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P19527

- NFL_RAT

UniProt

P19527 - NFL_RAT

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Protein
Neurofilament light polypeptide
Gene
Nefl, Nf68, Nfl
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

  1. phospholipase binding Source: RGD
  2. protein domain specific binding Source: RGD
  3. structural molecule activity Source: InterPro

GO - Biological processi

  1. intermediate filament bundle assembly Source: Ensembl
  2. locomotion Source: Ensembl
  3. microtubule cytoskeleton organization Source: Ensembl
  4. negative regulation of neuron apoptotic process Source: Ensembl
  5. neurofilament cytoskeleton organization Source: Ensembl
  6. neuromuscular process controlling balance Source: Ensembl
  7. neuron projection morphogenesis Source: Ensembl
  8. peripheral nervous system axon regeneration Source: Ensembl
  9. positive regulation of axonogenesis Source: Ensembl
  10. protein polymerization Source: RGD
  11. regulation of axon diameter Source: Ensembl
  12. response to corticosterone Source: RGD
  13. response to organic substance Source: RGD
  14. response to organonitrogen compound Source: RGD
  15. response to peptide hormone Source: RGD
  16. response to toxic substance Source: RGD
Complete GO annotation...

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 15

Organism-specific databases

RGDi621458. Nefl.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: RGD
  2. growth cone Source: RGD
  3. neurofilament Source: Ensembl
  4. neuron projection Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 542541Neurofilament light polypeptide
PRO_0000063790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Glycosylationi21 – 211O-linked (GlcNAc)1 Publication
CAR_000128
Glycosylationi27 – 271O-linked (GlcNAc)1 Publication
CAR_000129
Modified residuei43 – 431Phosphotyrosine By similarity
Modified residuei56 – 561Phosphoserine By similarity
Modified residuei67 – 671Phosphoserine By similarity
Modified residuei473 – 4731Phosphoserine By similarity
Modified residuei531 – 5311Phosphoserine By similarity

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, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP19527.
PRIDEiP19527.

2D gel databases

World-2DPAGE0004:P19527.

PTM databases

PhosphoSiteiP19527.
UniCarbKBiP19527.

Expressioni

Gene expression databases

GenevestigatoriP19527.

Interactioni

Subunit structurei

Interacts with ARHGEF28 By similarity. Interacts with TRIM2 By similarity.

Protein-protein interaction databases

BioGridi249778. 5 interactions.
DIPiDIP-1N.
IntActiP19527. 1 interaction.
STRINGi10116.ENSRNOP00000018599.

Structurei

3D structure databases

ProteinModelPortaliP19527.
SMRiP19527. Positions 88-124, 324-396.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9392Head
Add
BLAST
Regioni94 – 397304Rod
Add
BLAST
Regioni94 – 12532Coil 1A
Add
BLAST
Regioni126 – 13813Linker 1
Add
BLAST
Regioni139 – 23496Coil 1B
Add
BLAST
Regioni235 – 25319Linker 12
Add
BLAST
Regioni254 – 27219Coil 2A
Add
BLAST
Regioni273 – 2819Linker 2
Regioni282 – 397116Coil 2B
Add
BLAST
Regioni382 – 39211Epitope; recognized by IF-specific monoclonal antibody
Add
BLAST
Regioni398 – 542145Tail
Add
BLAST
Regioni398 – 44447Tail, subdomain A
Add
BLAST
Regioni445 – 54298Tail, 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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG145720.
GeneTreeiENSGT00750000117235.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP19527.
KOiK04572.
OMAiARNMQNA.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP19527.
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.

P19527-1 [UniParc]FASTAAdd to Basket

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MSSFSYEPYF STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS    50
LSVRRSYSSS SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR 100
FASFIERVHE LEQQNKVLEA ELLVLRQKHS EPSRFRALYE QEIRDLRLAA 150
EDATNEKQAL QGEREGLEET LRNLQARYEE EVLSREDAEG RLMEARKGAD 200
EAALARAELE KRIDSLMDEI AFLKKVHEEE IAELQAQIQY AQISVEMDVS 250
SKPDLSAALK DIRAQYEKLA AKNMQNAEEW FKSRFTVLTE SAAKNTDAVR 300
AAKDEVSESR RLLKAKTLEI EACRGMNEAL EKQLQELEDK QNADISAMQD 350
TINKLENELR STKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR 400
LSFTSVGSIT SGYSQSSQVF GRSAYSGLQS SSYLMSARAF PAYYTSHVQE 450
EQSEVEETIE ATKAEEAKDE PPSEGEAEEE EKEKEEGEEE EGAEEEEAAK 500
DESEDAKEEE GGEGEEEDTK ESEEEEKKEE SAGEEQAAKK KD 542
Length:542
Mass (Da):61,335
Last modified:January 23, 2007 - v3
Checksum:i1FCC739AF23BCCA8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti198 – 2036GADEAA → KARMSS in AAA41694. 1 Publication
Sequence conflicti400 – 4001R → K in AAA41694. 1 Publication
Sequence conflicti477 – 4771A → E in AAA41694. 1 Publication
Sequence conflicti481 – 4844EKEK → KKDE in AAA41694. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF031880 mRNA. Translation: AAB87069.1 .
M25638 mRNA. Translation: AAA41694.1 .
X53981 Genomic DNA. Translation: CAA37931.1 .
PIRi A21762.
I60434.
RefSeqi NP_113971.1. NM_031783.1.
UniGenei Rn.18568.

3D structure databases

ProteinModelPortali P19527.
SMRi P19527. Positions 88-124, 324-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249778. 5 interactions.
DIPi DIP-1N.
IntActi P19527. 1 interaction.
STRINGi 10116.ENSRNOP00000018599.

PTM databases

PhosphoSitei P19527.
UniCarbKBi P19527.

2D gel databases

World-2DPAGE 0004:P19527.

Proteomic databases

PaxDbi P19527.
PRIDEi P19527.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000018599 ; ENSRNOP00000018599 ; ENSRNOG00000013658 .
GeneIDi 83613.
KEGGi rno:83613.
UCSCi RGD:621458. rat.

Organism-specific databases

CTDi 4747.
RGDi 621458. Nefl.

Phylogenomic databases

eggNOGi NOG145720.
GeneTreei ENSGT00750000117235.
HOGENOMi HOG000230977.
HOVERGENi HBG013015.
InParanoidi P19527.
KOi K04572.
OMAi ARNMQNA.
OrthoDBi EOG7FV3Q8.
PhylomeDBi P19527.
TreeFami TF330122.

Miscellaneous databases

NextBioi 616157.
PROi P19527.

Gene expression databases

Genevestigatori P19527.

Family and domain databases

InterProi IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
PTHR23239:SF22. PTHR23239:SF22. 1 hit.
Pfami PF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view ]
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiNFL_RAT
AccessioniPrimary (citable) accession number: P19527
Secondary accession number(s): Q63367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 130 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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