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P02548

- NFL_BOVIN

UniProt

P02548 - NFL_BOVIN

Protein

Neurofilament light polypeptide

Gene

NEFL

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (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. identical protein binding Source: UniProtKB
    2. protein C-terminus binding Source: UniProtKB
    3. structural constituent of cytoskeleton Source: UniProtKB

    GO - Biological processi

    1. anterograde axon cargo transport Source: UniProtKB
    2. axon transport of mitochondrion Source: UniProtKB
    3. intermediate filament bundle assembly Source: AgBase
    4. intermediate filament organization Source: AgBase
    5. locomotion Source: AgBase
    6. microtubule cytoskeleton organization Source: AgBase
    7. negative regulation of neuron apoptotic process Source: AgBase
    8. neurofilament bundle assembly Source: UniProtKB
    9. neurofilament cytoskeleton organization Source: AgBase
    10. neuromuscular process controlling balance Source: AgBase
    11. neuron projection morphogenesis Source: AgBase
    12. peripheral nervous system axon regeneration Source: AgBase
    13. positive regulation of axonogenesis Source: AgBase
    14. regulation of axon diameter Source: AgBase
    15. retrograde axon cargo transport Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:NEFL
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 8

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: AgBase
    2. intermediate filament Source: AgBase
    3. neurofilament Source: AgBase

    Keywords - Cellular componenti

    Intermediate filament

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 555554Neurofilament light polypeptidePRO_0000063786Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei43 – 431PhosphotyrosineBy similarity
    Modified residuei56 – 561Phosphoserine1 Publication
    Modified residuei67 – 671Phosphoserine1 Publication
    Modified residuei473 – 4731Phosphoserine1 Publication

    Post-translational modificationi

    O-glycosylated.By similarity
    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

    PaxDbiP02548.
    PRIDEiP02548.

    Interactioni

    Subunit structurei

    Interacts with ARHGEF28. Interacts with TRIM2.By similarity

    Protein-protein interaction databases

    IntActiP02548. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP02548.
    SMRiP02548. Positions 88-124, 324-396.
    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
    Regioni398 – 555158TailAdd
    BLAST
    Regioni398 – 44447Tail, subdomain AAdd
    BLAST
    Regioni445 – 555111Tail, 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.
    InParanoidiP02548.
    KOiK04572.
    OMAiARNMQNA.
    OrthoDBiEOG7FV3Q8.
    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.

    P02548-1 [UniParc]FASTAAdd to Basket

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    MSSFSYEPYY STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS    50
    LSVRRSYSSS SGSLMPSLES 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 TTKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR 400
    LSFTSVGSLT TGYTQSSQVF GRSAYGGLQT SSYLMSARSF PSYYTSHVQE 450
    EQIEVEETIE AAKAEEAKDE PPSEGEAEEE EKEKEEAEAE AEAEAEAEAE 500
    EEEGAQEEEA AKEDAEEAKE EEGGEGEEAE ETKEAEEEEK KDEGAGEEQA 550
    TKKKD 555
    Length:555
    Mass (Da):62,646
    Last modified:January 23, 2007 - v3
    Checksum:iD772A27EE1F1DCD3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti495 – 5017Missing AA sequence (PubMed:3884373)Curated
    Sequence conflicti510 – 5101A → AEA AA sequence (PubMed:3884373)Curated

    Mass spectrometryi

    Molecular mass is 62600 Da from positions 2 - 555. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83919 mRNA. Translation: AAB41543.1.
    BC118240 mRNA. Translation: AAI18241.1.
    PIRiJW0094.
    RefSeqiNP_776546.1. NM_174121.1.
    UniGeneiBt.89013.

    Genome annotation databases

    EnsembliENSBTAT00000029264; ENSBTAP00000029264; ENSBTAG00000021949.
    GeneIDi281348.
    KEGGibta:281348.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83919 mRNA. Translation: AAB41543.1 .
    BC118240 mRNA. Translation: AAI18241.1 .
    PIRi JW0094.
    RefSeqi NP_776546.1. NM_174121.1.
    UniGenei Bt.89013.

    3D structure databases

    ProteinModelPortali P02548.
    SMRi P02548. Positions 88-124, 324-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P02548. 1 interaction.

    Proteomic databases

    PaxDbi P02548.
    PRIDEi P02548.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000029264 ; ENSBTAP00000029264 ; ENSBTAG00000021949 .
    GeneIDi 281348.
    KEGGi bta:281348.

    Organism-specific databases

    CTDi 4747.

    Phylogenomic databases

    eggNOGi NOG145720.
    GeneTreei ENSGT00750000117235.
    HOGENOMi HOG000230977.
    HOVERGENi HBG013015.
    InParanoidi P02548.
    KOi K04572.
    OMAi ARNMQNA.
    OrthoDBi EOG7FV3Q8.
    TreeFami TF330122.

    Miscellaneous databases

    NextBioi 20805356.

    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. 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.

    Entry informationi

    Entry nameiNFL_BOVIN
    AccessioniPrimary (citable) accession number: P02548
    Secondary accession number(s): P79127, Q17QQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 124 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