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Protein

Neurofilament medium polypeptide

Gene

Nefm

Organism
Mus musculus (Mouse)
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

GO - Biological processi

  • axo-dendritic transport Source: MGI
  • axon development Source: InterPro
  • intermediate filament bundle assembly Source: MGI
  • intermediate filament cytoskeleton organization Source: MGI
  • microtubule cytoskeleton organization Source: MGI
  • neurofilament cytoskeleton organization Source: MGI
  • regulation of axon diameter Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97314. Nefm.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • myelin sheath Source: UniProtKB
  • neurofilament Source: MGI
  • neuromuscular junction Source: MGI
  • neuron projection Source: MGI
  • postsynaptic density Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000637952 – 848Neurofilament medium polypeptideAdd BLAST847

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei30PhosphoserineBy similarity1
Modified residuei42Omega-N-methylarginineCombined sources1
Glycosylationi47O-linked (GlcNAc)1 Publication1
Modified residuei97PhosphoserineCombined sources1
Modified residuei224PhosphoserineCombined sources1
Modified residuei318PhosphotyrosineCombined sources1
Modified residuei344PhosphoserineBy similarity1
Modified residuei416PhosphoserineBy similarity1
Modified residuei428PhosphoserineBy similarity1
Glycosylationi430O-linked (GlcNAc)1 Publication1
Modified residuei466PhosphoserineBy similarity1
Modified residuei482PhosphoserineBy similarity1
Modified residuei502PhosphoserineBy similarity1
Modified residuei506PhosphoserineBy similarity1
Modified residuei537PhosphoserineBy similarity1
Modified residuei545PhosphoserineBy similarity1
Modified residuei550PhosphoserineCombined sources1
Modified residuei551PhosphoserineCombined sources1
Modified residuei565PhosphothreonineCombined sources1
Modified residuei605PhosphoserineCombined sources1
Modified residuei610PhosphoserineCombined sources1
Modified residuei642PhosphothreonineCombined sources1
Modified residuei645PhosphoserineBy similarity1
Modified residuei669PhosphoserineCombined sources1
Modified residuei689PhosphoserineBy similarity1
Modified residuei715PhosphoserineCombined sources1
Modified residuei723PhosphoserineCombined sources1
Modified residuei753PhosphoserineBy similarity1
Modified residuei769PhosphoserineCombined sources1

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.
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.
Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

EPDiP08553.
MaxQBiP08553.
PaxDbiP08553.
PeptideAtlasiP08553.
PRIDEiP08553.

2D gel databases

UCD-2DPAGEP08553.

PTM databases

iPTMnetiP08553.
PhosphoSitePlusiP08553.
SwissPalmiP08553.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022054.
CleanExiMM_NEFM.

Interactioni

Protein-protein interaction databases

BioGridi201758. 3 interactors.
IntActiP08553. 7 interactors.
MINTiMINT-4111839.
STRINGi10090.ENSMUSP00000022638.

Structurei

3D structure databases

DisProtiDP00362.
ProteinModelPortaliP08553.
SMRiP08553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 102HeadAdd BLAST101
Regioni103 – 410RodAdd BLAST308
Regioni103 – 134Coil 1AAdd BLAST32
Regioni135 – 147Linker 1Add BLAST13
Regioni148 – 246Coil 1BAdd BLAST99
Regioni247 – 263Linker 12Add BLAST17
Regioni264 – 285Coil 2AAdd BLAST22
Regioni286 – 289Linker 24
Regioni290 – 410Coil 2BAdd BLAST121
Regioni411 – 848TailAdd BLAST438

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOVERGENiHBG013015.
InParanoidiP08553.
KOiK04573.
PhylomeDBiP08553.
TreeFamiTF330122.

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. 2 hits.
PTHR23239:SF19. PTHR23239:SF19. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08553-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYTLDSLGN PSAYRRVTET RSSFSRVSGS PSSGFRSQSW SRGSPSTVSS
60 70 80 90 100
SYKRSALAPR LAYSSAMLSS AESSLDFSQS SSLLNGGSGG DYKLSRSNEK
110 120 130 140 150
EQLQGLNDRF AGYIEKVHYL EQQNKEIEAE IQALRQKQAS HAQLGDAYDQ
160 170 180 190 200
EIRELRATLE MVNHEKAQVQ LDSDHLEEDI HRLKERFEEE ARLRDDTEAA
210 220 230 240 250
IRALRKDIEE SSMVKVELDK KVQSLQDEVA FLRSNHEEEV ADLLAQIQAS
260 270 280 290 300
HITVERKDYL KTDISTALKE IRSQLECHSD QNMHQAEEWF KCRYAKLTEA
310 320 330 340 350
AEQNKEAIRS AKEEIAEYRR QLQSKSIELE SVRGTKESLE RQLSDIEERH
360 370 380 390 400
NHDLSSYQDT IQQLENELRG TKWEMARHLR EYQDLLNVKM ALDIEIAAYR
410 420 430 440 450
KLLEGEETRF STFSGSITGP LYTHRQPSVT ISSKIQKTKV EAPKLKVQHK
460 470 480 490 500
FVEEIIEETK VEDEKSEMEE TLTAIAEELA ASAKEEKEEA EEKEEEPEAE
510 520 530 540 550
KSPVKSPEAK EEEEEGEKEE EEEGQEEEEE EDEGVKSDQA EEGGSEKEGS
560 570 580 590 600
SEKDEGEQEE EEGETEAEGE GEEAEAKEEK KIEGKVEEVA VKEEIKVEKP
610 620 630 640 650
EKAKSPMPKS PVEEVKPKPE AKAGKGEQKE EEKVEEEKKE VTKESPKEEK
660 670 680 690 700
VEKKEEKPKD VADKKKAESP VKEKAVEEVI TISKSVKVSL EKDTKEEKPQ
710 720 730 740 750
PQEKVKEKAE EEGGSEEEGS DRSPQESKKE DIAINGEVEG KEEEEQETQE
760 770 780 790 800
KGSGREEEKG VVTNGLDVSP AEEKKGEDSS DDKVVVTKKV EKITSEGGDG
810 820 830 840
ATKYITKSVT VTQKVEEHEE TFEEKLVSTK KVEKVTSHAI VKEVTQGD
Length:848
Mass (Da):95,916
Last modified:May 1, 2007 - v4
Checksum:i0783F50558A7D4C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17V → VP in CAA29127 (PubMed:3036526).Curated1
Sequence conflicti53K → T in CAA29127 (PubMed:3036526).Curated1
Sequence conflicti57L → V in CAA29127 (PubMed:3036526).Curated1
Sequence conflicti234S → R in CAA29127 (PubMed:3036526).Curated1
Sequence conflicti432S → F in AAA39815 (PubMed:3103856).Curated1
Sequence conflicti539 – 540QA → RR in AAA39815 (PubMed:3103856).Curated2
Sequence conflicti628Q → H in ABA46749 (Ref. 2) Curated1
Sequence conflicti628Q → H in BAC34724 (PubMed:16141072).Curated1
Sequence conflicti628Q → H in BAE37734 (PubMed:16141072).Curated1
Sequence conflicti696E → K in BAC34724 (PubMed:16141072).Curated1
Sequence conflicti699P → L in ABA46749 (Ref. 2) Curated1
Sequence conflicti699P → L in BAC34724 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05640 Genomic DNA. Translation: CAA29127.1.
DQ201636 mRNA. Translation: ABA46749.1.
AK051696 mRNA. Translation: BAC34724.1.
AK164318 mRNA. Translation: BAE37734.1.
AK165041 mRNA. Translation: BAE38014.1.
BC119602 mRNA. Translation: AAI19603.1.
BC128564 mRNA. Translation: AAI28565.1.
M20481 mRNA. Translation: AAA39815.1.
CCDSiCCDS27233.1.
PIRiB43772.
S00030.
RefSeqiNP_032717.2. NM_008691.2.
UniGeneiMm.242832.
Mm.390700.

Genome annotation databases

GeneIDi18040.
KEGGimmu:18040.
UCSCiuc007ulo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05640 Genomic DNA. Translation: CAA29127.1.
DQ201636 mRNA. Translation: ABA46749.1.
AK051696 mRNA. Translation: BAC34724.1.
AK164318 mRNA. Translation: BAE37734.1.
AK165041 mRNA. Translation: BAE38014.1.
BC119602 mRNA. Translation: AAI19603.1.
BC128564 mRNA. Translation: AAI28565.1.
M20481 mRNA. Translation: AAA39815.1.
CCDSiCCDS27233.1.
PIRiB43772.
S00030.
RefSeqiNP_032717.2. NM_008691.2.
UniGeneiMm.242832.
Mm.390700.

3D structure databases

DisProtiDP00362.
ProteinModelPortaliP08553.
SMRiP08553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201758. 3 interactors.
IntActiP08553. 7 interactors.
MINTiMINT-4111839.
STRINGi10090.ENSMUSP00000022638.

PTM databases

iPTMnetiP08553.
PhosphoSitePlusiP08553.
SwissPalmiP08553.

2D gel databases

UCD-2DPAGEP08553.

Proteomic databases

EPDiP08553.
MaxQBiP08553.
PaxDbiP08553.
PeptideAtlasiP08553.
PRIDEiP08553.

Protocols and materials databases

DNASUi18040.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18040.
KEGGimmu:18040.
UCSCiuc007ulo.1. mouse.

Organism-specific databases

CTDi4741.
MGIiMGI:97314. Nefm.

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOVERGENiHBG013015.
InParanoidiP08553.
KOiK04573.
PhylomeDBiP08553.
TreeFamiTF330122.

Miscellaneous databases

PROiP08553.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022054.
CleanExiMM_NEFM.

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. 2 hits.
PTHR23239:SF19. PTHR23239:SF19. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNFM_MOUSE
AccessioniPrimary (citable) accession number: P08553
Secondary accession number(s): A2VCT5
, Q0VDM8, Q3HRJ6, Q3TNS4, Q3TPK2, Q61961, Q8BQ20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 2007
Last modified: November 2, 2016
This is version 167 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.