Primary Information |
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| BoMiProt ID | Bomi7440 |
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| Protein Name | Neurofilament light polypeptide/68 kDa neurofilament protein/Micro glutamic acid-rich protein/Neurofilament triplet L protein |
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| Organism | Bos taurus |
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| Uniprot ID | P02548 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776546.1 |
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| Aminoacid Length | 555 |
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| Molecular Weight | 62646 |
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| FASTA Sequence |
Download |
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| Gene Name | NEFL |
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| Gene ID | 281348 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | a component of neurofilament,intermediate filament assembly. |
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| Biochemical Properties | it is a three-domain structure that includes an N-terminal ‘head’ domain, a C-terminal ‘tail’ domain, and a central α-helical ‘rod’ domain.Three linker domains (L1, L12, and L2) are interspersed between distinct rod domain sub-helices (coil-1A, coil-1B, coil-2A, and coil-2B).NF-L tail is also short and contains many glutamic acid residues (an “E segment”).It can form 10-nm homopolymeric filaments in vitro and heteropolymers with other NF subunits.There are two major types of KSP repeats in the NF tail domain, KSPXK and KSPXXXP, in which X represents any amino acid.Most of this phosphorylation occurs at the KSP motif and the related smaller serine/threonine KSP repeats that vary in number across mammalian species. |
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| PTMs | Acetylation, Glycoprotein, Methylation, Phosphoprotein, Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P02548|NFL_BOVIN Neurofilament light polypeptide OS=Bos taurus OX=9913 GN=NEFL PE=1 SV=3
MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSY*43SAPVSSSLSVRRS*56YSSS
SGSLMPS*67LESLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFAS*103FIERVHELEQQNKVLEA
ELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEE
EVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQY
AQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVR
AAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELR
TTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYTQSSQVF
GRSAYGGLQTSSYLMSARSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPS*473EGEAEEE
EKEKEEAEAEAEAEAEAEAEEEEGAQEEEAAKEDAEEAKEEEGGEGEEAEET*532KEAEEEEK
KDEGAGEEQATKKKD
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Both PKA and PKC are able to phosphorylate NF-L at serine 55 and serine 23 and and a proline-directed threonine (Thr21) is phosphorylated by cyclin-dependent kinase 5 (cdk5),Erk1 and Erk2.Serine residues 12, 27, 33, and 51 on NF-L phosphorylated by PKC promote disassembly.NF-L glycosylation occurs on Thr21 and Ser27 in the head domain which alters the interactions of NFs with protein ligands, including protein 14-3-3.NF head domain and tail-domain regulation is highly compartmentalized,such that tail-domain phosphorylation via several kinases predominates in axons, whereas head-domain phosphorylation occurs within neuronal cell bodies |
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| Additional Comments | NEFL mutation is a cause of axonal or demyelinating forms of dominant Charcot-Marie-Tooth disease (CMT). |
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| Bibliography | 1.Snider, N. T., & Omary, M. B. (2014). Post-translational modifications of intermediate filament proteins: mechanisms and functions. Nature reviews. Molecular cell biology, 15(3), 163–177. https://doi.org/10.1038/nrm3753 2.Yuan, A., Rao, M. V., Veeranna, & Nixon, R. A. (2017). Neurofilaments and Neurofilament Proteins in Health and Disease. Cold Spring Harbor perspectives in biology, 9(4), a018309. https://doi.org/10.1101/cshperspect.a018309 |
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