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Neurofilament light polypeptide (NF-L) (68 kDa neurofilament protein) (Micro glutamic acid-rich protein) (Neurofilament triplet L protein)

 NFL_BOVIN               Reviewed;         555 AA.
P02548; P79127; Q17QQ0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 152.
RecName: Full=Neurofilament light polypeptide;
Short=NF-L;
AltName: Full=68 kDa neurofilament protein;
AltName: Full=Micro glutamic acid-rich protein;
AltName: Full=Neurofilament triplet L protein;
Name=NEFL;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Holstein; TISSUE=Brain;
Hill W.D., Zhang L., Balin B.J., Sprinkle T.J.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Basal ganglia;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 469-555.
PubMed=3884373; DOI=10.1016/0014-5793(85)80339-2;
Isobe T., Okuyama T.;
"Brain micro glutamic acid-rich protein is the C-terminal endpiece of
the neurofilament 68-kDa protein as determined by the primary
sequence.";
FEBS Lett. 182:389-392(1985).
[4]
ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-56; SER-67 AND SER-473,
AND MASS SPECTROMETRY.
PubMed=14967049; DOI=10.1021/bi030196q;
Trimpin S., Mixon A.E., Stapels M.D., Kim M.Y., Spencer P.S.,
Deinzer M.L.;
"Identification of endogenous phosphorylation sites of bovine medium
and low molecular weight neurofilament proteins by tandem mass
spectrometry.";
Biochemistry 43:2091-2105(2004).
-!- FUNCTION: Neurofilaments usually contain three intermediate
filament proteins: L, M, and H which are involved in the
maintenance of neuronal caliber.
-!- SUBUNIT: Interacts with ARHGEF28. Interacts with TRIM2.
{ECO:0000250}.
-!- DOMAIN: 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.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- PTM: Phosphorylated in the head and rod regions by the PKC kinase
PKN1, leading to the inhibition of polymerization. {ECO:0000250}.
-!- PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1.
{ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=62600; Method=MALDI; Range=2-555;
Evidence={ECO:0000269|PubMed:14967049};
-!- 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.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; U83919; AAB41543.1; -; mRNA.
EMBL; BC118240; AAI18241.1; -; mRNA.
PIR; JW0094; JW0094.
RefSeq; NP_776546.1; NM_174121.1.
UniGene; Bt.89013; -.
ProteinModelPortal; P02548; -.
SMR; P02548; -.
IntAct; P02548; 1.
STRING; 9913.ENSBTAP00000029264; -.
iPTMnet; P02548; -.
PaxDb; P02548; -.
PeptideAtlas; P02548; -.
PRIDE; P02548; -.
Ensembl; ENSBTAT00000029264; ENSBTAP00000029264; ENSBTAG00000021949.
GeneID; 281348; -.
KEGG; bta:281348; -.
CTD; 4747; -.
VGNC; VGNC:31986; NEFL.
eggNOG; ENOG410IGME; Eukaryota.
eggNOG; ENOG410XPTM; LUCA.
GeneTree; ENSGT00910000143989; -.
HOGENOM; HOG000230977; -.
HOVERGEN; HBG013015; -.
InParanoid; P02548; -.
KO; K04572; -.
OMA; EMDVSSK; -.
OrthoDB; EOG091G12MK; -.
TreeFam; TF330122; -.
Reactome; R-BTA-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-BTA-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-BTA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-BTA-5673001; RAF/MAP kinase cascade.
Proteomes; UP000009136; Chromosome 8.
Bgee; ENSBTAG00000021949; -.
GO; GO:0030424; C:axon; ISS:AgBase.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005882; C:intermediate filament; ISS:AgBase.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005883; C:neurofilament; ISS:AgBase.
GO; GO:0033596; C:TSC1-TSC2 complex; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
GO; GO:0045110; P:intermediate filament bundle assembly; ISS:AgBase.
GO; GO:0045109; P:intermediate filament organization; ISS:AgBase.
GO; GO:0040011; P:locomotion; ISS:AgBase.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:AgBase.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:AgBase.
GO; GO:0033693; P:neurofilament bundle assembly; ISS:UniProtKB.
GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:AgBase.
GO; GO:0050885; P:neuromuscular process controlling balance; ISS:AgBase.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:AgBase.
GO; GO:0014012; P:peripheral nervous system axon regeneration; ISS:AgBase.
GO; GO:0050772; P:positive regulation of axonogenesis; ISS:AgBase.
GO; GO:0031133; P:regulation of axon diameter; ISS:AgBase.
GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR027692; NF-L.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF22; PTHR23239:SF22; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome;
Direct protein sequencing; Glycoprotein; Intermediate filament;
Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:14967049}.
CHAIN 2 555 Neurofilament light polypeptide.
/FTId=PRO_0000063786.
DOMAIN 90 401 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 93 Head.
REGION 94 125 Coil 1A.
REGION 126 138 Linker 1.
REGION 139 234 Coil 1B.
REGION 235 253 Linker 12.
REGION 254 272 Coil 2A.
REGION 273 281 Linker 2.
REGION 282 397 Coil 2B.
REGION 398 555 Tail.
REGION 398 444 Tail, subdomain A.
REGION 445 555 Tail, subdomain B (acidic).
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:14967049}.
MOD_RES 23 23 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P08551}.
MOD_RES 23 23 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P08551}.
MOD_RES 30 30 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P08551}.
MOD_RES 43 43 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08551}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000269|PubMed:14967049}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000269|PubMed:14967049}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000250|UniProtKB:P19527}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000269|PubMed:14967049}.
MOD_RES 532 532 Phosphothreonine.
{ECO:0000250|UniProtKB:P19527}.
CONFLICT 495 501 Missing (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 510 510 A -> AEA (in Ref. 3; AA sequence).
{ECO:0000305}.
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


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