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P08551 (NFL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurofilament light polypeptide

Short name=NF-L
Alternative name(s):
68 kDa neurofilament protein
Neurofilament triplet L protein
Gene names
Name:Nefl
Synonyms:Nf68, Nfl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with ARHGEF28. Interacts with TRIM2. Ref.9 Ref.13

Domain

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.

Post-translational modification

O-glycosylated.

Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization By similarity. Ref.7

Ubiquitinated in the presence of TRIM2 and UBE2D1. Ref.13

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.

Sequence similarities

Belongs to the intermediate filament family.

Ontologies

Keywords
   Cellular componentIntermediate filament
   DomainCoiled coil
   PTMAcetylation
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processintermediate filament bundle assembly

Inferred from genetic interaction. Source: MGI

intermediate filament organization

Inferred from mutant phenotype PubMed 2121744PubMed 7946341. Source: MGI

locomotion

Inferred from mutant phenotype PubMed 15132161. Source: MGI

microtubule cytoskeleton organization

Inferred from mutant phenotype PubMed 11487626. Source: MGI

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 10884316PubMed 7946341. Source: MGI

neurofilament cytoskeleton organization

Inferred from mutant phenotype PubMed 11487626PubMed 14561875PubMed 15132161PubMed 16920084PubMed 9398473. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 15884021. Source: MGI

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 10884316. Source: MGI

peripheral nervous system axon regeneration

Inferred from mutant phenotype PubMed 9398473. Source: MGI

positive regulation of axonogenesis

Inferred from mutant phenotype PubMed 7946341. Source: MGI

protein polymerization

Inferred from electronic annotation. Source: Ensembl

regulation of axon diameter

Inferred from mutant phenotype PubMed 11343650PubMed 9398473. Source: MGI

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from direct assay PubMed 8110465PubMed 8821035. Source: MGI

growth cone

Inferred from electronic annotation. Source: Ensembl

intermediate filament

Inferred from direct assay. Source: MGI

neurofilament

Inferred from direct assay PubMed 10221457PubMed 15242779PubMed 8821035. Source: MGI

neuron projection

Inferred from direct assay PubMed 11834298PubMed 19646951. Source: MGI

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 543542Neurofilament light polypeptide
PRO_0000063788

Regions

Region2 – 9392Head
Region94 – 397304Rod
Region94 – 12532Coil 1A
Region126 – 13813Linker 1
Region139 – 23496Coil 1B
Region235 – 25319Linker 12
Region254 – 27219Coil 2A
Region273 – 2819Linker 2
Region282 – 397116Coil 2B
Region382 – 39211Epitope; recognized by IF-specific monoclonal antibody
Region398 – 543146Tail
Region398 – 44447Tail, subdomain A
Region445 – 54399Tail, subdomain B (acidic)

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue431Phosphotyrosine Ref.12
Modified residue561Phosphoserine Ref.7
Modified residue671Phosphoserine By similarity
Modified residue4731Phosphoserine Ref.10
Modified residue5321Phosphoserine Ref.10
Glycosylation211O-linked (GlcNAc) By similarity
Glycosylation271O-linked (GlcNAc) By similarity

Experimental info

Sequence conflict61Y → S in AAA39810. Ref.2
Sequence conflict91Y → I in AAA39810. Ref.2
Sequence conflict651M → K in AAA39810. Ref.2
Sequence conflict731L → V in AAA39810. Ref.2
Sequence conflict991D → H in AAA39810. Ref.2
Sequence conflict1951A → R in AAA39814. Ref.1
Sequence conflict2031Missing in AAA39814. Ref.1
Sequence conflict2401Y → I in AAA39810. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08551 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: BC40F8A8A536CFF5

FASTA54361,508
        10         20         30         40         50         60 
MSSFGYDPYF STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS 

        70         80         90        100        110        120 
SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR FASFIERVHE LEQQNKVLEA 

       130        140        150        160        170        180 
ELLVLRQKHS EPSRFRALYE QEIRDLRLAA EDATNEKQAL QGEREGLEET LRNLQARYEE 

       190        200        210        220        230        240 
EVLSREDAEG RLMEARKGAD EAALARAELE KRIDSLMDEI AFLKKVHEEE IAELQAQIQY 

       250        260        270        280        290        300 
AQISVEMDVS SKPDLSAALK DIRAQYEKLA AKNMQNAEEW FKSRFTVLTE SAAKNTDAVR 

       310        320        330        340        350        360 
AAKDEVSESR RLLKAKTLEI EACRGMNEAL EKQLQELEDK QNADISAMQD TINKLENELR 

       370        380        390        400        410        420 
STKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR LSFTSVGSIT SGYSQSSQVF 

       430        440        450        460        470        480 
GRSAYSGLQS SSYLMSARSF PAYYTSHVQE EQTEVEETIE ATKAEEAKDE PPSEGEAEEE 

       490        500        510        520        530        540 
EKEKEEGEEE EGAEEEEAAK DESEDTKEEE EGGEGEEEDT KESEEEEKKE ESAGEEQVAK 


KKD 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRQFMSL. A25227.
RefSeqNP_035040.1. NM_010910.1.
UniGeneMm.1956.

3D structure databases

ProteinModelPortalP08551.
SMRP08551. Positions 87-238, 253-322, 327-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201757. 7 interactions.
DIPDIP-31944N.
IntActP08551. 6 interactions.
MINTMINT-4116847.
STRING10090.ENSMUSP00000022639.

PTM databases

PhosphoSiteP08551.

2D gel databases

UCD-2DPAGEP08551.

Proteomic databases

PaxDbP08551.
PRIDEP08551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022639; ENSMUSP00000022639; ENSMUSG00000022055.
GeneID18039.
KEGGmmu:18039.
UCSCuc007uln.1. mouse.

Organism-specific databases

CTD4747.
MGIMGI:97313. Nefl.

Phylogenomic databases

eggNOGNOG145720.
GeneTreeENSGT00750000117235.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP08551.
KOK04572.
OMARSFPTYY.
OrthoDBEOG7FV3Q8.
PhylomeDBP08551.
TreeFamTF330122.

Gene expression databases

BgeeP08551.
CleanExMM_NEFL.
GenevestigatorP08551.

Family and domain databases

InterProIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF22. PTHR23239:SF22. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNEFL. mouse.
NextBio293145.
PROP08551.
SOURCESearch...

Entry information

Entry nameNFL_MOUSE
AccessionPrimary (citable) accession number: P08551
Secondary accession number(s): Q8K0Z0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 141 of the entry and version 5 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

MGD cross-references

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