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P08551

- NFL_MOUSE

UniProt

P08551 - NFL_MOUSE

Protein

Neurofilament light polypeptide

Gene

Nefl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. protein binding, bridging Source: BHF-UCL
    3. structural constituent of cytoskeleton Source: BHF-UCL

    GO - Biological processi

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

    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
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:97313. Nefl.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: MGI
    2. cytoplasm Source: BHF-UCL
    3. growth cone Source: Ensembl
    4. intermediate filament Source: BHF-UCL
    5. neurofilament Source: MGI
    6. neuron projection Source: MGI

    Keywords - Cellular componenti

    Intermediate filament

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 543542Neurofilament light polypeptidePRO_0000063788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Glycosylationi21 – 211O-linked (GlcNAc)By similarity
    Glycosylationi27 – 271O-linked (GlcNAc)By similarity
    Modified residuei43 – 431Phosphotyrosine1 Publication
    Modified residuei56 – 561Phosphoserine1 Publication
    Modified residuei67 – 671PhosphoserineBy similarity
    Modified residuei473 – 4731Phosphoserine1 Publication
    Modified residuei532 – 5321Phosphoserine1 Publication

    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, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP08551.
    PaxDbiP08551.
    PRIDEiP08551.

    2D gel databases

    UCD-2DPAGEP08551.

    PTM databases

    PhosphoSiteiP08551.

    Expressioni

    Gene expression databases

    BgeeiP08551.
    CleanExiMM_NEFL.
    GenevestigatoriP08551.

    Interactioni

    Subunit structurei

    Interacts with ARHGEF28. Interacts with TRIM2.2 Publications

    Protein-protein interaction databases

    BioGridi201757. 7 interactions.
    DIPiDIP-31944N.
    IntActiP08551. 6 interactions.
    MINTiMINT-4116847.
    STRINGi10090.ENSMUSP00000022639.

    Structurei

    3D structure databases

    ProteinModelPortaliP08551.
    SMRiP08551. Positions 87-238, 253-322, 327-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 9392HeadAdd
    BLAST
    Regioni94 – 397304RodAdd
    BLAST
    Regioni94 – 12532Coil 1AAdd
    BLAST
    Regioni126 – 13813Linker 1Add
    BLAST
    Regioni139 – 23496Coil 1BAdd
    BLAST
    Regioni235 – 25319Linker 12Add
    BLAST
    Regioni254 – 27219Coil 2AAdd
    BLAST
    Regioni273 – 2819Linker 2
    Regioni282 – 397116Coil 2BAdd
    BLAST
    Regioni382 – 39211Epitope; recognized by IF-specific monoclonal antibodyAdd
    BLAST
    Regioni398 – 543146TailAdd
    BLAST
    Regioni398 – 44447Tail, subdomain AAdd
    BLAST
    Regioni445 – 54399Tail, 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

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG145720.
    GeneTreeiENSGT00750000117235.
    HOGENOMiHOG000230977.
    HOVERGENiHBG013015.
    InParanoidiP08551.
    KOiK04572.
    OMAiARNMQNA.
    OrthoDBiEOG7FV3Q8.
    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]
    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

    MSSFGYDPYF 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 SSYLMSARSF PAYYTSHVQE 450
    EQTEVEETIE ATKAEEAKDE PPSEGEAEEE EKEKEEGEEE EGAEEEEAAK 500
    DESEDTKEEE EGGEGEEEDT KESEEEEKKE ESAGEEQVAK KKD 543
    Length:543
    Mass (Da):61,508
    Last modified:January 23, 2007 - v5
    Checksum:iBC40F8A8A536CFF5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61Y → S in AAA39810. (PubMed:3785173)Curated
    Sequence conflicti9 – 91Y → I in AAA39810. (PubMed:3785173)Curated
    Sequence conflicti65 – 651M → K in AAA39810. (PubMed:3785173)Curated
    Sequence conflicti73 – 731L → V in AAA39810. (PubMed:3785173)Curated
    Sequence conflicti99 – 991D → H in AAA39810. (PubMed:3785173)Curated
    Sequence conflicti195 – 1951A → R in AAA39814. (PubMed:3103856)Curated
    Sequence conflicti203 – 2031Missing in AAA39814. (PubMed:3103856)Curated
    Sequence conflicti240 – 2401Y → I in AAA39810. (PubMed:3785173)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS27232.1.
    PIRi A25227. QFMSL.
    RefSeqi NP_035040.1. NM_010910.1.
    UniGenei Mm.1956.

    3D structure databases

    ProteinModelPortali P08551.
    SMRi P08551. Positions 87-238, 253-322, 327-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201757. 7 interactions.
    DIPi DIP-31944N.
    IntActi P08551. 6 interactions.
    MINTi MINT-4116847.
    STRINGi 10090.ENSMUSP00000022639.

    PTM databases

    PhosphoSitei P08551.

    2D gel databases

    UCD-2DPAGE P08551.

    Proteomic databases

    MaxQBi P08551.
    PaxDbi P08551.
    PRIDEi P08551.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022639 ; ENSMUSP00000022639 ; ENSMUSG00000022055 .
    GeneIDi 18039.
    KEGGi mmu:18039.
    UCSCi uc007uln.1. mouse.

    Organism-specific databases

    CTDi 4747.
    MGIi MGI:97313. Nefl.

    Phylogenomic databases

    eggNOGi NOG145720.
    GeneTreei ENSGT00750000117235.
    HOGENOMi HOG000230977.
    HOVERGENi HBG013015.
    InParanoidi P08551.
    KOi K04572.
    OMAi ARNMQNA.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi P08551.
    TreeFami TF330122.

    Miscellaneous databases

    ChiTaRSi NEFL. mouse.
    NextBioi 293145.
    PROi P08551.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08551.
    CleanExi MM_NEFL.
    Genevestigatori P08551.

    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. "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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    13. "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.

    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: October 1, 2014
    This is version 145 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

    External Data

    Dasty 3