ID   NFL_RAT                 Reviewed;         542 AA.
AC   P19527; Q63367;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Neurofilament light polypeptide;
DE            Short=NF-L;
DE   AltName: Full=68 kDa neurofilament protein;
DE   AltName: Full=Neurofilament triplet L protein;
GN   Name=Nefl; Synonyms=Nf68, Nfl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2516804;
RA   Chin S.S., Liem R.K.H.;
RT   "Expression of rat neurofilament proteins NF-L and NF-M in transfected non-
RT   neuronal cells.";
RL   Eur. J. Cell Biol. 50:475-490(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 198-484.
RX   PubMed=3925999; DOI=10.1016/0167-4781(85)90067-3;
RA   Julien J.-P., Ramachandran K., Grosveld F.;
RT   "Cloning of a cDNA encoding the smallest neurofilament protein from the
RT   rat.";
RL   Biochim. Biophys. Acta 825:398-404(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX   PubMed=7745611; DOI=10.1002/jnr.490400206;
RA   Reeben M., Neuman T., Palgi J., Palm K., Paalme V., Saarma M.;
RT   "Characterization of the rat light neurofilament (NF-L) gene promoter and
RT   identification of NGF and cAMP responsive regions.";
RL   J. Neurosci. Res. 40:177-188(1995).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-14; 38-54; 56-84; 92-107; 117-126; 148-157; 165-172;
RP   212-224; 273-282; 285-294; 368-379; 381-391; 393-422 AND 439-463,
RP   ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Pradeep J.J.P., Afjehi-Sadat L., Diao W., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   GLYCOSYLATION AT THR-21 AND SER-27.
RX   PubMed=8344946; DOI=10.1016/s0021-9258(19)85471-6;
RA   Dong D.L.-Y., Xu Z.-S., Chevrier M.R., Cotter R.J., Cleveland D.W.,
RA   Hart G.W.;
RT   "Glycosylation of mammalian neurofilaments. Localization of multiple O-
RT   linked N-acetylglucosamine moieties on neurofilament polypeptides L and
RT   M.";
RL   J. Biol. Chem. 268:16679-16687(1993).
RN   [6]
RP   SUBUNIT, INTERACTION WITH NEFH; NEFM AND INA, AND TISSUE SPECIFICITY.
RX   PubMed=9388258; DOI=10.1074/jbc.272.49.31073;
RA   Athlan E.S., Mushynski W.E.;
RT   "Heterodimeric associations between neuronal intermediate filament
RT   proteins.";
RL   J. Biol. Chem. 272:31073-31078(1997).
RN   [7]
RP   ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Lubec G., Chen W.-Q.;
RL   Submitted (FEB-2007) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-103; SER-453;
RP   SER-473; SER-503; THR-519; SER-522 AND SER-531, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Neurofilaments usually contain three intermediate filament
CC       proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of
CC       neuronal caliber. May additionally cooperate with the neuronal
CC       intermediate filament proteins PRPH and INA to form neuronal
CC       filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08551}.
CC   -!- SUBUNIT: Forms homodimers (in vitro) (PubMed:9388258). Forms
CC       heterodimers with NEFH or NEFM; which can further hetero-oligomerize
CC       (in vitro) (PubMed:9388258). Forms heterodimers with INA (in vitro)
CC       (PubMed:9388258). Interacts with ARHGEF28. Interacts with TRIM2.
CC       {ECO:0000250, ECO:0000269|PubMed:9388258}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P08551}.
CC   -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglion neurons (at
CC       protein level). {ECO:0000269|PubMed:9388258}.
CC   -!- DOMAIN: The extra mass and high charge density that distinguish the
CC       neurofilament proteins from all other intermediate filament proteins
CC       are due to the tailpiece extensions. This region may form a charged
CC       scaffolding structure suitable for interaction with other neuronal
CC       components or ions.
CC   -!- PTM: O-glycosylated; contains three N-acetylglucosamine side chains.
CC       {ECO:0000269|PubMed:8344946}.
CC   -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1,
CC       leading to the inhibition of polymerization. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000250}.
CC   -!- MISCELLANEOUS: NF-L is the most abundant of the three neurofilament
CC       proteins and, like the other nonepithelial intermediate filament
CC       proteins, it can form homomeric 10-nm filaments.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AF031880; AAB87069.1; -; mRNA.
DR   EMBL; M25638; AAA41694.1; -; mRNA.
DR   EMBL; X53981; CAA37931.1; -; Genomic_DNA.
DR   PIR; A21762; A21762.
DR   PIR; I60434; I60434.
DR   RefSeq; NP_113971.1; NM_031783.1.
DR   AlphaFoldDB; P19527; -.
DR   SMR; P19527; -.
DR   BioGRID; 249778; 8.
DR   DIP; DIP-1N; -.
DR   IntAct; P19527; 3.
DR   MINT; P19527; -.
DR   STRING; 10116.ENSRNOP00000018599; -.
DR   GlyConnect; 431; 1 O-GlcNAc glycan (2 sites).
DR   GlyCosmos; P19527; 2 sites, 1 glycan.
DR   GlyGen; P19527; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; P19527; -.
DR   PhosphoSitePlus; P19527; -.
DR   SwissPalm; P19527; -.
DR   jPOST; P19527; -.
DR   PaxDb; 10116-ENSRNOP00000018599; -.
DR   Ensembl; ENSRNOT00000018599.4; ENSRNOP00000018599.1; ENSRNOG00000013658.4.
DR   Ensembl; ENSRNOT00055011317; ENSRNOP00055008886; ENSRNOG00055006877.
DR   Ensembl; ENSRNOT00060017783; ENSRNOP00060013824; ENSRNOG00060010521.
DR   Ensembl; ENSRNOT00065031593; ENSRNOP00065025187; ENSRNOG00065018809.
DR   GeneID; 83613; -.
DR   KEGG; rno:83613; -.
DR   UCSC; RGD:621458; rat.
DR   AGR; RGD:621458; -.
DR   RGD; 621458; Nefl.
DR   eggNOG; ENOG502QSXY; Eukaryota.
DR   GeneTree; ENSGT00940000156208; -.
DR   HOGENOM; CLU_012560_7_3_1; -.
DR   InParanoid; P19527; -.
DR   OMA; EATHEKQ; -.
DR   OrthoDB; 4640531at2759; -.
DR   PhylomeDB; P19527; -.
DR   TreeFam; TF330122; -.
DR   Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   PRO; PR:P19527; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000013658; Expressed in Ammon's horn and 8 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0098981; C:cholinergic synapse; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR   GO; GO:0005883; C:neurofilament; IDA:RGD.
DR   GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; ISO:RGD.
DR   GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; ISO:RGD.
DR   GO; GO:0099182; C:presynaptic intermediate filament cytoskeleton; ISO:RGD.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0043274; F:phospholipase binding; IPI:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR   GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; ISO:RGD.
DR   GO; GO:0008089; P:anterograde axonal transport; ISO:RGD.
DR   GO; GO:0019896; P:axonal transport of mitochondrion; ISO:RGD.
DR   GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR   GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; ISO:RGD.
DR   GO; GO:0045109; P:intermediate filament organization; ISO:RGD.
DR   GO; GO:0045105; P:intermediate filament polymerization or depolymerization; IDA:RGD.
DR   GO; GO:0040011; P:locomotion; ISO:RGD.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR   GO; GO:0097049; P:motor neuron apoptotic process; ISO:RGD.
DR   GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; ISO:RGD.
DR   GO; GO:0033693; P:neurofilament bundle assembly; IDA:RGD.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; ISO:RGD.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR   GO; GO:0014012; P:peripheral nervous system axon regeneration; ISO:RGD.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; ISO:RGD.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0051258; P:protein polymerization; IDA:RGD.
DR   GO; GO:0031133; P:regulation of axon diameter; ISO:RGD.
DR   GO; GO:0090128; P:regulation of synapse maturation; ISO:RGD.
DR   GO; GO:1903937; P:response to acrylamide; IEP:RGD.
DR   GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR   GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:1903935; P:response to sodium arsenite; IDA:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   GO; GO:0008090; P:retrograde axonal transport; ISO:RGD.
DR   GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1.
DR   PANTHER; PTHR45652:SF8; NEUROFILAMENT LIGHT POLYPEPTIDE; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
DR   World-2DPAGE; 0004:P19527; -.
DR   Genevisible; P19527; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Glycoprotein; Intermediate filament;
KW   Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT   CHAIN           2..542
FT                   /note="Neurofilament light polypeptide"
FT                   /id="PRO_0000063790"
FT   DOMAIN          90..401
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          2..93
FT                   /note="Head"
FT   REGION          94..125
FT                   /note="Coil 1A"
FT   REGION          126..138
FT                   /note="Linker 1"
FT   REGION          139..234
FT                   /note="Coil 1B"
FT   REGION          235..253
FT                   /note="Linker 12"
FT   REGION          254..272
FT                   /note="Coil 2A"
FT   REGION          273..281
FT                   /note="Linker 2"
FT   REGION          282..397
FT                   /note="Coil 2B"
FT   REGION          382..392
FT                   /note="Epitope; recognized by IF-specific monoclonal
FT                   antibody"
FT   REGION          398..542
FT                   /note="Tail"
FT   REGION          398..444
FT                   /note="Tail, subdomain A"
FT   REGION          445..542
FT                   /note="Tail, subdomain B (acidic)"
FT   REGION          451..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..524
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT   MOD_RES         23
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08551"
FT   MOD_RES         23
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08551"
FT   MOD_RES         30
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P08551"
FT   MOD_RES         43
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P08551"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02548"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         473
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         519
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         531
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        21
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000269|PubMed:8344946"
FT                   /id="CAR_000128"
FT   CARBOHYD        27
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000269|PubMed:8344946"
FT                   /id="CAR_000129"
FT   CONFLICT        198..203
FT                   /note="GADEAA -> KARMSS (in Ref. 2; AAA41694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="R -> K (in Ref. 2; AAA41694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="A -> E (in Ref. 2; AAA41694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481..484
FT                   /note="EKEK -> KKDE (in Ref. 2; AAA41694)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   542 AA;  61335 MW;  1FCC739AF23BCCA8 CRC64;
     MSSFSYEPYF STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS
     SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR FASFIERVHE LEQQNKVLEA
     ELLVLRQKHS EPSRFRALYE QEIRDLRLAA EDATNEKQAL QGEREGLEET LRNLQARYEE
     EVLSREDAEG RLMEARKGAD EAALARAELE KRIDSLMDEI AFLKKVHEEE IAELQAQIQY
     AQISVEMDVS SKPDLSAALK DIRAQYEKLA AKNMQNAEEW FKSRFTVLTE SAAKNTDAVR
     AAKDEVSESR RLLKAKTLEI EACRGMNEAL EKQLQELEDK QNADISAMQD TINKLENELR
     STKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR LSFTSVGSIT SGYSQSSQVF
     GRSAYSGLQS SSYLMSARAF PAYYTSHVQE EQSEVEETIE ATKAEEAKDE PPSEGEAEEE
     EKEKEEGEEE EGAEEEEAAK DESEDAKEEE GGEGEEEDTK ESEEEEKKEE SAGEEQAAKK
     KD
//