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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
Proteomesi
  • UP000002494 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)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)1 Publication1
Modified residuei98PhosphoserineBy similarity1
Modified residuei225PhosphoserineBy similarity1
Modified residuei319PhosphotyrosineBy similarity1
Modified residuei345PhosphoserineCombined sources1
Modified residuei417PhosphoserineCombined sources1
Modified residuei429PhosphoserineCombined sources1
GlycosylationiCAR_000131431O-linked (GlcNAc)1 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-2DPAGE0004:P12839.

PTM databases

iPTMnetiP12839.
PhosphoSitePlusiP12839.
UniCarbKBiP12839.

Interactioni

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

BioGridi246731. 3 interactors.
DIPiDIP-208N.
STRINGi10116.ENSRNOP00000065853.

Structurei

3D structure databases

ProteinModelPortaliP12839.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 104HeadAdd BLAST103
Regioni104 – 411RodAdd BLAST308
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.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
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. 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.

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.

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246731. 3 interactors.
DIPiDIP-208N.
STRINGi10116.ENSRNOP00000065853.

PTM databases

iPTMnetiP12839.
PhosphoSitePlusiP12839.
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

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP12839.
KOiK04573.
PhylomeDBiP12839.

Miscellaneous databases

PROiP12839.

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_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: November 2, 2016
This is version 142 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

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.