General information | DisProt: | DP00524 | Name: | Reticulon-4 [Isoform 2 (RTN 4B)(ASY)(Nogo-B)(RTN-xS)(Foocen-M)] | Synonym(s): | RTN4_HUMAN
Nogo-B
Neurite outgrowth inhibitor
Nogo protein
Foocen
Neuroendocrine-specific protein
NSP
Neuroendocrine-specific protein C homolog
RTN-x
Reticulon-5
| First appeared in release: | Release 3.6 (06/29/2007) | UniProt: | Q9NQC3-2 | UniGene: | Hs.704007 | SwissProt: | RTN4_HUMAN | TrEMBL: | | NCBI (GI): | 17369290 | Source organism: | Homo sapiens (Human) | Sequence length: | 373 | Percent disordered: | 62% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MEDLDQSPLV SSSDSPPRPQ PAFKYQFVRE PEDEEEEEEE EEEDEDEDLE ELEVLERKPA - 60 AGLSAAPVPT APAAGAPLMD FGNDFVPPAP RGPLPAAPPV APERQPSWDP SPVSSTVPAP - 120 SPLSAAAVSP SKLPEDDEPP ARPPPPPPAS VSPQAEPVWT PPAPAPAAPP STPAAPKRRG - 180 SSGSVVVDLL YWRDIKKTGV VFGASLFLLL SLTVFSIVSV TAYIALALLS VTISFRIYKG - 240 VIQAIQKSDE GHPFRAYLES EVAISEELVQ KYSNSALGHV NCTIKELRRL FLVDDLVDSL - 300 KFAVLMWVFT YVGALFNGLT LLILALISLF SVPVIYERHQ AQIDHYLGLA NKNVKDAMAK - 360 IQAKIPGLKR KAE
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Functional narrative |
Nogo-B is one of three different isoforms (others including Nogo-A and -C) that are all generated from the gene RTN4, which is located on human chromosome 2, location p14-p13, by means of either alternative promoter usage and/or splicing. The N-terminus of Nogo-B is almost completely homologous to the first 200 residues of Nogo-A and has been determined to play a part in many integral biological processes, including interaction with beta-amyloid converting enzyme (BACE1), regulation of vascular remodeling, and induction of apoptosis. It is also believed that Nogo-B plays a role as a positive regulator of EC functions and as a negative regulator of SMC migration. The importance of Nogo molecules in general being intrinsically unstructured appears to serve two functional purposes for the organism, including generating/maintaining structures associated with the membrane as well as playing a role in such cellular signaling processes which are utilized in apoptosis, CNS neuronal regeneration, vascular remodeling, etc. The majority of the RTN4/Nogo molecules are concentrated in the ER with small amounts found on the cell surface. This protein is a potent neurite growth inhibitor in vitro and plays a role both in the restriction of axonal regeneration after injury and in structural plasticity in the CNS. Isoform 2 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 inhibit BACE1 activity and amyloid precursor protein processing.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | N-terminus | Location: | 1 - 200 | Length: | 200 | Region sequence: |
MEDLDQSPLVSSSDSPPRPQPAFKYQFVREPEDEEEEEEEEEEDEDEDLEELEVLERKPA AGLSAAPVPTAPAAGAPLMDFGNDFVPPAPRGPLPAAPPVAPERQPSWDPSPVSSTVPAP SPLSAAAVSPSKLPEDDEPPARPPPPPPASVSPQAEPVWTPPAPAPAAPPSTPAAPKRRG SSGSVVVDLLYWRDIKKTGV | Modification type: | Fragment
| PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | | Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 6.8; phosphate buffer (buffer) 20 mM; protein 50 uM)
- Circular dichroism (CD) spectroscopy, near-UV (293 K; pH: 6.8; phosphate buffer (buffer) 20 mM; protein 100 uM)
- Nuclear magnetic resonance (NMR) (pH: 6.8; D2O (deuterium lock signal) 10 %; lyophilized proteins; phosphate buffer (buffer) 20 mM)
| References:
- Li M, Song J. "The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications." Proteins. 2007; 68(1): 100-8. PubMed: 17397058
| Comments:
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Region 2 | Type: | Disordered | Name: | C-terminus | Location: | 336 - 368 | Length: | 33 | Region sequence: |
YERHQAQIDHYLGLANKNVKDAMAKIQAKIPGL | Modification type: | Fragment
| PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | | Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 6.8; phosphate buffer (buffer) 20 mM; protein 50 uM)
- Circular dichroism (CD) spectroscopy, near-UV (293 K; pH: 6.8; phosphate buffer (buffer) 20 mM; protein 100 uM)
- Nuclear magnetic resonance (NMR) (pH: 6.8; D2O (deuterium lock signal) 10 %; lyophilized proteins; phosphate buffer (buffer) 20 mM)
| References:
- Li M, Song J. "The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications." Proteins. 2007; 68(1): 100-8. PubMed: 17397058
| Comments:
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References |
- Li M, Song J. "Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain." Biochem Biophys Res Commun. 2007; 360(1): 128-34. PubMed: 17585875
- Rodriguez-Feo JA, Hellings WE, Verhoeven BA, Moll FL, de Kleijn DP, Prendergast J, Gao Y, van der Graaf Y, Tellides G, Sessa WC, Pasterkamp G. "Low levels of Nogo-B in human carotid atherosclerotic plaques are associated with an atheromatous phenotype, restenosis, and stenosis severity." Arterioscler Thromb Vasc Biol. 2007; 27(6): 1354-60. PubMed: 17413036
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Comments |
In addition to biophysical characterization, bioinformatic analysis for Nogo-A and -B was carried out using the following neural network-based programs: PSIPRES, GlobPlot, IUPred, VSL2B, and ELM while the secondary structures were predicted using PSIPRED. The Nogo-A and -B sequences were assessed for globularity and disordered regions using GlobPlot, IUPred, and VSL2B and for the functional sites in eukaryotic proteins, ELM was utilized for prediction.
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