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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 axonal transport Source: MGI
  • axonal 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 axonal transport Source: MGI
  • spinal cord development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-MMU-442729. CREB phosphorylation through the activation of CaMKII.
R-MMU-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-MMU-5673001. RAF/MAP kinase cascade.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:97313. Nefl.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • axon cytoplasm Source: GOC
  • 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000637882 – 543Neurofilament light polypeptideAdd BLAST542

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Glycosylationi21O-linked (GlcNAc)By similarity1
Modified residuei23Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei23Omega-N-methylarginine; alternateCombined sources1
Glycosylationi27O-linked (GlcNAc)By similarity1
Modified residuei30Omega-N-methylarginineCombined sources1
Modified residuei43PhosphotyrosineCombined sources1
Modified residuei56Phosphoserine1 Publication1
Modified residuei67PhosphoserineBy similarity1
Modified residuei103PhosphoserineBy similarity1
Modified residuei473PhosphoserineCombined sources1
Modified residuei503PhosphoserineBy similarity1
Modified residuei520PhosphothreonineBy similarity1
Modified residuei523PhosphoserineBy similarity1
Modified residuei532PhosphoserineCombined sources1

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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP08551.
MaxQBiP08551.
PaxDbiP08551.
PeptideAtlasiP08551.
PRIDEiP08551.

2D gel databases

UCD-2DPAGEP08551.

PTM databases

iPTMnetiP08551.
PhosphoSitePlusiP08551.
SwissPalmiP08551.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022055.
CleanExiMM_NEFL.
GenevisibleiP08551. MM.

Interactioni

Subunit structurei

Interacts with ARHGEF28. Interacts with TRIM2.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201757. 8 interactors.
DIPiDIP-31944N.
IntActiP08551. 7 interactors.
MINTiMINT-4116847.
STRINGi10090.ENSMUSP00000022639.

Structurei

3D structure databases

ProteinModelPortaliP08551.
SMRiP08551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 93HeadAdd BLAST92
Regioni94 – 397RodAdd BLAST304
Regioni94 – 125Coil 1AAdd BLAST32
Regioni126 – 138Linker 1Add BLAST13
Regioni139 – 234Coil 1BAdd BLAST96
Regioni235 – 253Linker 12Add BLAST19
Regioni254 – 272Coil 2AAdd BLAST19
Regioni273 – 281Linker 29
Regioni282 – 397Coil 2BAdd BLAST116
Regioni382 – 392Epitope; recognized by IF-specific monoclonal antibodyAdd BLAST11
Regioni398 – 543TailAdd BLAST146
Regioni398 – 444Tail, subdomain AAdd BLAST47
Regioni445 – 543Tail, subdomain B (acidic)Add BLAST99

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

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP08551.
KOiK04572.
OMAiRSFPTYY.
OrthoDBiEOG091G12MK.
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]
SMARTiSM01391. Filament. 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)DescriptionActionsGraphical viewLength
Sequence conflicti6Y → S in AAA39810 (PubMed:3785173).Curated1
Sequence conflicti9Y → I in AAA39810 (PubMed:3785173).Curated1
Sequence conflicti65M → K in AAA39810 (PubMed:3785173).Curated1
Sequence conflicti73L → V in AAA39810 (PubMed:3785173).Curated1
Sequence conflicti99D → H in AAA39810 (PubMed:3785173).Curated1
Sequence conflicti195A → R in AAA39814 (PubMed:3103856).Curated1
Sequence conflicti203Missing in AAA39814 (PubMed:3103856).Curated1
Sequence conflicti240Y → I in AAA39810 (PubMed:3785173).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201757. 8 interactors.
DIPiDIP-31944N.
IntActiP08551. 7 interactors.
MINTiMINT-4116847.
STRINGi10090.ENSMUSP00000022639.

PTM databases

iPTMnetiP08551.
PhosphoSitePlusiP08551.
SwissPalmiP08551.

2D gel databases

UCD-2DPAGEP08551.

Proteomic databases

EPDiP08551.
MaxQBiP08551.
PaxDbiP08551.
PeptideAtlasiP08551.
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

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP08551.
KOiK04572.
OMAiRSFPTYY.
OrthoDBiEOG091G12MK.
PhylomeDBiP08551.
TreeFamiTF330122.

Enzyme and pathway databases

ReactomeiR-MMU-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-MMU-442729. CREB phosphorylation through the activation of CaMKII.
R-MMU-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-MMU-5673001. RAF/MAP kinase cascade.

Miscellaneous databases

ChiTaRSiNefl. mouse.
PROiP08551.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022055.
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]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 165 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

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 one 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.