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P19527 (NFL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length542 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 By similarity. Interacts with TRIM2 By similarity.

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; contains three N-acetylglucosamine side chains. Ref.5

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 By similarity.

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 electronic annotation. Source: Ensembl

locomotion

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neurofilament cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

peripheral nervous system axon regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

protein polymerization

Inferred from direct assay PubMed 17157386. Source: RGD

regulation of axon diameter

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from expression pattern PubMed 17229084. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 18177991. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 17043767. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 18157692. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 18001836. Source: RGD

   Cellular_componentaxon

Inferred from direct assay PubMed 8737171. Source: RGD

growth cone

Inferred from direct assay PubMed 12226091. Source: RGD

neurofilament

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from direct assay PubMed 12226091. Source: RGD

   Molecular_functionphospholipase binding

Inferred from physical interaction PubMed 16819285. Source: RGD

protein domain specific binding

Inferred from physical interaction PubMed 16819285. Source: RGD

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 542541Neurofilament light polypeptide
PRO_0000063790

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 – 542145Tail
Region398 – 44447Tail, subdomain A
Region445 – 54298Tail, subdomain B (acidic)

Amino acid modifications

Modified residue21N-acetylserine Ref.4 Ref.6
Modified residue431Phosphotyrosine By similarity
Modified residue561Phosphoserine By similarity
Modified residue671Phosphoserine By similarity
Modified residue4731Phosphoserine By similarity
Modified residue5311Phosphoserine By similarity
Glycosylation211O-linked (GlcNAc) Ref.5
CAR_000128
Glycosylation271O-linked (GlcNAc) Ref.5
CAR_000129

Experimental info

Sequence conflict198 – 2036GADEAA → KARMSS in AAA41694. Ref.2
Sequence conflict4001R → K in AAA41694. Ref.2
Sequence conflict4771A → E in AAA41694. Ref.2
Sequence conflict481 – 4844EKEK → KKDE in AAA41694. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19527 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1FCC739AF23BCCA8

FASTA54261,335
        10         20         30         40         50         60 
MSSFSYEPYF 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 SSYLMSARAF PAYYTSHVQE EQSEVEETIE ATKAEEAKDE PPSEGEAEEE 

       490        500        510        520        530        540 
EKEKEEGEEE EGAEEEEAAK DESEDAKEEE GGEGEEEDTK ESEEEEKKEE SAGEEQAAKK 


KD 

« Hide

References

[1]"Expression of rat neurofilament proteins NF-L and NF-M in transfected non-neuronal cells."
Chin S.S., Liem R.K.H.
Eur. J. Cell Biol. 50:475-490(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of a cDNA encoding the smallest neurofilament protein from the rat."
Julien J.-P., Ramachandran K., Grosveld F.
Biochim. Biophys. Acta 825:398-404(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-484.
[3]"Characterization of the rat light neurofilament (NF-L) gene promoter and identification of NGF and cAMP responsive regions."
Reeben M., Neuman T., Palgi J., Palm K., Paalme V., Saarma M.
J. Neurosci. Res. 40:177-188(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[4]Lubec G., Pradeep J.J.P., Afjehi-Sadat L., Diao W., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14; 38-54; 56-84; 92-107; 117-126; 148-157; 165-172; 212-224; 273-282; 285-294; 368-379; 381-391; 393-422 AND 439-463, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[5]"Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M."
Dong D.L.-Y., Xu Z.-S., Chevrier M.R., Cotter R.J., Cleveland D.W., Hart G.W.
J. Biol. Chem. 268:16679-16687(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-21 AND SER-27.
[6]Lubec G., Chen W.-Q.
Submitted (FEB-2007) to UniProtKB
Cited for: ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031880 mRNA. Translation: AAB87069.1.
M25638 mRNA. Translation: AAA41694.1.
X53981 Genomic DNA. Translation: CAA37931.1.
PIRA21762.
I60434.
RefSeqNP_113971.1. NM_031783.1.
UniGeneRn.18568.

3D structure databases

ProteinModelPortalP19527.
SMRP19527. Positions 88-124, 324-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249778. 5 interactions.
DIPDIP-1N.
IntActP19527. 1 interaction.
STRING10116.ENSRNOP00000018599.

PTM databases

PhosphoSiteP19527.
UniCarbKBP19527.

2D gel databases

World-2DPAGE0004:P19527.

Proteomic databases

PaxDbP19527.
PRIDEP19527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018599; ENSRNOP00000018599; ENSRNOG00000013658.
GeneID83613.
KEGGrno:83613.
UCSCRGD:621458. rat.

Organism-specific databases

CTD4747.
RGD621458. Nefl.

Phylogenomic databases

eggNOGNOG145720.
GeneTreeENSGT00750000117235.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP19527.
KOK04572.
OMARSFPTYY.
OrthoDBEOG7FV3Q8.
PhylomeDBP19527.
TreeFamTF330122.

Gene expression databases

GenevestigatorP19527.

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

NextBio616157.
PROP19527.

Entry information

Entry nameNFL_RAT
AccessionPrimary (citable) accession number: P19527
Secondary accession number(s): Q63367
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 3 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