Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neurofilament light polypeptide

Gene

Nefl

Organism
Rattus norvegicus (Rat)
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.

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.

GO - Molecular functioni

  • identical protein binding Source: Ensembl
  • phospholipase binding Source: RGD
  • protein binding, bridging Source: Ensembl
  • protein C-terminus binding Source: Ensembl
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • structural constituent of cytoskeleton Source: Ensembl

GO - Biological processi

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

Enzyme and pathway databases

ReactomeiR-RNO-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-RNO-442729. CREB phosphorylation through the activation of CaMKII.
R-RNO-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi621458. Nefl.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • axon cytoplasm Source: GOC
  • growth cone Source: RGD
  • myelin sheath Source: Ensembl
  • neurofilament Source: RGD
  • neuron projection Source: RGD
  • TSC1-TSC2 complex Source: Ensembl

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000637902 – 542Neurofilament light polypeptideAdd BLAST541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine2 Publications1
GlycosylationiCAR_00012821O-linked (GlcNAc) threonine1 Publication1
Modified residuei23Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei23Omega-N-methylarginine; alternateBy similarity1
GlycosylationiCAR_00012927O-linked (GlcNAc) serine1 Publication1
Modified residuei30Omega-N-methylarginineBy similarity1
Modified residuei43PhosphotyrosineBy similarity1
Modified residuei56PhosphoserineBy similarity1
Modified residuei67PhosphoserineCombined sources1
Modified residuei103PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei473PhosphoserineCombined sources1
Modified residuei503PhosphoserineCombined sources1
Modified residuei519PhosphothreonineCombined sources1
Modified residuei522PhosphoserineCombined sources1
Modified residuei531PhosphoserineCombined sources1

Post-translational modificationi

O-glycosylated; contains three N-acetylglucosamine side chains.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.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP19527.
PRIDEiP19527.

2D gel databases

World-2DPAGEi0004:P19527.

PTM databases

iPTMnetiP19527.
PhosphoSitePlusiP19527.
UniCarbKBiP19527.

Expressioni

Gene expression databases

BgeeiENSRNOG00000013658.
GenevisibleiP19527. RN.

Interactioni

Subunit structurei

Interacts with ARHGEF28. Interacts with TRIM2.By similarity

GO - Molecular functioni

  • identical protein binding Source: Ensembl
  • phospholipase binding Source: RGD
  • protein binding, bridging Source: Ensembl
  • protein C-terminus binding Source: Ensembl
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi249778. 5 interactors.
DIPiDIP-1N.
IntActiP19527. 1 interactor.
STRINGi10116.ENSRNOP00000018599.

Structurei

3D structure databases

ProteinModelPortaliP19527.
SMRiP19527.
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 – 542TailAdd BLAST145
Regioni398 – 444Tail, subdomain AAdd BLAST47
Regioni445 – 542Tail, subdomain B (acidic)Add BLAST98

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.
InParanoidiP19527.
KOiK04572.
OMAiEMDVSSK.
OrthoDBiEOG091G12MK.
PhylomeDBiP19527.
TreeFamiTF330122.

Family and domain databases

InterProiView protein in InterPro
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF242. PTHR23239:SF242. 1 hit.
PfamiView protein in Pfam
PF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
SMARTiView protein in SMART
SM01391. Filament. 1 hit.
PROSITEiView protein in PROSITE
PS00226. IF. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P19527-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFSYEPYF 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 SSYLMSARAF PAYYTSHVQE
460 470 480 490 500
EQSEVEETIE ATKAEEAKDE PPSEGEAEEE EKEKEEGEEE EGAEEEEAAK
510 520 530 540
DESEDAKEEE GGEGEEEDTK ESEEEEKKEE SAGEEQAAKK KD
Length:542
Mass (Da):61,335
Last modified:January 23, 2007 - v3
Checksum:i1FCC739AF23BCCA8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti198 – 203GADEAA → KARMSS in AAA41694 (PubMed:3925999).Curated6
Sequence conflicti400R → K in AAA41694 (PubMed:3925999).Curated1
Sequence conflicti477A → E in AAA41694 (PubMed:3925999).Curated1
Sequence conflicti481 – 484EKEK → KKDE in AAA41694 (PubMed:3925999).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031880 mRNA. Translation: AAB87069.1.
M25638 mRNA. Translation: AAA41694.1.
X53981 Genomic DNA. Translation: CAA37931.1.
PIRiA21762.
I60434.
RefSeqiNP_113971.1. NM_031783.1.
UniGeneiRn.18568.

Genome annotation databases

EnsembliENSRNOT00000018599; ENSRNOP00000018599; ENSRNOG00000013658.
GeneIDi83613.
KEGGirno:83613.
UCSCiRGD:621458. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031880 mRNA. Translation: AAB87069.1.
M25638 mRNA. Translation: AAA41694.1.
X53981 Genomic DNA. Translation: CAA37931.1.
PIRiA21762.
I60434.
RefSeqiNP_113971.1. NM_031783.1.
UniGeneiRn.18568.

3D structure databases

ProteinModelPortaliP19527.
SMRiP19527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249778. 5 interactors.
DIPiDIP-1N.
IntActiP19527. 1 interactor.
STRINGi10116.ENSRNOP00000018599.

PTM databases

iPTMnetiP19527.
PhosphoSitePlusiP19527.
UniCarbKBiP19527.

2D gel databases

World-2DPAGEi0004:P19527.

Proteomic databases

PaxDbiP19527.
PRIDEiP19527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018599; ENSRNOP00000018599; ENSRNOG00000013658.
GeneIDi83613.
KEGGirno:83613.
UCSCiRGD:621458. rat.

Organism-specific databases

CTDi4747.
RGDi621458. Nefl.

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP19527.
KOiK04572.
OMAiEMDVSSK.
OrthoDBiEOG091G12MK.
PhylomeDBiP19527.
TreeFamiTF330122.

Enzyme and pathway databases

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

Miscellaneous databases

PROiPR:P19527.

Gene expression databases

BgeeiENSRNOG00000013658.
GenevisibleiP19527. RN.

Family and domain databases

InterProiView protein in InterPro
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF242. PTHR23239:SF242. 1 hit.
PfamiView protein in Pfam
PF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
SMARTiView protein in SMART
SM01391. Filament. 1 hit.
PROSITEiView protein in PROSITE
PS00226. IF. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNFL_RAT
AccessioniPrimary (citable) accession number: P19527
Secondary accession number(s): Q63367
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 155 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.