.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:MGI.
GO; GO:0021801; P:cerebral cortex radial glia guided migration; IMP:UniProtKB.
GO; GO:0071787; P:endoplasmic reticulum tubular network formation; ISS:UniProtKB.
GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; ISS:UniProtKB.
GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISS:UniProtKB.
GO; GO:0030517; P:negative regulation of axon extension; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:1903860; P:negative regulation of dendrite extension; IMP:MGI.
GO; GO:1905943; P:negative regulation of formation of growth cone in injured axon; IMP:MGI.
GO; GO:0007399; P:nervous system development; IDA:MGI.
GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
GO; GO:0048694; P:positive regulation of collateral sprouting of injured axon; IMP:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:1905580; P:positive regulation of ERBB3 signaling pathway; ISO:MGI.
GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:1905552; P:positive regulation of protein localization to endoplasmic reticulum; ISO:MGI.
GO; GO:0050821; P:protein stabilization; IMP:CAFA.
GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; IMP:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
GO; GO:0051960; P:regulation of nervous system development; IMP:UniProtKB.
InterPro; IPR003388; Reticulon.
Pfam; PF02453; Reticulon; 1.
PROSITE; PS50845; RETICULON; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Membrane;
Neurogenesis; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 1162 Reticulon-4.
/FTId=PRO_0000168166.
TOPO_DOM 1 988 Cytoplasmic. {ECO:0000255}.
TRANSMEM 989 1009 Helical. {ECO:0000255}.
TOPO_DOM 1010 1078 Lumenal. {ECO:0000255}.
TRANSMEM 1079 1099 Helical. {ECO:0000255}.
TOPO_DOM 1100 1162 Cytoplasmic. {ECO:0000255}.
DOMAIN 975 1162 Reticulon. {ECO:0000255|PROSITE-
ProRule:PRU00170}.
COMPBIAS 31 57 Glu-rich.
COMPBIAS 68 160 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQC3}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 145 145 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:19144319}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK11}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 348 348 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 426 426 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK11}.
MOD_RES 430 430 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JK11}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 768 768 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 832 832 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK11}.
MOD_RES 834 834 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JK11}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 961 961 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQC3}.
MOD_RES 1074 1074 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9NQC3}.
VAR_SEQ 1 963 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_018088.
VAR_SEQ 1 116 Missing (in isoform 2).
{ECO:0000303|PubMed:12488097}.
/FTId=VSP_018089.
VAR_SEQ 117 169 LPPAAAVLPSKLPEDDEPPARPPAPAGASPLAEPAAPPSTP
AAPKRRGSGSVD -> MAPPLAGGGQKGGAASEAWVPSLFV
GVSGSTCTAAKSLVPIPARSSRLSAARN (in isoform
2). {ECO:0000303|PubMed:12488097}.
/FTId=VSP_018090.
VAR_SEQ 964 974 AVLSAELNKTS -> MDDQKKRWKDK (in isoform
3). {ECO:0000303|Ref.2}.
/FTId=VSP_018091.
CONFLICT 4 4 I -> V (in Ref. 4; BAD90301).
{ECO:0000305}.
CONFLICT 16 16 S -> R (in Ref. 4; BAD90301).
{ECO:0000305}.
CONFLICT 21 21 P -> L (in Ref. 4; BAD90301).
{ECO:0000305}.
CONFLICT 67 67 A -> V (in Ref. 3; AAM77068).
{ECO:0000305}.
CONFLICT 413 413 G -> S (in Ref. 3; AAM77068 and 4;
BAD90301). {ECO:0000305}.
CONFLICT 429 429 R -> S (in Ref. 3; AAM77068 and 4;
BAD90301). {ECO:0000305}.
CONFLICT 448 448 S -> T (in Ref. 3; AAM77068 and 4;
BAD90301). {ECO:0000305}.
CONFLICT 487 490 KTSP -> HASA (in Ref. 6; AAH32192).
{ECO:0000305}.
CONFLICT 651 651 S -> A (in Ref. 3; AAM77068, 6; AAH32192
and 4; BAD90301). {ECO:0000305}.
CONFLICT 665 665 A -> V (in Ref. 4; BAD90301).
{ECO:0000305}.
CONFLICT 692 692 E -> G (in Ref. 3; AAM77068 and 7;
BAC75974). {ECO:0000305}.
CONFLICT 733 733 E -> D (in Ref. 4; BAD90301).
{ECO:0000305}.
CONFLICT 772 772 V -> L (in Ref. 4; BAD90301).
{ECO:0000305}.
CONFLICT 916 916 S -> F (in Ref. 7; BAC75974).
{ECO:0000305}.
CONFLICT 990 990 V -> VY (in Ref. 3; AAM77068).
{ECO:0000305}.
HELIX 1026 1029 {ECO:0000244|PDB:2KO2}.
HELIX 1031 1035 {ECO:0000244|PDB:2KO2}.
TURN 1037 1040 {ECO:0000244|PDB:2KO2}.
HELIX 1044 1053 {ECO:0000244|PDB:2KO2}.
HELIX 1057 1063 {ECO:0000244|PDB:2KO2}.
TURN 1065 1067 {ECO:0000244|PDB:2KO2}.
HELIX 1068 1082 {ECO:0000244|PDB:2KO2}.
HELIX 1087 1089 {ECO:0000244|PDB:2KO2}.
SEQUENCE 1162 AA; 126613 MW; 855697FBEE11781F CRC64;
MEDIDQSSLV SSSADSPPRP PPAFKYQFVT EPEDEEDEED EEEEEDDEDL EELEVLERKP
AAGLSAAPVP PAAAPLLDFS SDSVPPAPRG PLPAAPPTAP ERQPSWERSP AASAPSLPPA
AAVLPSKLPE DDEPPARPPA PAGASPLAEP AAPPSTPAAP KRRGSGSVDE TLFALPAASE
PVIPSSAEKI MDLKEQPGNT VSSGQEDFPS VLFETAASLP SLSPLSTVSF KEHGYLGNLS
AVASTEGTIE ETLNEASREL PERATNPFVN RESAEFSVLE YSEMGSSFNG SPKGESAMLV
ENTKEEVIVR SKDKEDLVCS AALHNPQESP ATLTKVVKED GVMSPEKTMD IFNEMKMSVV
APVREEYADF KPFEQAWEVK DTYEGSRDVL AARANMESKV DKKCFEDSLE QKGHGKDSES
RNENASFPRT PELVKDGSRA YITCDSFSSA TESTAANIFP VLEDHTSENK TDEKKIEERK
AQIITEKTSP KTSNPFLVAI HDSEADYVTT DNLSKVTEAV VATMPEGLTP DLVQEACESE
LNEATGTKIA YETKVDLVQT SEAIQESIYP TAQLCPSFEE AEATPSPVLP DIVMEAPLNS
LLPSTGASVA QPSASPLEVP SPVSYDGIKL EPENPPPYEE AMSVALKTSD SKEEIKEPES
FNAAAQEAEA PYISIACDLI KETKLSTEPS PEFSNYSEIA KFEKSVPDHC ELVDDSSPES
EPVDLFSDDS IPEVPQTQEE AVMLMKESLT EVSETVTQHK HKERLSASPQ EVGKPYLESF
QPNLHITKDA ASNEIPTLTK KETISLQMEE FNTAIYSNDD LLSSKEDKMK ESETFSDSSP
IEIIDEFPTF VSAKDDSPKE YTDLEVSNKS EIANVQSGAN SLPCSELPCD LSFKNTYPKD
EAHVSDEFSK SRSSVSKVPL LLPNVSALES QIEMGNIVKP KVLTKEAEEK LPSDTEKEDR
SLTAVLSAEL NKTSVVDLLY WRDIKKTGVV FGASLFLLLS LTVFSIVSVT AYIALALLSV
TISFRIYKGV IQAIQKSDEG HPFRAYLESE VAISEELVQK YSNSALGHVN STIKELRRLF
LVDDLVDSLK FAVLMWVFTY VGALFNGLTL LILALISLFS IPVIYERHQA QIDHYLGLAN
KSVKDAMAKI QAKIPGLKRK AE


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