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Protein

Neurofilament medium polypeptide

Gene

Nefm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber.

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD
  • structural molecule activity Source: InterPro
  • toxic substance binding Source: RGD

GO - Biological processi

  • axon regeneration Source: RGD
  • cellular response to estradiol stimulus Source: RGD
  • cellular response to oxidative stress Source: RGD
  • cerebral cortex development Source: RGD
  • hippocampus development Source: RGD
  • intermediate filament polymerization or depolymerization Source: RGD
  • neurofilament bundle assembly Source: RGD
  • response to acrylamide Source: RGD
  • spinal cord development Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Neurofilament medium polypeptide
Short name:
NF-M
Alternative name(s):
160 kDa neurofilament protein
Neurofilament 3
Neurofilament triplet M protein
Gene namesi
Name:Nefm
Synonyms:Nef3, Nfm
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3160. Nefm.

Subcellular locationi

GO - Cellular componenti

  • axon Source: BHF-UCL
  • cytoskeleton Source: UniProtKB
  • intermediate filament Source: RGD
  • neurofilament Source: RGD
  • perikaryon Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 846845Neurofilament medium polypeptidePRO_0000063798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Glycosylationi48 – 481O-linked (GlcNAc)1 PublicationCAR_000130
Modified residuei319 – 3191PhosphotyrosineBy similarity
Glycosylationi431 – 4311O-linked (GlcNAc)1 PublicationCAR_000131
Modified residuei503 – 5031Phosphoserine1 Publication
Modified residuei507 – 5071Phosphoserine1 Publication
Modified residuei537 – 5371Phosphoserine1 Publication
Modified residuei545 – 5451PhosphoserineBy similarity
Modified residuei551 – 5511PhosphoserineBy similarity
Modified residuei604 – 6041Phosphoserine1 Publication
Modified residuei609 – 6091Phosphoserine1 Publication
Modified residuei643 – 6431PhosphoserineBy similarity
Modified residuei667 – 6671Phosphoserine1 Publication
Modified residuei687 – 6871PhosphoserineBy similarity
Modified residuei713 – 7131PhosphoserineBy similarity
Modified residuei767 – 7671PhosphoserineBy similarity

Post-translational modificationi

There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.1 Publication
Phosphorylation seems to play a major role in the functioning of the larger neurofilament polypeptides (NF-M and NF-H), the levels of phosphorylation being altered developmentally and coincidentally with a change in the neurofilament function.1 Publication
Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP12839.
PRIDEiP12839.

2D gel databases

World-2DPAGE0004:P12839.

PTM databases

PhosphoSiteiP12839.
UniCarbKBiP12839.

Expressioni

Gene expression databases

GenevestigatoriP12839.

Interactioni

Protein-protein interaction databases

BioGridi246731. 3 interactions.
DIPiDIP-208N.
STRINGi10116.ENSRNOP00000018637.

Structurei

3D structure databases

ProteinModelPortaliP12839.
SMRiP12839. Positions 98-135, 329-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 104103HeadAdd
BLAST
Regioni104 – 411308RodAdd
BLAST
Regioni104 – 13532Coil 1AAdd
BLAST
Regioni136 – 14813Linker 1Add
BLAST
Regioni149 – 24799Coil 1BAdd
BLAST
Regioni248 – 26417Linker 12Add
BLAST
Regioni265 – 28622Coil 2AAdd
BLAST
Regioni287 – 2904Linker 2
Regioni291 – 411121Coil 2BAdd
BLAST
Regioni412 – 845434TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264891.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP12839.
KOiK04573.
PhylomeDBiP12839.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR027697. NF-M.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF19. PTHR23239:SF19. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12839-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYTLDSLGN PSAYRRVPTE TRSSFSRVSG SPSSGFRSQS WSRGSPSTVS
60 70 80 90 100
SSYKRSALAP RLAYSSAMLS SAESSLDFSQ SSSLLNGGSG GDYKLSRSNE
110 120 130 140 150
KEQLQGLNDR FAGYIEKVHY LEQQNKEIEA EIHALRQKQA SHAQLGDAYD
160 170 180 190 200
QEIRELRATL EMVNHEKAQV QLDSDHLEED IHRLKERFEE EARLRDDTEA
210 220 230 240 250
AIRAVRKDIE ESSMVKVELD KKVQSLQDEV AFLRSNHEEE VADLLAQIQA
260 270 280 290 300
SHITVERKDY LKTDISTALK EIRSQLECHS DQNMHQAEEW FKCRYAKLTE
310 320 330 340 350
AAEQNKEAIR SAKEEIAEYR RQLQSKSIEL ESVRGTKESL ERQLSDIEER
360 370 380 390 400
HNHDLSSYQD TIQQLENELR GTKWEMARHL REYQDLLNVK MALDIEIAAY
410 420 430 440 450
RKLLEGEETR FSTFSGSITG PLYTHRQPSV TISSKIQKTK VEAPKLKVQH
460 470 480 490 500
KFVEEIIEET KVEDEKSEME DALTVIAEEL AASAKEEKEE AEEKEEEPEV
510 520 530 540 550
EKSPVKSPEA KEEEEGEKEE EEEGQEEEEE EDEGVKSDQA EEGGSEKEGS
560 570 580 590 600
SEKDEGEQEE EGETEAEGEG EEAEAKEEKK TEGKVEEMAI KEEIKVEKPE
610 620 630 640 650
KAKSPVPKSP VEEVKPKPEA KAGKDEQKEE EKVEEKKEVA KESPKEEKVE
660 670 680 690 700
KKEEKPKDVP DKKKAESPVK EKAVEEMITI TKSVKVSLEK DTKEEKPQQQ
710 720 730 740 750
EKVKEKAEEE GGSEEEVGDK SPQESKKEDI AINGEVEGKE EEEQETQEKG
760 770 780 790 800
SGQEEEKGVV TNGLDVSPAE EKKGEDRSDD KVVVTKKVEK ITSEGGDGAT
810 820 830 840
KYITKSVTVT QKVEEHEETF EEKLVSTKKV EKVTSHAIVK EVTQGD
Length:846
Mass (Da):95,791
Last modified:January 23, 2007 - v4
Checksum:i14DE91A1D1F68EC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181Missing in CAA78136 (PubMed:1321159).Curated
Sequence conflicti22 – 221R → P in CAA78136 (PubMed:1321159).Curated
Sequence conflicti205 – 2051V → L in CAA78136 (PubMed:1321159).Curated
Sequence conflicti501 – 5011Missing in AAA41696 (PubMed:2441012).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18628 mRNA. Translation: AAA41696.1.
Z12152 mRNA. Translation: CAA78136.1.
PIRiA45669.
RefSeqiNP_058725.1. NM_017029.2.
UniGeneiRn.10971.

Genome annotation databases

GeneIDi24588.
KEGGirno:24588.
UCSCiRGD:3160. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18628 mRNA. Translation: AAA41696.1.
Z12152 mRNA. Translation: CAA78136.1.
PIRiA45669.
RefSeqiNP_058725.1. NM_017029.2.
UniGeneiRn.10971.

3D structure databases

ProteinModelPortaliP12839.
SMRiP12839. Positions 98-135, 329-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246731. 3 interactions.
DIPiDIP-208N.
STRINGi10116.ENSRNOP00000018637.

PTM databases

PhosphoSiteiP12839.
UniCarbKBiP12839.

2D gel databases

World-2DPAGE0004:P12839.

Proteomic databases

PaxDbiP12839.
PRIDEiP12839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24588.
KEGGirno:24588.
UCSCiRGD:3160. rat.

Organism-specific databases

CTDi4741.
RGDi3160. Nefm.

Phylogenomic databases

eggNOGiNOG264891.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP12839.
KOiK04573.
PhylomeDBiP12839.

Miscellaneous databases

NextBioi603770.
PROiP12839.

Gene expression databases

GenevestigatoriP12839.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR027697. NF-M.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF19. PTHR23239:SF19. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete amino acid sequence and in vitro expression of rat NF-M, the middle molecular weight neurofilament protein."
    Napolitano E.W., Chin S.S.M., Colman D.R., Liem R.K.H.
    J. Neurosci. 7:2590-2599(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Schwann cells of the myelin-forming phenotype express neurofilament protein NF-M."
    Kelly B.M., Gillespie C.S., Sherman D.L., Brophy P.J.
    J. Cell Biol. 118:397-410(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
  3. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 102-117; 139-154; 168-183; 207-216; 223-258; 352-371; 391-410; 412-427; 452-461 AND 686-693, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  4. "Identification of six phosphorylation sites in the COOH-terminal tail region of the rat neurofilament protein M."
    Xu Z.-S., Liu W.-S., Willard M.B.
    J. Biol. Chem. 267:4467-4471(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-503; SER-507; SER-537; SER-604; SER-609 AND SER-667, SEQUENCE REVISION TO 500.
  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-48 AND THR-431.
  6. Lubec G., Chen W.-Q.
    Submitted (FEB-2007) to UniProtKB
    Cited for: ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNFM_RAT
AccessioniPrimary (citable) accession number: P12839
Secondary accession number(s): Q63370
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.