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P12839 (NFM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurofilament medium polypeptide

Short name=NF-M
Alternative name(s):
160 kDa neurofilament protein
Neurofilament 3
Neurofilament triplet M protein
Gene names
Name:Nefm
Synonyms:Nef3, Nfm
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length846 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Post-translational modification

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. Ref.4

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. Ref.4

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 846845Neurofilament medium polypeptide
PRO_0000063798

Regions

Region2 – 104103Head
Region104 – 411308Rod
Region104 – 13532Coil 1A
Region136 – 14813Linker 1
Region149 – 24799Coil 1B
Region248 – 26417Linker 12
Region265 – 28622Coil 2A
Region287 – 2904Linker 2
Region291 – 411121Coil 2B
Region412 – 845434Tail

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue3191Phosphotyrosine By similarity
Modified residue5031Phosphoserine Ref.4
Modified residue5071Phosphoserine Ref.4
Modified residue5371Phosphoserine Ref.4
Modified residue5451Phosphoserine By similarity
Modified residue5511Phosphoserine By similarity
Modified residue6041Phosphoserine Ref.4
Modified residue6091Phosphoserine Ref.4
Modified residue6431Phosphoserine By similarity
Modified residue6671Phosphoserine Ref.4
Modified residue6871Phosphoserine By similarity
Modified residue7131Phosphoserine By similarity
Modified residue7671Phosphoserine By similarity
Glycosylation481O-linked (GlcNAc) Ref.5
CAR_000130
Glycosylation4311O-linked (GlcNAc) Ref.5
CAR_000131

Experimental info

Sequence conflict181Missing in CAA78136. Ref.2
Sequence conflict221R → P in CAA78136. Ref.2
Sequence conflict2051V → L in CAA78136. Ref.2
Sequence conflict5011Missing in AAA41696. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P12839 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 14DE91A1D1F68EC8

FASTA84695,791
        10         20         30         40         50         60 
MSYTLDSLGN PSAYRRVPTE TRSSFSRVSG SPSSGFRSQS WSRGSPSTVS SSYKRSALAP 

        70         80         90        100        110        120 
RLAYSSAMLS SAESSLDFSQ SSSLLNGGSG GDYKLSRSNE KEQLQGLNDR FAGYIEKVHY 

       130        140        150        160        170        180 
LEQQNKEIEA EIHALRQKQA SHAQLGDAYD QEIRELRATL EMVNHEKAQV QLDSDHLEED 

       190        200        210        220        230        240 
IHRLKERFEE EARLRDDTEA AIRAVRKDIE ESSMVKVELD KKVQSLQDEV AFLRSNHEEE 

       250        260        270        280        290        300 
VADLLAQIQA SHITVERKDY LKTDISTALK EIRSQLECHS DQNMHQAEEW FKCRYAKLTE 

       310        320        330        340        350        360 
AAEQNKEAIR SAKEEIAEYR RQLQSKSIEL ESVRGTKESL ERQLSDIEER HNHDLSSYQD 

       370        380        390        400        410        420 
TIQQLENELR GTKWEMARHL REYQDLLNVK MALDIEIAAY RKLLEGEETR FSTFSGSITG 

       430        440        450        460        470        480 
PLYTHRQPSV TISSKIQKTK VEAPKLKVQH KFVEEIIEET KVEDEKSEME DALTVIAEEL 

       490        500        510        520        530        540 
AASAKEEKEE AEEKEEEPEV EKSPVKSPEA KEEEEGEKEE EEEGQEEEEE EDEGVKSDQA 

       550        560        570        580        590        600 
EEGGSEKEGS SEKDEGEQEE EGETEAEGEG EEAEAKEEKK TEGKVEEMAI KEEIKVEKPE 

       610        620        630        640        650        660 
KAKSPVPKSP VEEVKPKPEA KAGKDEQKEE EKVEEKKEVA KESPKEEKVE KKEEKPKDVP 

       670        680        690        700        710        720 
DKKKAESPVK EKAVEEMITI TKSVKVSLEK DTKEEKPQQQ EKVKEKAEEE GGSEEEVGDK 

       730        740        750        760        770        780 
SPQESKKEDI AINGEVEGKE EEEQETQEKG SGQEEEKGVV TNGLDVSPAE EKKGEDRSDD 

       790        800        810        820        830        840 
KVVVTKKVEK ITSEGGDGAT KYITKSVTVT QKVEEHEETF EEKLVSTKKV EKVTSHAIVK 


EVTQGD 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18628 mRNA. Translation: AAA41696.1.
Z12152 mRNA. Translation: CAA78136.1.
PIRA45669.
RefSeqNP_058725.1. NM_017029.2.
UniGeneRn.10971.

3D structure databases

ProteinModelPortalP12839.
SMRP12839. Positions 98-135, 329-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246731. 3 interactions.
DIPDIP-208N.
STRING10116.ENSRNOP00000018637.

PTM databases

PhosphoSiteP12839.
UniCarbKBP12839.

2D gel databases

World-2DPAGE0004:P12839.

Proteomic databases

PaxDbP12839.
PRIDEP12839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24588.
KEGGrno:24588.
UCSCRGD:3160. rat.

Organism-specific databases

CTD4741.
RGD3160. Nefm.

Phylogenomic databases

eggNOGNOG264891.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP12839.
KOK04573.
PhylomeDBP12839.

Gene expression databases

GenevestigatorP12839.

Family and domain databases

InterProIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR027697. NF-M.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF19. PTHR23239:SF19. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603770.
PROP12839.

Entry information

Entry nameNFM_RAT
AccessionPrimary (citable) accession number: P12839
Secondary accession number(s): Q63370
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families