Neurofilament light polypeptide - Mus musculus (Mouse)

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P08551 (NFL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 132. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Interacts with TRIM2. Ref.9 Ref.14
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. Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization By similarity. Ref.7 Ubiquitinated in the presence of TRIM2 and UBE2D1. Ref.14
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 component	Intermediate filament
Domain	Coiled coil
PTM	Acetylation Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intermediate filament bundle assembly Inferred from genetic interaction PubMed 10461886. Source: MGI locomotion Inferred from mutant phenotype PubMed 15132161. Source: MGI microtubule cytoskeleton organization Inferred from mutant phenotype PubMed 11487626. Source: MGI negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 10884316 PubMed 7946341. Source: MGI neurofilament cytoskeleton organization Inferred from mutant phenotype PubMed 11487626 PubMed 14561875 PubMed 15132161 PubMed 16920084 PubMed 9398473. Source: MGI neuromuscular process controlling balance Inferred from mutant phenotype PubMed 15884021. Source: MGI peripheral nervous system axon regeneration Inferred from mutant phenotype PubMed 9398473. Source: MGI positive regulation of axonogenesis Inferred from mutant phenotype PubMed 7946341. Source: MGI protein polymerization Inferred from electronic annotation. Source: Compara regulation of axon diameter Inferred from mutant phenotype PubMed 11343650 PubMed 9398473. Source: MGI response to corticosterone stimulus Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara
Cellular_component	growth cone Inferred from electronic annotation. Source: Compara neurofilament Inferred from direct assay PubMed 10221457 PubMed 15242779 PubMed 8821035. Source: MGI
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 543

542

Neurofilament light polypeptide

PRO_0000063788

Regions

Region

2 – 93

Head

Region

94 – 397

304

Rod

Region

94 – 125

Coil 1A

Region

126 – 138

Linker 1

Region

139 – 234

Coil 1B

Region

235 – 253

Linker 12

Region

254 – 272

Coil 2A

Region

273 – 281

Linker 2

Region

282 – 397

116

Coil 2B

Region

382 – 392

Epitope; recognized by IF-specific monoclonal antibody

Region

398 – 543

146

Tail

Region

398 – 444

Tail, subdomain A

Region

445 – 543

Tail, subdomain B (acidic)

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphotyrosine Ref.12

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine By similarity

Modified residue

425

Phosphotyrosine Ref.12

Modified residue

433

Phosphotyrosine Ref.12

Modified residue

473

Phosphoserine Ref.10

Modified residue

532

Phosphoserine Ref.10 Ref.13

Glycosylation

O-linked (GlcNAc) By similarity

Glycosylation

O-linked (GlcNAc) By similarity

Experimental info

Sequence conflict

Y → S in AAA39810. Ref.2

Sequence conflict

Y → I in AAA39810. Ref.2

Sequence conflict

M → K in AAA39810. Ref.2

Sequence conflict

L → V in AAA39810. Ref.2

Sequence conflict

D → H in AAA39810. Ref.2

Sequence conflict

195

A → R in AAA39814. Ref.1

Sequence conflict

203

Missing in AAA39814. Ref.1

Sequence conflict

240

Y → I in AAA39810. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P08551 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: BC40F8A8A536CFF5
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FASTA

543

61,508

        10         20         30         40         50         60 
MSSFGYDPYF 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 SSYLMSARSF PAYYTSHVQE EQTEVEETIE ATKAEEAKDE PPSEGEAEEE 

       490        500        510        520        530        540 
EKEKEEGEEE EGAEEEEAAK DESEDTKEEE EGGEGEEEDT KESEEEEKKE ESAGEEQVAK 


KKD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and developmental expression of the murine neurofilament gene family." Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F. Brain Res. 387:243-250(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Anomalous placement of introns in a member of the intermediate filament multigene family: an evolutionary conundrum." Lewis S.A., Cowan N.J. Mol. Cell. Biol. 6:1529-1534(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[3]	Jensen K.H., Brown A. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cerebellum.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[5]	"Structure of the 68-kDa neurofilament gene and regulation of its expression." Nakahira K., Ikenaka K., Wada K., Tamura T.A., Furuichi T., Mikoshiba K. J. Biol. Chem. 265:19786-19791(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[6]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 38-54; 117-126 AND 381-391, MASS SPECTROMETRY. Tissue: Hippocampus.
[7]	"Identification of Ser-55 as a major protein kinase A phosphorylation site on the 70-kDa subunit of neurofilaments. Early turnover during axonal transport." Sihag R.K., Nixon R.A. J. Biol. Chem. 266:18861-18867(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 52-57, PHOSPHORYLATION AT SER-56.
[8]	"Genetics, evolution, and expression of the 68,000-mol-wt neurofilament protein: isolation of a cloned cDNA probe." Lewis S.A., Cowan N.J. J. Cell Biol. 100:843-850(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 242-543. Tissue: Brain.
[9]	"RNA-binding protein is involved in aggregation of light neurofilament protein and is implicated in the pathogenesis of motor neuron degeneration." Lin H., Zhai J., Schlaepfer W.W. Hum. Mol. Genet. 14:3643-3659(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF28.
[10]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-532, MASS SPECTROMETRY. Tissue: Brain.
[11]	"O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry." Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Brain.
[12]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43; TYR-425 AND TYR-433, MASS SPECTROMETRY. Tissue: Brain.
[13]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532, MASS SPECTROMETRY. Tissue: Melanoma.
[14]	"Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament light chain and neurodegeneration." Balastik M., Ferraguti F., Pires-da Silva A., Lee T.H., Alvarez-Bolado G., Lu K.P., Gruss P. Proc. Natl. Acad. Sci. U.S.A. 105:12016-12021(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRIM2, UBIQUITINATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00554928.
PIR	QFMSL. A25227.
RefSeq	NP_035040.1. NM_010910.1.
UniGene	Mm.1956.
3D structure databases
ProteinModelPortal	P08551.
SMR	P08551. Positions 87-238, 253-322, 327-396.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31944N.
IntAct	P08551. 5 interactions.
STRING	10090.ENSMUSP00000022639.
PTM databases
PhosphoSite	P08551.
2D gel databases
UCD-2DPAGE	P08551.
Proteomic databases
PaxDb	P08551.
PRIDE	P08551.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000022639; ENSMUSP00000022639; ENSMUSG00000022055.
GeneID	18039.
KEGG	mmu:18039.
UCSC	uc007uln.1. mouse.
Organism-specific databases
CTD	4747.
MGI	MGI:97313. Nefl.
Phylogenomic databases
eggNOG	NOG145720.
GeneTree	ENSGT00690000102043.
HOGENOM	HOG000230977.
HOVERGEN	HBG013015.
InParanoid	P08551.
KO	K04572.
OMA	PRVHISS.
OrthoDB	EOG42Z4QC.
Gene expression databases
Bgee	P08551.
CleanEx	MM_NEFL.
Genevestigator	P08551.
GermOnline	ENSMUSG00000022055. Mus musculus.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR006821. Intermed_filament_DNA-bd. IPR018039. Intermediate_filament_CS. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. PF04732. Filament_head. 1 hit. [Graphical view]
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NEFL. mouse.
NextBio	293145.
SOURCE	Search...

Entry information

Entry name

NFL_MOUSE

Accession

Primary (citable) accession number: P08551
Secondary accession number(s): Q8K0Z0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 132 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents