Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02548 (NFL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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
Micro glutamic acid-rich protein
Neurofilament triplet L protein
Gene names
Name:NEFL
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length555 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 By similarity.

Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization By similarity. Ref.4

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.

Mass spectrometry

Molecular mass is 62600 Da from positions 2 - 555. Determined by MALDI. Ref.4

Ontologies

Keywords
   Cellular componentIntermediate filament
   DomainCoiled coil
   PTMAcetylation
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processanterograde axon cargo transport

Inferred from sequence or structural similarity. Source: UniProtKB

axon transport of mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

intermediate filament bundle assembly

Inferred from sequence or structural similarity. Source: AgBase

intermediate filament organization

Inferred from sequence or structural similarity. Source: AgBase

locomotion

Inferred from sequence or structural similarity. Source: AgBase

microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: AgBase

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: AgBase

neurofilament bundle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

neurofilament cytoskeleton organization

Inferred from sequence or structural similarity. Source: AgBase

neuromuscular process controlling balance

Inferred from sequence or structural similarity. Source: AgBase

neuron projection morphogenesis

Inferred from sequence or structural similarity. Source: AgBase

peripheral nervous system axon regeneration

Inferred from sequence or structural similarity. Source: AgBase

positive regulation of axonogenesis

Inferred from sequence or structural similarity. Source: AgBase

regulation of axon diameter

Inferred from sequence or structural similarity. Source: AgBase

retrograde axon cargo transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: AgBase

intermediate filament

Inferred from sequence or structural similarity. Source: AgBase

neurofilament

Inferred from sequence or structural similarity. Source: AgBase

   Molecular_functionidentical protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein C-terminus binding

Inferred from sequence or structural similarity. Source: UniProtKB

structural constituent of cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 555554Neurofilament light polypeptide
PRO_0000063786

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
Region398 – 555158Tail
Region398 – 44447Tail, subdomain A
Region445 – 555111Tail, subdomain B (acidic)

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue431Phosphotyrosine By similarity
Modified residue561Phosphoserine Ref.4
Modified residue671Phosphoserine Ref.4
Modified residue4731Phosphoserine Ref.4

Experimental info

Sequence conflict495 – 5017Missing AA sequence Ref.3
Sequence conflict5101A → AEA AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P02548 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D772A27EE1F1DCD3

FASTA55562,646
        10         20         30         40         50         60 
MSSFSYEPYY STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS 

        70         80         90        100        110        120 
SGSLMPSLES 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 
TTKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR LSFTSVGSLT TGYTQSSQVF 

       430        440        450        460        470        480 
GRSAYGGLQT SSYLMSARSF PSYYTSHVQE EQIEVEETIE AAKAEEAKDE PPSEGEAEEE 

       490        500        510        520        530        540 
EKEKEEAEAE AEAEAEAEAE EEEGAQEEEA AKEDAEEAKE EEGGEGEEAE ETKEAEEEEK 

       550 
KDEGAGEEQA TKKKD 

« Hide

References

« Hide 'large scale' references
[1]Hill W.D., Zhang L., Balin B.J., Sprinkle T.J.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Holstein.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Basal ganglia.
[3]"Brain micro glutamic acid-rich protein is the C-terminal endpiece of the neurofilament 68-kDa protein as determined by the primary sequence."
Isobe T., Okuyama T.
FEBS Lett. 182:389-392(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 469-555.
[4]"Identification of endogenous phosphorylation sites of bovine medium and low molecular weight neurofilament proteins by tandem mass spectrometry."
Trimpin S., Mixon A.E., Stapels M.D., Kim M.Y., Spencer P.S., Deinzer M.L.
Biochemistry 43:2091-2105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-56; SER-67 AND SER-473, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U83919 mRNA. Translation: AAB41543.1.
BC118240 mRNA. Translation: AAI18241.1.
PIRJW0094.
RefSeqNP_776546.1. NM_174121.1.
UniGeneBt.89013.

3D structure databases

ProteinModelPortalP02548.
SMRP02548. Positions 88-124, 324-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02548. 1 interaction.

Proteomic databases

PaxDbP02548.
PRIDEP02548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000029264; ENSBTAP00000029264; ENSBTAG00000021949.
GeneID281348.
KEGGbta:281348.

Organism-specific databases

CTD4747.

Phylogenomic databases

eggNOGNOG145720.
GeneTreeENSGT00750000117235.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP02548.
KOK04572.
OMARSFPTYY.
OrthoDBEOG7FV3Q8.
TreeFamTF330122.

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

NextBio20805356.

Entry information

Entry nameNFL_BOVIN
AccessionPrimary (citable) accession number: P02548
Secondary accession number(s): P79127, Q17QQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 122 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