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Q99P72 (RTN4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reticulon-4
Alternative name(s):
Neurite outgrowth inhibitor
Short name=Nogo protein
Gene names
Name:Rtn4
Synonyms:Kiaa0886, Nogo
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1162 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.17 Ref.18

Subunit structure

Binds to RTN4R. Interacts with Bcl-xl and Bcl-2. Interacts in trans with CNTNAP1. Interacts with ATL1 By similarity. Interacts with RTN4IP1. Ref.10

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Anchored to the membrane of the endoplasmic reticulum through 2 putative transmembrane domains By similarity.

Developmental stage

Expressed in radial glial cells, migrating postmitotic as well as postmigratory neurons of the embryonic cortex. Ref.17

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.

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. Ref.17 Ref.18

Sequence similarities

Contains 1 reticulon domain.

Sequence caution

The sequence AAH32192.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BC056373 differs from that shown. Reason: Erroneous termination at position 721. Translated as Glu.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from mutant phenotype PubMed 15034570. Source: MGI

axonal fasciculation

Inferred from mutant phenotype Ref.18. Source: UniProtKB

cardiac epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 19156209. Source: MGI

cerebral cortex radial glia guided migration

Inferred from mutant phenotype Ref.17. Source: UniProtKB

endoplasmic reticulum tubular network organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of axon extension

Inferred from mutant phenotype Ref.18. Source: UniProtKB

nervous system development

Inferred from direct assay PubMed 12225863. Source: MGI

regulation of branching morphogenesis of a nerve

Inferred from mutant phenotype Ref.18. Source: UniProtKB

regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of nervous system development

Inferred from mutant phenotype Ref.18. Source: UniProtKB

   Cellular_componentcell projection

Inferred from direct assay PubMed 15121177. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 12225863. Source: MGI

integral component of endoplasmic reticulum membrane

Inferred from sequence or structural similarity PubMed 10667797. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 15121177. Source: MGI

nuclear envelope

Inferred from sequence or structural similarity PubMed 11126360. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99P72-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99P72-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: Missing.
     117-169: LPPAAAVLPS...PKRRGSGSVD → MAPPLAGGGQ...RSSRLSAARN
Isoform 3 (identifier: Q99P72-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-963: Missing.
     964-974: AVLSAELNKTS → MDDQKKRWKDK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11621162Reticulon-4
PRO_0000168166

Regions

Topological domain1 – 988988Cytoplasmic Potential
Transmembrane989 – 100921Helical; Potential
Topological domain1010 – 107869Lumenal Potential
Transmembrane1079 – 109921Helical; Potential
Topological domain1100 – 116263Cytoplasmic Potential
Domain975 – 1162188Reticulon
Compositional bias31 – 5727Glu-rich
Compositional bias68 – 16093Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14
Modified residue71Phosphoserine By similarity
Modified residue161Phosphoserine Ref.16
Modified residue1051Phosphoserine Ref.16
Modified residue1451Phosphoserine Ref.11 Ref.15
Modified residue1651Phosphoserine By similarity
Modified residue3441Phosphoserine Ref.15
Modified residue4891Phosphoserine Ref.15
Modified residue6901Phosphoserine Ref.11
Modified residue10741N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 963963Missing in isoform 3.
VSP_018088
Alternative sequence1 – 116116Missing in isoform 2.
VSP_018089
Alternative sequence117 – 16953LPPAA…SGSVD → MAPPLAGGGQKGGAASEAWV PSLFVGVSGSTCTAAKSLVP IPARSSRLSAARN in isoform 2.
VSP_018090
Alternative sequence964 – 97411AVLSAELNKTS → MDDQKKRWKDK in isoform 3.
VSP_018091

Experimental info

Sequence conflict41I → V in BAD90301. Ref.4
Sequence conflict161S → R in BAD90301. Ref.4
Sequence conflict211P → L in BAD90301. Ref.4
Sequence conflict671A → V in AAM77068. Ref.3
Sequence conflict4131G → S in AAM77068. Ref.3
Sequence conflict4131G → S in BAD90301. Ref.4
Sequence conflict4291R → S in AAM77068. Ref.3
Sequence conflict4291R → S in BAD90301. Ref.4
Sequence conflict4481S → T in AAM77068. Ref.3
Sequence conflict4481S → T in BAD90301. Ref.4
Sequence conflict487 – 4904KTSP → HASA in AAH32192. Ref.6
Sequence conflict6511S → A in AAM77068. Ref.3
Sequence conflict6511S → A in AAH32192. Ref.6
Sequence conflict6511S → A in BAD90301. Ref.4
Sequence conflict6651A → V in BAD90301. Ref.4
Sequence conflict6921E → G in AAM77068. Ref.3
Sequence conflict6921E → G in BAC75974. Ref.7
Sequence conflict7331E → D in BAD90301. Ref.4
Sequence conflict7721V → L in BAD90301. Ref.4
Sequence conflict9161S → F in BAC75974. Ref.7
Sequence conflict9901V → VY in AAM77068. Ref.3

Secondary structure

................ 1162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 855697FBEE11781F

FASTA1,162126,613
        10         20         30         40         50         60 
MEDIDQSSLV SSSADSPPRP PPAFKYQFVT EPEDEEDEED EEEEEDDEDL EELEVLERKP 

        70         80         90        100        110        120 
AAGLSAAPVP PAAAPLLDFS SDSVPPAPRG PLPAAPPTAP ERQPSWERSP AASAPSLPPA 

       130        140        150        160        170        180 
AAVLPSKLPE DDEPPARPPA PAGASPLAEP AAPPSTPAAP KRRGSGSVDE TLFALPAASE 

       190        200        210        220        230        240 
PVIPSSAEKI MDLKEQPGNT VSSGQEDFPS VLFETAASLP SLSPLSTVSF KEHGYLGNLS 

       250        260        270        280        290        300 
AVASTEGTIE ETLNEASREL PERATNPFVN RESAEFSVLE YSEMGSSFNG SPKGESAMLV 

       310        320        330        340        350        360 
ENTKEEVIVR SKDKEDLVCS AALHNPQESP ATLTKVVKED GVMSPEKTMD IFNEMKMSVV 

       370        380        390        400        410        420 
APVREEYADF KPFEQAWEVK DTYEGSRDVL AARANMESKV DKKCFEDSLE QKGHGKDSES 

       430        440        450        460        470        480 
RNENASFPRT PELVKDGSRA YITCDSFSSA TESTAANIFP VLEDHTSENK TDEKKIEERK 

       490        500        510        520        530        540 
AQIITEKTSP KTSNPFLVAI HDSEADYVTT DNLSKVTEAV VATMPEGLTP DLVQEACESE 

       550        560        570        580        590        600 
LNEATGTKIA YETKVDLVQT SEAIQESIYP TAQLCPSFEE AEATPSPVLP DIVMEAPLNS 

       610        620        630        640        650        660 
LLPSTGASVA QPSASPLEVP SPVSYDGIKL EPENPPPYEE AMSVALKTSD SKEEIKEPES 

       670        680        690        700        710        720 
FNAAAQEAEA PYISIACDLI KETKLSTEPS PEFSNYSEIA KFEKSVPDHC ELVDDSSPES 

       730        740        750        760        770        780 
EPVDLFSDDS IPEVPQTQEE AVMLMKESLT EVSETVTQHK HKERLSASPQ EVGKPYLESF 

       790        800        810        820        830        840 
QPNLHITKDA ASNEIPTLTK KETISLQMEE FNTAIYSNDD LLSSKEDKMK ESETFSDSSP 

       850        860        870        880        890        900 
IEIIDEFPTF VSAKDDSPKE YTDLEVSNKS EIANVQSGAN SLPCSELPCD LSFKNTYPKD 

       910        920        930        940        950        960 
EAHVSDEFSK SRSSVSKVPL LLPNVSALES QIEMGNIVKP KVLTKEAEEK LPSDTEKEDR 

       970        980        990       1000       1010       1020 
SLTAVLSAEL NKTSVVDLLY WRDIKKTGVV FGASLFLLLS LTVFSIVSVT AYIALALLSV 

      1030       1040       1050       1060       1070       1080 
TISFRIYKGV IQAIQKSDEG HPFRAYLESE VAISEELVQK YSNSALGHVN STIKELRRLF 

      1090       1100       1110       1120       1130       1140 
LVDDLVDSLK FAVLMWVFTY VGALFNGLTL LILALISLFS IPVIYERHQA QIDHYLGLAN 

      1150       1160 
KSVKDAMAKI QAKIPGLKRK AE 

« Hide

Isoform 2 [UniParc].

Checksum: 8CE2E2238ED51222
Show »

FASTA1,046114,222
Isoform 3 [UniParc].

Checksum: 07BE5D580059ED9C
Show »

FASTA19922,466

References

« Hide 'large scale' references
[1]"Genomic structure and functional characterisation of the promoters of human and mouse nogo/rtn4."
Oertle T., Huber C., van der Putten H., Schwab M.E.
J. Mol. Biol. 325:299-323(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
Strain: 129/Sv.
[2]"Mouse vp20/RTN4C cDNA."
Coulson A.C., Craggs P.D., Morris N.J.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Adipocyte.
[3]"Cloning and expression of the mouse Nogo-A protein."
Jin W., Long M., Li R., Ju G.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
[4]"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."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"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] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain and Mammary gland.
[7]"The partial sequence of mouse nogo-A cDNA clone#4109."
Tozaki H., Hirata T.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 585-1162.
[8]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 975-982; 1061-1074 AND 1079-1090, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[9]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1133-1162.
Strain: C57BL/6J.
Tissue: Embryo.
[10]"Identification and characterization of a novel Nogo-interacting mitochondrial protein (NIMP)."
Hu W.-H., Hausmann O.N., Yan M.-S., Walters W.M., Wong P.K.Y., Bethea J.R.
J. Neurochem. 81:36-45(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTN4IP1.
[11]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[12]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[13]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
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.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[14]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-344 AND SER-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[17]"Nogo-a regulates neural precursor migration in the embryonic mouse cortex."
Mathis C., Schroeter A., Thallmair M., Schwab M.E.
Cereb. Cortex 20:2380-2390(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[18]"Neuronal Nogo-A regulates neurite fasciculation, branching and extension in the developing nervous system."
Petrinovic M.M., Duncan C.S., Bourikas D., Weinman O., Montani L., Schroeter A., Maerki D., Sommer L., Stoeckli E.T., Schwab M.E.
Development 137:2539-2550(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Nerve regrowth: nipped by a no-go - Issue 69 of April 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY102280 mRNA. Translation: AAM73502.1.
AY102284 mRNA. Translation: AAM73506.1.
AY102286 Genomic DNA. Translation: AAM73507.1.
AY102286 Genomic DNA. Translation: AAM73511.1.
AF326337 mRNA. Translation: AAK08076.1.
AY114152 mRNA. Translation: AAM77068.1.
AK220511 mRNA. Translation: BAD90301.1.
AL929371 Genomic DNA. Translation: CAI24273.1.
AL929371 Genomic DNA. Translation: CAI24274.1.
BC032192 mRNA. Translation: AAH32192.1. Different initiation.
BC056373 mRNA. No translation available.
AB073672 mRNA. Translation: BAC75974.1.
AK003859 mRNA. No translation available.
RefSeqNP_077188.1. NM_024226.4.
NP_918940.1. NM_194051.3.
NP_918943.1. NM_194054.3.
UniGeneMm.192580.
Mm.440639.
Mm.488364.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KO2NMR-A1025-1090[»]
ProteinModelPortalQ99P72.
SMRQ99P72. Positions 1025-1090.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212938. 6 interactions.
IntActQ99P72. 3 interactions.
MINTMINT-188330.
STRING10090.ENSMUSP00000099907.

PTM databases

PhosphoSiteQ99P72.

Proteomic databases

PaxDbQ99P72.
PRIDEQ99P72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060992; ENSMUSP00000053754; ENSMUSG00000020458. [Q99P72-1]
ENSMUST00000102841; ENSMUSP00000099905; ENSMUSG00000020458. [Q99P72-3]
ENSMUST00000102843; ENSMUSP00000099907; ENSMUSG00000020458. [Q99P72-2]
GeneID68585.
KEGGmmu:68585.
UCSCuc007ihk.2. mouse. [Q99P72-2]
uc007ihn.2. mouse. [Q99P72-3]

Organism-specific databases

CTD57142.
MGIMGI:1915835. Rtn4.
RougeSearch...

Phylogenomic databases

eggNOGNOG306139.
GeneTreeENSGT00390000009934.
HOVERGENHBG023134.
InParanoidQ99P72.
OMAHTSENKT.
OrthoDBEOG7CZK7J.
PhylomeDBQ99P72.
TreeFamTF105431.

Gene expression databases

ArrayExpressQ99P72.
BgeeQ99P72.
CleanExMM_RTN4.
GenevestigatorQ99P72.

Family and domain databases

InterProIPR003388. Reticulon.
[Graphical view]
PANTHERPTHR10994. PTHR10994. 1 hit.
PfamPF02453. Reticulon. 1 hit.
[Graphical view]
PROSITEPS50845. RETICULON. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRTN4. mouse.
EvolutionaryTraceQ99P72.
NextBio327502.
PROQ99P72.
SOURCESearch...

Entry information

Entry nameRTN4_MOUSE
AccessionPrimary (citable) accession number: Q99P72
Secondary accession number(s): Q5DTK9 expand/collapse secondary AC list , Q7TNB7, Q80W95, Q8BGK7, Q8BGM9, Q8K290, Q8K3G8, Q9CTE3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot