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UniProtKB/Swiss-Prot entry Q9NQC3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RTN4_HUMAN
Primary accession number Q9NQC3
Secondary accession numbers O94962 Q7L7Q8 Q96B16 Q9BXG5 Q9H212 Q9H3I3 Q9UQ42 Q9Y293 Q9Y2Y7 Q9Y5U6
Integrated into Swiss-Prot on November 16, 2001
Sequence was last modified on November 16, 2001 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 94)
Name and origin of the protein
Protein name Reticulon-4
Synonyms Neurite outgrowth inhibitor
Nogo protein
Foocen
Neuroendocrine-specific protein
NSP
Neuroendocrine-specific protein C homolog
RTN-x
Reticulon-5
Gene name
Name: RTN4
Synonyms: KIAA0886, NOGO
ORFNames: My043, SP1507
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=10773680 [NCBI, ExPASy, EBI, Israel, Japan]
Yang J., Yu L., Bi A.D., Zhao S.-Y.;
"Assignment of the human reticulon 4 gene (RTN4) to chromosome 2p14-->2p13 by radiation hybrid mapping.";
Cytogenet. Cell Genet. 88:101-102(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
DOI=10.1038/35000287; PubMed=10667780 [NCBI, ExPASy, EBI, Israel, Japan]
Prinjha R., Moore S.E., Vinson M., Blake S., Morrow R., Christie G., Michalovich D., Simmons D.L., Walsh F.S.;
"Inhibitor of neurite outgrowth in humans.";
Nature 403:383-384(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
DOI=10.1038/sj.onc.1203948; PubMed=11126360 [NCBI, ExPASy, EBI, Israel, Japan]
Tagami S., Eguchi Y., Kinoshita M., Takeda M., Tsujimoto Y.;
"A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity.";
Oncogene 19:5736-5746(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
TISSUE=Testis;
PubMed=11866689 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou Z.M., Sha J.H., Li J.M., Lin M., Zhu H., Zhou Y.D., Wang L.R., Zhu H., Wang Y.Q., Zhou K.Y.;
"Expression of a novel reticulon-like gene in human testis.";
Reproduction 123:227-234(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 5).
DOI=10.1016/S0022-2836(02)01179-8; PubMed=12488097 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Fibroblast;
Yutsudo M.;
"Isolation of a cell death-inducing gene.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Pituitary;
Song H., Peng Y., Zhou J., Huang Q., Dai M., Mao Y.M., Yu Y., Xu X., Luo B., Hu R., Chen J.;
"Human neuroendocrine-specific protein C (NSP) homolog gene.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Placenta, and Skeletal muscle;
Ito T., Schwartz S.M.;
"Cloning of a member of the reticulon gene family in human.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Jin W.-L., Ju G.;
"Developmentally-regulated alternative splicing in a novel Nogo-A.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1093/dnares/5.6.355; PubMed=10048485 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Umbilical cord blood;
DOI=10.1101/gr.140200; PubMed=11042152 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
DOI=10.1073/pnas.0404089101; PubMed=15498874 [NCBI, ExPASy, EBI, Israel, Japan]
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
TISSUE=Brain, Eye, Kidney, Ovary, Pancreas, Placenta, and Skeletal muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-1192 (ISOFORMS 1/4).
TISSUE=Fetal brain;
Mao Y.M., Xie Y., Zheng Z.H.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[17]
TOPOLOGY, AND FUNCTION.
TISSUE=Brain;
DOI=10.1038/35000226; PubMed=10667797 [NCBI, ExPASy, EBI, Israel, Japan]
GrandPre T., Nakamura F., Vartanian T., Strittmatter S.M.;
"Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein.";
Nature 403:439-444(2000).
[18]
FUNCTION.
TISSUE=Brain;
DOI=10.1038/35053072; PubMed=11201742 [NCBI, ExPASy, EBI, Israel, Japan]
Fournier A.E., GrandPre T., Strittmatter S.M.;
"Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration.";
Nature 409:341-346(2001).
[19]
REVIEW.
DOI=10.1002/jnr.10134; PubMed=11891768 [NCBI, ExPASy, EBI, Israel, Japan]
Ng C.E.L., Tang B.L.;
"Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron regeneration.";
J. Neurosci. Res. 67:559-565(2002).
[20]
INTERACTION WITH RTN3.
DOI=10.1002/jcp.10297; PubMed=12811824 [NCBI, ExPASy, EBI, Israel, Japan]
Qi B., Qi Y., Watari A., Yoshioka N., Inoue H., Minemoto Y., Yamashita K., Sasagawa T., Yutsudo M.;
"Pro-apoptotic ASY/Nogo-B protein associates with ASYIP.";
J. Cell. Physiol. 196:312-318(2003).
[21]
INTERACTION WITH BACE1.
DOI=10.1038/nm1088; PubMed=15286784 [NCBI, ExPASy, EBI, Israel, Japan]
He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.;
"Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation.";
Nat. Med. 10:959-965(2004).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-15; SER-107; SER-184 AND THR-188, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[23]
INTERACTION WITH BACE1 AND BACE2, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
DOI=10.1111/j.1460-9568.2006.05005.x; PubMed=16965550 [NCBI, ExPASy, EBI, Israel, Japan]
Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.;
"Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein.";
Eur. J. Neurosci. 24:1237-1244(2006).
[24]
INTERACTION WITH RTN3.
DOI=10.1016/j.jmb.2006.07.094; PubMed=16979658 [NCBI, ExPASy, EBI, Israel, Japan]
He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.;
"Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins.";
J. Mol. Biol. 363:625-634(2006).
[25]
INTERACTION WITH NGBR.
DOI=10.1073/pnas.0602427103; PubMed=16835300 [NCBI, ExPASy, EBI, Israel, Japan]
Miao R.Q., Gao Y., Harrison K.D., Prendergast J., Acevedo L.M., Yu J., Hu F., Strittmatter S.M., Sessa W.C.;
"Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 103:10997-11002(2006).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-182 AND SER-184, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[28]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[29]
VARIANT [LARGE SCALE ANALYSIS] VAL-429.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF087901; AAG12205.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF148537; AAG12176.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF148538; AAG12177.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ251383; CAB99248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ251384; CAB99249.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ251385; CAB99250.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB040462; BAB18927.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB040463; BAB18928.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF333336; AAK20831.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY102285; AAM64242.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY102285; AAM64243.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY102278; AAM64247.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY102279; AAM64248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB015639; BAA83712.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077050; AAD27783.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF132047; AAD31021.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF132048; AAD31022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320999; AAG40878.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020693; BAA74909.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125103; AAD39920.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177332; AAG17976.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC013414; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC092461; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC093165; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471053; EAX00116.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471053; EAX00132.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001035; AAH01035.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007109; AAH07109.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010737; AAH10737.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012619; AAH12619.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014366; AAH14366.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016165; AAH16165.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026788; AAH26788.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068991; AAH68991.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC150182; AAI50183.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC152425; AAI52426.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC152555; AAI52556.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF063601; AAG43160.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00021766; -.
IPI00219207; -.
IPI00298289; -.
IPI00477663; -.
RefSeq NP_065393.1; -.
NP_997404.1; -.
UniGene Hs.714726
3D structure databases
PDB
2G31; NMR; -; A=1055-1114.[ExPASy / RCSB / EBI]
2JV5; NMR; -; A=1055-1108.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2G31; -.
2JV5; -.
ModBase Q9NQC3.
Protein-protein interaction databases
IntAct Q9NQC3; 20.
PTM databases
PhosphoSite Q9NQC3; -.
Enzyme and pathway databases
Pathway_Interaction_DB p75ntrpathway; p75(NTR)-mediated signaling.
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC02M055110; -.
H-InvDB HIX0002059; -.
HGNC HGNC:14085; RTN4.
GenAtlas RTN4.
HPA CAB005388; -.
MIM 604475; gene. [NCBI / EBI]
PharmGKB PA34883; -.
HUGE KIAA0886.
Gene expression databases
Bgee Q9NQC3; -.
GermOnline ENSG00000115310; Homo sapiens.
Ontologies
GO
GO:0030176; Cellular component: integral to endoplasmic reticulum membrane (inferred from direct assay from UniProtKB).
GO:0005635; Cellular component: nuclear envelope (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006915; Biological process: apoptosis (non-traceable author statement from UniProtKB).
GO:0019987; Biological process: negative regulation of anti-apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0030517; Biological process: negative regulation of axon extension (inferred from direct assay from UniProtKB).
GO:0042981; Biological process: regulation of apoptosis (non-traceable author statement from UniProtKB).
GO:0030334; Biological process: regulation of cell migration (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR003388; Reticulon.
Graphical view of domain structure.
PANTHER PTHR10994; Reticulon; 1.
Pfam PF02453; Reticulon; 1.
Pfam graphical view of domain structure.
PROSITE PS50845; RETICULON; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9NQC3; -.
Genome annotation databases
Ensembl ENSG00000115310; Homo sapiens. [Contig view]
GeneID 57142; -.
Phylogenomic databases
HOVERGEN Q9NQC3; -.
OMA Q9NQC3; KAQIVTE.
Other
NextBio 63075; -.
PMAP-CutDB Q9NQC3; -.
SOURCE RTN4; Homo sapiens.
ProtoNet Q9NQC3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Endoplasmic reticulum; Membrane; Phosphoprotein; Polymorphism; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1192  1192     Reticulon-4. PRO_0000168165
TOPO_DOM   1   1018  1018     Cytoplasmic (Potential). 
TRANSMEM   1019   1039  21     Potential. 
TOPO_DOM   1040   1133  94     Lumenal (Potential). 
TRANSMEM   1134   1154  21     Potential. 
TOPO_DOM   1155   1192  38     Cytoplasmic (Potential). 
DOMAIN   1005   1192  188     Reticulon. 
COMPBIAS   30     47  18     Poly-Glu. 
COMPBIAS   143    148  6     Poly-Pro. 
MOD_RES   7      7        Phosphoserine. 
MOD_RES   15     15        Phosphoserine. 
MOD_RES   107    107        Phosphoserine. 
MOD_RES   152    152        Phosphoserine (By similarity). 
MOD_RES   181    181        Phosphoserine. 
MOD_RES   182    182        Phosphoserine. 
MOD_RES   184    184        Phosphoserine. 
MOD_RES   188    188        Phosphothreonine. 
MOD_RES   361    361        Phosphoserine (By similarity). 
MOD_RES   446    446        Phosphoserine (By similarity). 
MOD_RES   860    860        Phosphoserine (By similarity). 
MOD_RES   863    863        Phosphoserine (By similarity). 
MOD_RES   881    881        Phosphoserine (By similarity). 
MOD_RES   889    889        Phosphotyrosine (By similarity). 
VAR_SEQ   1    993        Missing (in isoform 3). VSP_005652
VAR_SEQ   1    206        Missing (in isoform 6). VSP_037112
VAR_SEQ   58    289        Missing (in isoform 4). VSP_005654
VAR_SEQ   186   1004        Missing (in isoform 2). VSP_005655
VAR_SEQ   205   1004        Missing (in isoform 5). VSP_037113
VAR_SEQ   994   1004        AIFSAELSKTS -> MDGQKKNWKDK (in isoform 3). VSP_005653
VARIANT   357    357  1     D -> V (in dbSNP:rs11677099 [NCBI]). VAR_053633 
VARIANT   429    429  1     L -> V (in a colorectal cancer sample; somatic mutation). VAR_035904 
VARIANT   899    899  1     E -> Q (in dbSNP:rs6757519 [NCBI]). VAR_053634 
VARIANT   920    920  1     S -> C (in dbSNP:rs6757705 [NCBI]). VAR_053635 
CONFLICT   107    107        S -> C (in Ref. 6; BAA83712). 
CONFLICT   135    135        E -> Q (in Ref. 6; BAA83712). 
CONFLICT   458    458        S -> P (in Ref. 2; CAB99248). 
CONFLICT   564    564        N -> S (in Ref. 4; AAK20831). 
Sequence information
Length: 1192 AA [This is the length of the unprocessed precursor] Molecular weight: 129931 Da [This is the MW of the unprocessed precursor] CRC64: CDE239BBF31589CA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEDLDQSPLV SSSDSPPRPQ PAFKYQFVRE PEDEEEEEEE EEEDEDEDLE ELEVLERKPA 

        70         80         90        100        110        120 
AGLSAAPVPT APAAGAPLMD FGNDFVPPAP RGPLPAAPPV APERQPSWDP SPVSSTVPAP 

       130        140        150        160        170        180 
SPLSAAAVSP SKLPEDDEPP ARPPPPPPAS VSPQAEPVWT PPAPAPAAPP STPAAPKRRG 

       190        200        210        220        230        240 
SSGSVDETLF ALPAASEPVI RSSAENMDLK EQPGNTISAG QEDFPSVLLE TAASLPSLSP 

       250        260        270        280        290        300 
LSAASFKEHE YLGNLSTVLP TEGTLQENVS EASKEVSEKA KTLLIDRDLT EFSELEYSEM 

       310        320        330        340        350        360 
GSSFSVSPKA ESAVIVANPR EEIIVKNKDE EEKLVSNNIL HNQQELPTAL TKLVKEDEVV 

       370        380        390        400        410        420 
SSEKAKDSFN EKRVAVEAPM REEYADFKPF ERVWEVKDSK EDSDMLAAGG KIESNLESKV 

       430        440        450        460        470        480 
DKKCFADSLE QTNHEKDSES SNDDTSFPST PEGIKDRSGA YITCAPFNPA ATESIATNIF 

       490        500        510        520        530        540 
PLLGDPTSEN KTDEKKIEEK KAQIVTEKNT STKTSNPFLV AAQDSETDYV TTDNLTKVTE 

       550        560        570        580        590        600 
EVVANMPEGL TPDLVQEACE SELNEVTGTK IAYETKMDLV QTSEVMQESL YPAAQLCPSF 

       610        620        630        640        650        660 
EESEATPSPV LPDIVMEAPL NSAVPSAGAS VIQPSSSPLE ASSVNYESIK HEPENPPPYE 

       670        680        690        700        710        720 
EAMSVSLKKV SGIKEEIKEP ENINAALQET EAPYISIACD LIKETKLSAE PAPDFSDYSE 

       730        740        750        760        770        780 
MAKVEQPVPD HSELVEDSSP DSEPVDLFSD DSIPDVPQKQ DETVMLVKES LTETSFESMI 

       790        800        810        820        830        840 
EYENKEKLSA LPPEGGKPYL ESFKLSLDNT KDTLLPDEVS TLSKKEKIPL QMEELSTAVY 

       850        860        870        880        890        900 
SNDDLFISKE AQIRETETFS DSSPIEIIDE FPTLISSKTD SFSKLAREYT DLEVSHKSEI 

       910        920        930        940        950        960 
ANAPDGAGSL PCTELPHDLS LKNIQPKVEE KISFSDDFSK NGSATSKVLL LPPDVSALAT 

       970        980        990       1000       1010       1020 
QAEIESIVKP KVLVKEAEKK LPSDTEKEDR SPSAIFSAEL SKTSVVDLLY WRDIKKTGVV 

      1030       1040       1050       1060       1070       1080 
FGASLFLLLS LTVFSIVSVT AYIALALLSV TISFRIYKGV IQAIQKSDEG HPFRAYLESE 

      1090       1100       1110       1120       1130       1140 
VAISEELVQK YSNSALGHVN CTIKELRRLF LVDDLVDSLK FAVLMWVFTY VGALFNGLTL 

      1150       1160       1170       1180       1190 
LILALISLFS VPVIYERHQA QIDHYLGLAN KNVKDAMAKI QAKIPGLKRK AE 

Q9NQC3 in FASTA format

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