Q99P72 (RTN4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Reticulon-4

Alternative name(s):
Neurite outgrowth inhibitor
Short name=Nogo protein

Gene names

Name:	Rtn4
Synonyms:	Kiaa0886, Nogo

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1162 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Neurogenesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis 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: Compara negative regulation of axon extension Inferred from mutant phenotype Ref.18. Source: UniProtKB regulation of branching morphogenesis of a nerve Inferred from mutant phenotype Ref.18. Source: UniProtKB regulation of cell migration Inferred from electronic annotation. Source: Compara
Cellular_component	cell projection Inferred from direct assay PubMed 15121177. Source: MGI integral to 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1162

1162

Reticulon-4

PRO_0000168166

Regions

Topological domain

1 – 988

988

Cytoplasmic Potential

Transmembrane

989 – 1009

21

Helical; Potential

Topological domain

1010 – 1078

69

Lumenal Potential

Transmembrane

1079 – 1099

21

Helical; Potential

Topological domain

1100 – 1162

63

Cytoplasmic Potential

Domain

975 – 1162

188

Reticulon

Compositional bias

31 – 57

27

Glu-rich

Compositional bias

68 – 160

93

Pro-rich

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

7

1

Phosphoserine By similarity

Modified residue

16

1

Phosphoserine Ref.13 Ref.16

Modified residue

105

1

Phosphoserine Ref.13 Ref.14 Ref.16

Modified residue

145

1

Phosphoserine Ref.11 Ref.12 Ref.15

Modified residue

165

1

Phosphoserine Ref.12 Ref.13

Modified residue

171

1

Phosphothreonine Ref.12

Modified residue

344

1

Phosphoserine Ref.15

Modified residue

426

1

Phosphoserine Ref.12

Modified residue

690

1

Phosphoserine Ref.11

Modified residue

836

1

Phosphoserine Ref.11

Modified residue

839

1

Phosphoserine Ref.11

Modified residue

857

1

Phosphoserine Ref.12

Modified residue

861

1

Phosphotyrosine Ref.12

Modified residue

1074

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

1 – 963

963

Missing in isoform 3.

VSP_018088

Alternative sequence

1 – 116

116

Missing in isoform 2.

VSP_018089

Alternative sequence

117 – 169

53

LPPAA…SGSVD → MAPPLAGGGQKGGAASEAWV PSLFVGVSGSTCTAAKSLVP IPARSSRLSAARN in isoform 2.

VSP_018090

Alternative sequence

964 – 974

11

AVLSAELNKTS → MDDQKKRWKDK in isoform 3.

VSP_018091

Experimental info

Sequence conflict

4

1

I → V in BAD90301. Ref.4

Sequence conflict

16

1

S → R in BAD90301. Ref.4

Sequence conflict

21

1

P → L in BAD90301. Ref.4

Sequence conflict

67

1

A → V in AAM77068. Ref.3

Sequence conflict

413

1

G → S in AAM77068. Ref.3

Sequence conflict

413

1

G → S in BAD90301. Ref.4

Sequence conflict

429

1

R → S in AAM77068. Ref.3

Sequence conflict

429

1

R → S in BAD90301. Ref.4

Sequence conflict

448

1

S → T in AAM77068. Ref.3

Sequence conflict

448

1

S → T in BAD90301. Ref.4

Sequence conflict

487 – 490

4

KTSP → HASA in AAH32192. Ref.6

Sequence conflict

651

1

S → A in AAM77068. Ref.3

Sequence conflict

651

1

S → A in AAH32192. Ref.6

Sequence conflict

651

1

S → A in BAD90301. Ref.4

Sequence conflict

665

1

A → V in BAD90301. Ref.4

Sequence conflict

692

1

E → G in AAM77068. Ref.3

Sequence conflict

692

1

E → G in BAC75974. Ref.7

Sequence conflict

733

1

E → D in BAD90301. Ref.4

Sequence conflict

772

1

V → L in BAD90301. Ref.4

Sequence conflict

916

1

S → F in BAC75974. Ref.7

Sequence conflict

990

1

V → VY in AAM77068. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1162

Helix Strand Turn

Details...

Helix

1026 – 1029

4

Helix

1031 – 1035

5

Turn

1037 – 1040

4

Helix

1044 – 1053

10

Helix

1057 – 1063

7

Turn

1065 – 1067

3

Helix

1068 – 1082

15

Helix

1087 – 1089

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 2, 2006. Version 2. Checksum: 855697FBEE11781F	FASTA	1,162	126,613
	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
	Isoform 2 [UniParc]. Checksum: 8CE2E2238ED51222	FASTA	1,046	114,222
	10 20 30 40 50 60 MAPPLAGGGQ KGGAASEAWV PSLFVGVSGS TCTAAKSLVP IPARSSRLSA ARNETLFALP 70 80 90 100 110 120 AASEPVIPSS AEKIMDLKEQ PGNTVSSGQE DFPSVLFETA ASLPSLSPLS TVSFKEHGYL 130 140 150 160 170 180 GNLSAVASTE GTIEETLNEA SRELPERATN PFVNRESAEF SVLEYSEMGS SFNGSPKGES 190 200 210 220 230 240 AMLVENTKEE VIVRSKDKED LVCSAALHNP QESPATLTKV VKEDGVMSPE KTMDIFNEMK 250 260 270 280 290 300 MSVVAPVREE YADFKPFEQA WEVKDTYEGS RDVLAARANM ESKVDKKCFE DSLEQKGHGK 310 320 330 340 350 360 DSESRNENAS FPRTPELVKD GSRAYITCDS FSSATESTAA NIFPVLEDHT SENKTDEKKI 370 380 390 400 410 420 EERKAQIITE KTSPKTSNPF LVAIHDSEAD YVTTDNLSKV TEAVVATMPE GLTPDLVQEA 430 440 450 460 470 480 CESELNEATG TKIAYETKVD LVQTSEAIQE SIYPTAQLCP SFEEAEATPS PVLPDIVMEA 490 500 510 520 530 540 PLNSLLPSTG ASVAQPSASP LEVPSPVSYD GIKLEPENPP PYEEAMSVAL KTSDSKEEIK 550 560 570 580 590 600 EPESFNAAAQ EAEAPYISIA CDLIKETKLS TEPSPEFSNY SEIAKFEKSV PDHCELVDDS 610 620 630 640 650 660 SPESEPVDLF SDDSIPEVPQ TQEEAVMLMK ESLTEVSETV TQHKHKERLS ASPQEVGKPY 670 680 690 700 710 720 LESFQPNLHI TKDAASNEIP TLTKKETISL QMEEFNTAIY SNDDLLSSKE DKMKESETFS 730 740 750 760 770 780 DSSPIEIIDE FPTFVSAKDD SPKEYTDLEV SNKSEIANVQ SGANSLPCSE LPCDLSFKNT 790 800 810 820 830 840 YPKDEAHVSD EFSKSRSSVS KVPLLLPNVS ALESQIEMGN IVKPKVLTKE AEEKLPSDTE 850 860 870 880 890 900 KEDRSLTAVL SAELNKTSVV DLLYWRDIKK TGVVFGASLF LLLSLTVFSI VSVTAYIALA 910 920 930 940 950 960 LLSVTISFRI YKGVIQAIQK SDEGHPFRAY LESEVAISEE LVQKYSNSAL GHVNSTIKEL 970 980 990 1000 1010 1020 RRLFLVDDLV DSLKFAVLMW VFTYVGALFN GLTLLILALI SLFSIPVIYE RHQAQIDHYL 1030 1040 GLANKSVKDA MAKIQAKIPG LKRKAE
	Isoform 3 [UniParc]. Checksum: 07BE5D580059ED9C	FASTA	199	22,466
	10 20 30 40 50 60 MDDQKKRWKD KVVDLLYWRD IKKTGVVFGA SLFLLLSLTV FSIVSVTAYI ALALLSVTIS 70 80 90 100 110 120 FRIYKGVIQA IQKSDEGHPF RAYLESEVAI SEELVQKYSN SALGHVNSTI KELRRLFLVD 130 140 150 160 170 180 DLVDSLKFAV LMWVFTYVGA LFNGLTLLIL ALISLFSIPV IYERHQAQID HYLGLANKSV 190 KDAMAKIQAK IPGLKRKAE

References

	« Hide 'large scale' referencesShow '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. , 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, 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. , 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; SER-690; SER-836 AND SER-839, MASS SPECTROMETRY. Tissue: Embryonic brain.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-165; THR-171; SER-426; SER-857 AND TYR-861, MASS SPECTROMETRY. Tissue: Brain cortex.
[13]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-105 AND SER-165, MASS SPECTROMETRY. Tissue: Liver.
[14]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, MASS SPECTROMETRY. Tissue: Melanoma.
[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 AND SER-344, MASS SPECTROMETRY. Tissue: Macrophage.
[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, MASS SPECTROMETRY. 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.

IPI

IPI00120415.
IPI00270767.
IPI00469392.

RefSeq

NP_077188.1. NM_024226.4.
NP_918940.1. NM_194051.3.
NP_918943.1. NM_194054.3.

UniGene

Mm.192580.
Mm.440639.
Mm.445271.
Mm.488364.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KO2	NMR	-	A	1025-1090	[»]

ProteinModelPortal

Q99P72.

SMR

Q99P72. Positions 1025-1090.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99P72. 1 interaction.

MINT

MINT-188330.

STRING

10090.ENSMUSP00000099907.

PTM databases

PhosphoSite

Q99P72.

Proteomic databases

PaxDb

Q99P72.

PRIDE

Q99P72.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENSMUST00000060992; ENSMUSP00000053754; ENSMUSG00000020458.
ENSMUST00000102841; ENSMUSP00000099905; ENSMUSG00000020458.
ENSMUST00000102843; ENSMUSP00000099907; ENSMUSG00000020458.

GeneID

68585.

KEGG

mmu:68585.

UCSC

uc007ihk.2. mouse.
uc007ihn.2. mouse.

Organism-specific databases

CTD

57142.

MGI

MGI:1915835. Rtn4.

Rouge

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Phylogenomic databases

eggNOG

NOG306139.

GeneTree

ENSGT00390000009934.

HOVERGEN

HBG023134.

InParanoid

Q99P72.

OMA

HTSENKT.

OrthoDB

EOG4XH010.

Gene expression databases

ArrayExpress

Q99P72.

Bgee

Q99P72.

CleanEx

MM_RTN4.

Genevestigator

Q99P72.

GermOnline

ENSMUSG00000020458. Mus musculus.

Family and domain databases

InterPro

IPR003388. Reticulon.
[Graphical view]

PANTHER

PTHR10994. PTHR10994. 1 hit.

Pfam

PF02453. Reticulon. 1 hit.
[Graphical view]

PROSITE

PS50845. RETICULON. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

RTN4. mouse.

EvolutionaryTrace

Q99P72.

NextBio

327502.

SOURCE

Search...

Entry information

Entry name

RTN4_MOUSE

Accession

Primary (citable) accession number: Q99P72
Secondary accession number(s): Q5DTK9 , 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 3, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program