NFL_BOVIN
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 03-AUG-2022, entry version 173.
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 hetero-oligomerize
CC (in 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 IntAct; P02548; 1.
DR STRING; 9913.ENSBTAP00000029264; -.
DR iPTMnet; P02548; -.
DR PaxDb; P02548; -.
DR PeptideAtlas; P02548; -.
DR PRIDE; P02548; -.
DR Ensembl; ENSBTAT00000029264; ENSBTAP00000029264; ENSBTAG00000021949.
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; YEPYYAT; -.
DR OrthoDB; 655109at2759; -.
DR TreeFam; TF330122; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000021949; Expressed in prefrontal cortex and 51 other tissues.
DR GO; GO:0030424; C:axon; ISS:AgBase.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; ISS:AgBase.
DR GO; GO:0005883; C:neurofilament; ISS:AgBase.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0099182; C:presynaptic intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus 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:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
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:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
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 GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR027692; NF-L.
DR PANTHER; PTHR45652:SF8; PTHR45652:SF8; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
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 471..537
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..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
