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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
  • neuronal postsynaptic density Source: MGI
  • neuron projection Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 848847Neurofilament medium polypeptidePRO_0000063795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei30 – 301PhosphoserineBy similarity
Glycosylationi47 – 471O-linked (GlcNAc)1 Publication
Modified residuei97 – 971PhosphoserineCombined sources
Modified residuei224 – 2241PhosphoserineCombined sources
Modified residuei318 – 3181PhosphotyrosineCombined sources
Modified residuei344 – 3441PhosphoserineBy similarity
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei428 – 4281PhosphoserineBy similarity
Glycosylationi430 – 4301O-linked (GlcNAc)1 Publication
Modified residuei466 – 4661PhosphoserineBy similarity
Modified residuei482 – 4821PhosphoserineBy similarity
Modified residuei502 – 5021PhosphoserineBy similarity
Modified residuei506 – 5061PhosphoserineBy similarity
Modified residuei537 – 5371PhosphoserineBy similarity
Modified residuei545 – 5451PhosphoserineBy similarity
Modified residuei550 – 5501PhosphoserineCombined sources
Modified residuei551 – 5511PhosphoserineCombined sources
Modified residuei565 – 5651PhosphothreonineCombined sources
Modified residuei605 – 6051PhosphoserineCombined sources
Modified residuei610 – 6101PhosphoserineCombined sources
Modified residuei642 – 6421PhosphothreonineCombined sources
Modified residuei645 – 6451PhosphoserineBy similarity
Modified residuei669 – 6691PhosphoserineCombined sources
Modified residuei689 – 6891PhosphoserineBy similarity
Modified residuei715 – 7151PhosphoserineCombined sources
Modified residuei723 – 7231PhosphoserineCombined sources
Modified residuei753 – 7531PhosphoserineBy similarity
Modified residuei769 – 7691PhosphoserineCombined sources

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, Phosphoprotein

Proteomic databases

EPDiP08553.
MaxQBiP08553.
PaxDbiP08553.
PeptideAtlasiP08553.
PRIDEiP08553.

2D gel databases

UCD-2DPAGEP08553.

PTM databases

iPTMnetiP08553.
PhosphoSiteiP08553.
SwissPalmiP08553.

Expressioni

Gene expression databases

BgeeiP08553.
CleanExiMM_NEFM.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

DisProtiDP00362.
ProteinModelPortaliP08553.
SMRiP08553. Positions 98-247, 263-332, 337-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 102101HeadAdd
BLAST
Regioni103 – 410308RodAdd
BLAST
Regioni103 – 13432Coil 1AAdd
BLAST
Regioni135 – 14713Linker 1Add
BLAST
Regioni148 – 24699Coil 1BAdd
BLAST
Regioni247 – 26317Linker 12Add
BLAST
Regioni264 – 28522Coil 2AAdd
BLAST
Regioni286 – 2894Linker 2
Regioni290 – 410121Coil 2BAdd
BLAST
Regioni411 – 848438TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOVERGENiHBG013015.
InParanoidiP08553.
KOiK04573.
OrthoDBiEOG7FV3Q8.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171V → VP in CAA29127 (PubMed:3036526).Curated
Sequence conflicti53 – 531K → T in CAA29127 (PubMed:3036526).Curated
Sequence conflicti57 – 571L → V in CAA29127 (PubMed:3036526).Curated
Sequence conflicti234 – 2341S → R in CAA29127 (PubMed:3036526).Curated
Sequence conflicti432 – 4321S → F in AAA39815 (PubMed:3103856).Curated
Sequence conflicti539 – 5402QA → RR in AAA39815 (PubMed:3103856).Curated
Sequence conflicti628 – 6281Q → H in ABA46749 (Ref. 2) Curated
Sequence conflicti628 – 6281Q → H in BAC34724 (PubMed:16141072).Curated
Sequence conflicti628 – 6281Q → H in BAE37734 (PubMed:16141072).Curated
Sequence conflicti696 – 6961E → K in BAC34724 (PubMed:16141072).Curated
Sequence conflicti699 – 6991P → L in ABA46749 (Ref. 2) Curated
Sequence conflicti699 – 6991P → L in BAC34724 (PubMed:16141072).Curated

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. Positions 98-247, 263-332, 337-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP08553.
PhosphoSiteiP08553.
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.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP08553.
TreeFamiTF330122.

Miscellaneous databases

PROiP08553.
SOURCEiSearch...

Gene expression databases

BgeeiP08553.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and evolutionary origin of the gene encoding mouse NF-M, the middle-molecular-mass neurofilament protein."
    Levy E., Liem R.K.H., D'Eustachio P., Cowan N.J.
    Eur. J. Biochem. 166:71-77(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Jensen K.H., Brown A.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cerebellum.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye and Spinal ganglion.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-848.
  5. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 167-182; 222-233 AND 410-425, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  6. "Cloning and developmental expression of the murine neurofilament gene family."
    Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F.
    Brain Res. 387:243-250(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 322-540.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610; THR-642; SER-669 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
    Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND THR-430.
    Tissue: Brain.
  10. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  11. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-224; SER-550; SER-551; THR-565; SER-605; SER-610; SER-715; SER-723 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Lung.

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: July 6, 2016
This is version 164 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.