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Protein

Neurofilament medium polypeptide

Gene

Nefm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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
  • 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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3160 Nefm

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000637982 – 846Neurofilament medium polypeptideAdd BLAST845

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei31PhosphoserineCombined sources1
Modified residuei43Omega-N-methylarginineBy similarity1
GlycosylationiCAR_00013048O-linked (GlcNAc) threonine1 Publication1
Modified residuei98PhosphoserineBy similarity1
Modified residuei225PhosphoserineBy similarity1
Modified residuei319PhosphotyrosineBy similarity1
Modified residuei345PhosphoserineCombined sources1
Modified residuei417PhosphoserineCombined sources1
Modified residuei429PhosphoserineCombined sources1
GlycosylationiCAR_000131431O-linked (GlcNAc) threonine1 Publication1
Modified residuei467PhosphoserineCombined sources1
Modified residuei483PhosphoserineCombined sources1
Modified residuei503PhosphoserineCombined sources1 Publication1
Modified residuei507PhosphoserineCombined sources1 Publication1
Modified residuei537PhosphoserineCombined sources1 Publication1
Modified residuei545PhosphoserineCombined sources1
Modified residuei550PhosphoserineCombined sources1
Modified residuei551PhosphoserineCombined sources1
Modified residuei564PhosphothreonineCombined sources1
Modified residuei604PhosphoserineCombined sources1 Publication1
Modified residuei609PhosphoserineCombined sources1 Publication1
Modified residuei643PhosphoserineCombined sources1
Modified residuei667PhosphoserineCombined sources1 Publication1
Modified residuei687PhosphoserineBy similarity1
Modified residuei713PhosphoserineCombined sources1
Modified residuei721PhosphoserineCombined sources1
Modified residuei751PhosphoserineCombined sources1
Modified residuei767PhosphoserineCombined 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.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, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP12839
PRIDEiP12839

2D gel databases

World-2DPAGEi0004:P12839

PTM databases

GlyConnecti432
iPTMnetiP12839
PhosphoSitePlusiP12839
UniCarbKBiP12839

Interactioni

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi246731, 3 interactors
DIPiDIP-208N
STRINGi10116.ENSRNOP00000065853

Structurei

3D structure databases

ProteinModelPortaliP12839
SMRiP12839
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini100 – 411IF rodPROSITE-ProRule annotationAdd BLAST312

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 104HeadAdd BLAST103
Regioni104 – 135Coil 1AAdd BLAST32
Regioni136 – 148Linker 1Add BLAST13
Regioni149 – 247Coil 1BAdd BLAST99
Regioni248 – 264Linker 12Add BLAST17
Regioni265 – 286Coil 2AAdd BLAST22
Regioni287 – 290Linker 24
Regioni291 – 411Coil 2BAdd BLAST121
Regioni412 – 845TailAdd BLAST434

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGME Eukaryota
ENOG410XPTM LUCA
HOGENOMiHOG000230977
HOVERGENiHBG013015
InParanoidiP12839
KOiK04573
PhylomeDBiP12839

Family and domain databases

InterProiView protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR006821 Intermed_filament_DNA-bd
IPR002957 Keratin_I
IPR027697 NF-M
PANTHERiPTHR23239 PTHR23239, 3 hits
PTHR23239:SF19 PTHR23239:SF19, 3 hits
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PF04732 Filament_head, 1 hit
PRINTSiPR01248 TYPE1KERATIN
SMARTiView protein in SMART
SM01391 Filament, 1 hit
PROSITEiView protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti18Missing in CAA78136 (PubMed:1321159).Curated1
Sequence conflicti22R → P in CAA78136 (PubMed:1321159).Curated1
Sequence conflicti205V → L in CAA78136 (PubMed:1321159).Curated1
Sequence conflicti501Missing in AAA41696 (PubMed:2441012).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiNFM_RAT
AccessioniPrimary (citable) accession number: P12839
Secondary accession number(s): Q63370
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 149 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health