P19527 (NFL_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neurofilament light polypeptide
Short name=NF-L

Alternative name(s):
68 kDa neurofilament protein
Neurofilament triplet L protein

Gene names

Name:	Nefl
Synonyms:	Nf68, Nfl

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber.
Subunit structure	Interacts with ARHGEF28 By similarity. Interacts with TRIM2 By similarity.
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.
Post-translational modification	O-glycosylated; contains three N-acetylglucosamine side chains. Ref.5 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.
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.
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Intermediate filament
Domain	Coiled coil
PTM	Acetylation Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intermediate filament bundle assembly Inferred from electronic annotation. Source: Compara locomotion Inferred from electronic annotation. Source: Compara microtubule cytoskeleton organization Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara neurofilament cytoskeleton organization Inferred from electronic annotation. Source: Compara neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara peripheral nervous system axon regeneration Inferred from electronic annotation. Source: Compara positive regulation of axonogenesis Inferred from electronic annotation. Source: Compara protein polymerization Inferred from direct assay PubMed 17157386. Source: RGD regulation of axon diameter Inferred from electronic annotation. Source: Compara response to corticosterone stimulus Inferred from expression pattern PubMed 17229084. Source: RGD response to peptide hormone stimulus Inferred from expression pattern PubMed 18157692. Source: RGD response to stress Inferred from expression pattern PubMed 17683840. Source: RGD response to toxin Inferred from expression pattern PubMed 18001836. Source: RGD
Cellular_component	axon Inferred from direct assay PubMed 8737171. Source: RGD growth cone Inferred from direct assay PubMed 12226091. Source: RGD neurofilament Inferred from electronic annotation. Source: Compara
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 542	541	Neurofilament light polypeptide		PRO_0000063790
Regions
	Region	2 – 93	92	Head
	Region	94 – 397	304	Rod
	Region	94 – 125	32	Coil 1A
	Region	126 – 138	13	Linker 1
	Region	139 – 234	96	Coil 1B
	Region	235 – 253	19	Linker 12
	Region	254 – 272	19	Coil 2A
	Region	273 – 281	9	Linker 2
	Region	282 – 397	116	Coil 2B
	Region	382 – 392	11	Epitope; recognized by IF-specific monoclonal antibody
	Region	398 – 542	145	Tail
	Region	398 – 444	47	Tail, subdomain A
	Region	445 – 542	98	Tail, subdomain B (acidic)
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.4 Ref.6
	Modified residue	43	1	Phosphotyrosine By similarity
	Modified residue	56	1	Phosphoserine By similarity
	Modified residue	67	1	Phosphoserine By similarity
	Modified residue	425	1	Phosphotyrosine By similarity
	Modified residue	433	1	Phosphotyrosine By similarity
	Modified residue	473	1	Phosphoserine By similarity
	Modified residue	531	1	Phosphoserine By similarity
	Glycosylation	21	1	O-linked (GlcNAc) Ref.5		CAR_000128
	Glycosylation	27	1	O-linked (GlcNAc) Ref.5		CAR_000129
Experimental info
	Sequence conflict	198 – 203	6	GADEAA → KARMSS in AAA41694. Ref.2
	Sequence conflict	400	1	R → K in AAA41694. Ref.2
	Sequence conflict	477	1	A → E in AAA41694. Ref.2
	Sequence conflict	481 – 484	4	EKEK → KKDE in AAA41694. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P19527 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1FCC739AF23BCCA8	FASTA	542	61,335
	10 20 30 40 50 60 MSSFSYEPYF STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS 70 80 90 100 110 120 SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR FASFIERVHE LEQQNKVLEA 130 140 150 160 170 180 ELLVLRQKHS EPSRFRALYE QEIRDLRLAA EDATNEKQAL QGEREGLEET LRNLQARYEE 190 200 210 220 230 240 EVLSREDAEG RLMEARKGAD EAALARAELE KRIDSLMDEI AFLKKVHEEE IAELQAQIQY 250 260 270 280 290 300 AQISVEMDVS SKPDLSAALK DIRAQYEKLA AKNMQNAEEW FKSRFTVLTE SAAKNTDAVR 310 320 330 340 350 360 AAKDEVSESR RLLKAKTLEI EACRGMNEAL EKQLQELEDK QNADISAMQD TINKLENELR 370 380 390 400 410 420 STKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR LSFTSVGSIT SGYSQSSQVF 430 440 450 460 470 480 GRSAYSGLQS SSYLMSARAF PAYYTSHVQE EQSEVEETIE ATKAEEAKDE PPSEGEAEEE 490 500 510 520 530 540 EKEKEEGEEE EGAEEEEAAK DESEDAKEEE GGEGEEEDTK ESEEEEKKEE SAGEEQAAKK KD

References

[1]	"Expression of rat neurofilament proteins NF-L and NF-M in transfected non-neuronal cells." Chin S.S., Liem R.K.H. Eur. J. Cell Biol. 50:475-490(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of a cDNA encoding the smallest neurofilament protein from the rat." Julien J.-P., Ramachandran K., Grosveld F. Biochim. Biophys. Acta 825:398-404(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-484.
[3]	"Characterization of the rat light neurofilament (NF-L) gene promoter and identification of NGF and cAMP responsive regions." Reeben M., Neuman T., Palgi J., Palm K., Paalme V., Saarma M. J. Neurosci. Res. 40:177-188(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[4]	Lubec G., Pradeep J.J.P., Afjehi-Sadat L., Diao W., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14; 38-54; 56-84; 92-107; 117-126; 148-157; 165-172; 212-224; 273-282; 285-294; 368-379; 381-391; 393-422 AND 439-463, ACETYLATION AT SER-2, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
[5]	"Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M." Dong D.L.-Y., Xu Z.-S., Chevrier M.R., Cotter R.J., Cleveland D.W., Hart G.W. J. Biol. Chem. 268:16679-16687(1993) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-21 AND SER-27.
[6]	Lubec G., Chen W.-Q. Submitted (FEB-2007) to UniProtKB Cited for: ACETYLATION AT SER-2, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF031880 mRNA. Translation: AAB87069.1. M25638 mRNA. Translation: AAA41694.1. X53981 Genomic DNA. Translation: CAA37931.1.
IPI	IPI00231302.
PIR	A21762. I60434.
RefSeq	NP_113971.1. NM_031783.1.
UniGene	Rn.18568.
3D structure databases
ProteinModelPortal	P19527.
SMR	P19527. Positions 88-124, 324-396.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1N.
IntAct	P19527. 1 interaction.
STRING	10116.ENSRNOP00000018599.
PTM databases
GlycoSuiteDB	P19527.
PhosphoSite	P19527.
2D gel databases
World-2DPAGE	0004:P19527.
Proteomic databases
PaxDb	P19527.
PRIDE	P19527.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000018599; ENSRNOP00000018599; ENSRNOG00000013658.
GeneID	83613.
KEGG	rno:83613.
UCSC	RGD:621458. rat.
Organism-specific databases
CTD	4747.
RGD	621458. Nefl.
Phylogenomic databases
eggNOG	NOG145720.
GeneTree	ENSGT00690000102043.
HOGENOM	HOG000230977.
HOVERGEN	HBG013015.
InParanoid	P19527.
KO	K04572.
OMA	PRVHISS.
OrthoDB	EOG42Z4QC.
Gene expression databases
Genevestigator	P19527.
GermOnline	ENSRNOG00000013658. Rattus norvegicus.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR006821. Intermed_filament_DNA-bd. IPR018039. Intermediate_filament_CS. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. PF04732. Filament_head. 1 hit. [Graphical view]
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	616157.

Entry information

Entry name

NFL_RAT

Accession

Primary (citable) accession number: P19527
Secondary accession number(s): Q63367

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program