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Protein

Neurofilament light polypeptide

Gene

Nefl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber.

GO - Molecular functioni

  • identical protein binding Source: MGI
  • protein binding, bridging Source: BHF-UCL
  • protein C-terminus binding Source: MGI
  • structural constituent of cytoskeleton Source: BHF-UCL

GO - Biological processi

  • anterograde axon cargo transport Source: MGI
  • axon transport of mitochondrion Source: MGI
  • cerebral cortex development Source: Ensembl
  • hippocampus development Source: Ensembl
  • intermediate filament bundle assembly Source: BHF-UCL
  • intermediate filament organization Source: MGI
  • intermediate filament polymerization or depolymerization Source: Ensembl
  • locomotion Source: MGI
  • microtubule cytoskeleton organization Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • neurofilament bundle assembly Source: MGI
  • neurofilament cytoskeleton organization Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • neuron projection morphogenesis Source: MGI
  • peripheral nervous system axon regeneration Source: MGI
  • positive regulation of axonogenesis Source: MGI
  • protein polymerization Source: Ensembl
  • regulation of axon diameter Source: MGI
  • response to acrylamide Source: Ensembl
  • response to corticosterone Source: Ensembl
  • response to peptide hormone Source: Ensembl
  • response to sodium arsenite Source: Ensembl
  • response to toxic substance Source: Ensembl
  • retrograde axon cargo transport Source: MGI
  • spinal cord development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_331187. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_331823. Ras activation uopn Ca2+ infux through NMDA receptor.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurofilament light polypeptide
Short name:
NF-L
Alternative name(s):
68 kDa neurofilament protein
Neurofilament triplet L protein
Gene namesi
Name:Nefl
Synonyms:Nf68, Nfl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:97313. Nefl.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • cytoplasm Source: BHF-UCL
  • growth cone Source: Ensembl
  • intermediate filament Source: BHF-UCL
  • myelin sheath Source: UniProtKB
  • neurofilament Source: MGI
  • neuron projection Source: MGI
  • TSC1-TSC2 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 543542Neurofilament light polypeptidePRO_0000063788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Glycosylationi21 – 211O-linked (GlcNAc)By similarity
Glycosylationi27 – 271O-linked (GlcNAc)By similarity
Modified residuei43 – 431Phosphotyrosine1 Publication
Modified residuei56 – 561Phosphoserine1 Publication
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei532 – 5321Phosphoserine1 Publication

Post-translational modificationi

O-glycosylated.1 Publication
Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization.By similarity
Ubiquitinated in the presence of TRIM2 and UBE2D1.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP08551.
PaxDbiP08551.
PRIDEiP08551.

2D gel databases

UCD-2DPAGEP08551.

PTM databases

PhosphoSiteiP08551.

Expressioni

Gene expression databases

BgeeiP08551.
CleanExiMM_NEFL.
GenevisibleiP08551. MM.

Interactioni

Subunit structurei

Interacts with ARHGEF28. Interacts with TRIM2.2 Publications

Protein-protein interaction databases

BioGridi201757. 8 interactions.
DIPiDIP-31944N.
IntActiP08551. 6 interactions.
MINTiMINT-4116847.
STRINGi10090.ENSMUSP00000022639.

Structurei

3D structure databases

ProteinModelPortaliP08551.
SMRiP08551. Positions 87-238, 253-322, 327-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9392HeadAdd
BLAST
Regioni94 – 397304RodAdd
BLAST
Regioni94 – 12532Coil 1AAdd
BLAST
Regioni126 – 13813Linker 1Add
BLAST
Regioni139 – 23496Coil 1BAdd
BLAST
Regioni235 – 25319Linker 12Add
BLAST
Regioni254 – 27219Coil 2AAdd
BLAST
Regioni273 – 2819Linker 2
Regioni282 – 397116Coil 2BAdd
BLAST
Regioni382 – 39211Epitope; recognized by IF-specific monoclonal antibodyAdd
BLAST
Regioni398 – 543146TailAdd
BLAST
Regioni398 – 44447Tail, subdomain AAdd
BLAST
Regioni445 – 54399Tail, subdomain B (acidic)Add
BLAST

Domaini

The extra mass and high charge density that distinguish the neurofilament proteins from all other intermediate filament proteins are due to the tailpiece extensions. This region may form a charged scaffolding structure suitable for interaction with other neuronal components or ions.

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG145720.
GeneTreeiENSGT00760000118905.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP08551.
KOiK04572.
OMAiRSFPTYY.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP08551.
TreeFamiTF330122.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF22. PTHR23239:SF22. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFGYDPYF STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS
60 70 80 90 100
LSVRRSYSSS SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR
110 120 130 140 150
FASFIERVHE LEQQNKVLEA ELLVLRQKHS EPSRFRALYE QEIRDLRLAA
160 170 180 190 200
EDATNEKQAL QGEREGLEET LRNLQARYEE EVLSREDAEG RLMEARKGAD
210 220 230 240 250
EAALARAELE KRIDSLMDEI AFLKKVHEEE IAELQAQIQY AQISVEMDVS
260 270 280 290 300
SKPDLSAALK DIRAQYEKLA AKNMQNAEEW FKSRFTVLTE SAAKNTDAVR
310 320 330 340 350
AAKDEVSESR RLLKAKTLEI EACRGMNEAL EKQLQELEDK QNADISAMQD
360 370 380 390 400
TINKLENELR STKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR
410 420 430 440 450
LSFTSVGSIT SGYSQSSQVF GRSAYSGLQS SSYLMSARSF PAYYTSHVQE
460 470 480 490 500
EQTEVEETIE ATKAEEAKDE PPSEGEAEEE EKEKEEGEEE EGAEEEEAAK
510 520 530 540
DESEDTKEEE EGGEGEEEDT KESEEEEKKE ESAGEEQVAK KKD
Length:543
Mass (Da):61,508
Last modified:January 23, 2007 - v5
Checksum:iBC40F8A8A536CFF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Y → S in AAA39810 (PubMed:3785173).Curated
Sequence conflicti9 – 91Y → I in AAA39810 (PubMed:3785173).Curated
Sequence conflicti65 – 651M → K in AAA39810 (PubMed:3785173).Curated
Sequence conflicti73 – 731L → V in AAA39810 (PubMed:3785173).Curated
Sequence conflicti99 – 991D → H in AAA39810 (PubMed:3785173).Curated
Sequence conflicti195 – 1951A → R in AAA39814 (PubMed:3103856).Curated
Sequence conflicti203 – 2031Missing in AAA39814 (PubMed:3103856).Curated
Sequence conflicti240 – 2401Y → I in AAA39810 (PubMed:3785173).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20480 mRNA. Translation: AAA39814.1.
M13016 Genomic DNA. Translation: AAA39810.1.
DQ201635 mRNA. Translation: ABA46748.1.
BC029203 mRNA. Translation: AAH29203.1.
AH002053 Genomic DNA. Translation: AAA39812.1.
X02165 mRNA. Translation: CAB51616.1.
CCDSiCCDS27232.1.
PIRiA25227. QFMSL.
RefSeqiNP_035040.1. NM_010910.1.
UniGeneiMm.1956.

Genome annotation databases

EnsembliENSMUST00000022639; ENSMUSP00000022639; ENSMUSG00000022055.
GeneIDi18039.
KEGGimmu:18039.
UCSCiuc007uln.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20480 mRNA. Translation: AAA39814.1.
M13016 Genomic DNA. Translation: AAA39810.1.
DQ201635 mRNA. Translation: ABA46748.1.
BC029203 mRNA. Translation: AAH29203.1.
AH002053 Genomic DNA. Translation: AAA39812.1.
X02165 mRNA. Translation: CAB51616.1.
CCDSiCCDS27232.1.
PIRiA25227. QFMSL.
RefSeqiNP_035040.1. NM_010910.1.
UniGeneiMm.1956.

3D structure databases

ProteinModelPortaliP08551.
SMRiP08551. Positions 87-238, 253-322, 327-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201757. 8 interactions.
DIPiDIP-31944N.
IntActiP08551. 6 interactions.
MINTiMINT-4116847.
STRINGi10090.ENSMUSP00000022639.

PTM databases

PhosphoSiteiP08551.

2D gel databases

UCD-2DPAGEP08551.

Proteomic databases

MaxQBiP08551.
PaxDbiP08551.
PRIDEiP08551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022639; ENSMUSP00000022639; ENSMUSG00000022055.
GeneIDi18039.
KEGGimmu:18039.
UCSCiuc007uln.1. mouse.

Organism-specific databases

CTDi4747.
MGIiMGI:97313. Nefl.

Phylogenomic databases

eggNOGiNOG145720.
GeneTreeiENSGT00760000118905.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP08551.
KOiK04572.
OMAiRSFPTYY.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP08551.
TreeFamiTF330122.

Enzyme and pathway databases

ReactomeiREACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_331187. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_331823. Ras activation uopn Ca2+ infux through NMDA receptor.

Miscellaneous databases

ChiTaRSiNefl. mouse.
NextBioi293145.
PROiP08551.
SOURCEiSearch...

Gene expression databases

BgeeiP08551.
CleanExiMM_NEFL.
GenevisibleiP08551. MM.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF22. PTHR23239:SF22. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and developmental expression of the murine neurofilament gene family."
    Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F.
    Brain Res. 387:243-250(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Anomalous placement of introns in a member of the intermediate filament multigene family: an evolutionary conundrum."
    Lewis S.A., Cowan N.J.
    Mol. Cell. Biol. 6:1529-1534(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  3. Jensen K.H., Brown A.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cerebellum.
  4. "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].
    Tissue: Eye.
  5. "Structure of the 68-kDa neurofilament gene and regulation of its expression."
    Nakahira K., Ikenaka K., Wada K., Tamura T.A., Furuichi T., Mikoshiba K.
    J. Biol. Chem. 265:19786-19791(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  6. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 38-54; 117-126 AND 381-391, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  7. "Identification of Ser-55 as a major protein kinase A phosphorylation site on the 70-kDa subunit of neurofilaments. Early turnover during axonal transport."
    Sihag R.K., Nixon R.A.
    J. Biol. Chem. 266:18861-18867(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 52-57, PHOSPHORYLATION AT SER-56.
  8. "Genetics, evolution, and expression of the 68,000-mol-wt neurofilament protein: isolation of a cloned cDNA probe."
    Lewis S.A., Cowan N.J.
    J. Cell Biol. 100:843-850(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 242-543.
    Tissue: Brain.
  9. "RNA-binding protein is involved in aggregation of light neurofilament protein and is implicated in the pathogenesis of motor neuron degeneration."
    Lin H., Zhai J., Schlaepfer W.W.
    Hum. Mol. Genet. 14:3643-3659(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF28.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-532, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  11. "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
    Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  12. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  13. "Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament light chain and neurodegeneration."
    Balastik M., Ferraguti F., Pires-da Silva A., Lee T.H., Alvarez-Bolado G., Lu K.P., Gruss P.
    Proc. Natl. Acad. Sci. U.S.A. 105:12016-12021(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM2, UBIQUITINATION.

Entry informationi

Entry nameiNFL_MOUSE
AccessioniPrimary (citable) accession number: P08551
Secondary accession number(s): Q8K0Z0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 153 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

NF-L is the most abundant of the three neurofilament proteins and, like the other nonepithelial intermediate filament proteins, it can form homopolymeric 10-nm filaments.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.