ID   NFL_BOVIN               Reviewed;         555 AA.
AC   P02548; P79127; Q17QQ0;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, entry version 191.
DE   RecName: Full=Neurofilament light polypeptide;
DE            Short=NF-L;
DE   AltName: Full=68 kDa neurofilament protein;
DE   AltName: Full=Micro glutamic acid-rich protein;
DE   AltName: Full=Neurofilament triplet L protein;
GN   Name=NEFL;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein; TISSUE=Brain;
RA   Hill W.D., Zhang L., Balin B.J., Sprinkle T.J.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 469-555.
RX   PubMed=3884373; DOI=10.1016/0014-5793(85)80339-2;
RA   Isobe T., Okuyama T.;
RT   "Brain micro glutamic acid-rich protein is the C-terminal endpiece of the
RT   neurofilament 68-kDa protein as determined by the primary sequence.";
RL   FEBS Lett. 182:389-392(1985).
RN   [4]
RP   ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-56; SER-67 AND SER-473, AND
RP   MASS SPECTROMETRY.
RX   PubMed=14967049; DOI=10.1021/bi030196q;
RA   Trimpin S., Mixon A.E., Stapels M.D., Kim M.Y., Spencer P.S., Deinzer M.L.;
RT   "Identification of endogenous phosphorylation sites of bovine medium and
RT   low molecular weight neurofilament proteins by tandem mass spectrometry.";
RL   Biochemistry 43:2091-2105(2004).
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) (By similarity). Forms
CC       heterodimers with NEFH or NEFM; which can further heterooligomerize (in
CC       vitro) (By similarity). Forms heterodimers with INA (in vitro) (By
CC       similarity). Interacts with ARHGEF28. Interacts with TRIM2.
CC       {ECO:0000250, ECO:0000250|UniProtKB:P19527}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P08551}.
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. {ECO:0000250}.
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   -!- MASS SPECTROMETRY: Mass=62600; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14967049};
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; U83919; AAB41543.1; -; mRNA.
DR   EMBL; BC118240; AAI18241.1; -; mRNA.
DR   PIR; JW0094; JW0094.
DR   RefSeq; NP_776546.1; NM_174121.1.
DR   AlphaFoldDB; P02548; -.
DR   SMR; P02548; -.
DR   FunCoup; P02548; 292.
DR   IntAct; P02548; 1.
DR   STRING; 9913.ENSBTAP00000029264; -.
DR   iPTMnet; P02548; -.
DR   PaxDb; 9913-ENSBTAP00000029264; -.
DR   PeptideAtlas; P02548; -.
DR   Ensembl; ENSBTAT00000029264.6; ENSBTAP00000029264.4; ENSBTAG00000021949.6.
DR   Ensembl; ENSBTAT00085000984; ENSBTAP00085001236; ENSBTAG00085013194.
DR   Ensembl; ENSBTAT00090013566; ENSBTAP00090006370; ENSBTAG00090007325.
DR   GeneID; 281348; -.
DR   KEGG; bta:281348; -.
DR   CTD; 4747; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021949; -.
DR   VGNC; VGNC:31986; NEFL.
DR   eggNOG; ENOG502QSXY; Eukaryota.
DR   GeneTree; ENSGT00940000156208; -.
DR   HOGENOM; CLU_012560_7_3_1; -.
DR   InParanoid; P02548; -.
DR   OMA; ACEYKVG; -.
DR   OrthoDB; 2441647at2759; -.
DR   Reactome; R-BTA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-BTA-5673001; RAF/MAP kinase cascade.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000021949; Expressed in prefrontal cortex and 51 other cell types or tissues.
DR   GO; GO:0030424; C:axon; ISS:AgBase.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005882; C:intermediate filament; ISS:AgBase.
DR   GO; GO:0005883; C:neurofilament; ISS:AgBase.
DR   GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR   GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
DR   GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR   GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; ISS:AgBase.
DR   GO; GO:0045109; P:intermediate filament organization; ISS:AgBase.
DR   GO; GO:0040011; P:locomotion; ISS:AgBase.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:AgBase.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:AgBase.
DR   GO; GO:0033693; P:neurofilament bundle assembly; ISS:UniProtKB.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:AgBase.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; ISS:AgBase.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISS:AgBase.
DR   GO; GO:0014012; P:peripheral nervous system axon regeneration; ISS:AgBase.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; ISS:AgBase.
DR   GO; GO:0031133; P:regulation of axon diameter; ISS:AgBase.
DR   GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB.
DR   FunFam; 1.20.5.1160:FF:000001; Keratin type II; 1.
DR   FunFam; 1.20.5.170:FF:000002; Type I keratin KA11; 1.
DR   FunFam; 1.20.5.500:FF:000001; Type II keratin 23; 1.
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   InterPro; IPR050405; Intermediate_filament.
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.
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|PubMed:14967049"
FT   CHAIN           2..555
FT                   /note="Neurofilament light polypeptide"
FT                   /id="PRO_0000063786"
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          398..555
FT                   /note="Tail"
FT   REGION          398..444
FT                   /note="Tail, subdomain A"
FT   REGION          445..555
FT                   /note="Tail, subdomain B (acidic)"
FT   REGION          463..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..540
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..555
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|PubMed:14967049"
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:0000269|PubMed:14967049"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14967049"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19527"
FT   MOD_RES         473
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14967049"
FT   MOD_RES         532
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P19527"
FT   CONFLICT        495..501
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        510
FT                   /note="A -> AEA (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   555 AA;  62646 MW;  D772A27EE1F1DCD3 CRC64;
     MSSFSYEPYY STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS
     SGSLMPSLES 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
     TTKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR LSFTSVGSLT TGYTQSSQVF
     GRSAYGGLQT SSYLMSARSF PSYYTSHVQE EQIEVEETIE AAKAEEAKDE PPSEGEAEEE
     EKEKEEAEAE AEAEAEAEAE EEEGAQEEEA AKEDAEEAKE EEGGEGEEAE ETKEAEEEEK
     KDEGAGEEQA TKKKD
//