P12839 (NFM_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 115.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Neurofilament medium polypeptide Short name=NF-M Alternative name(s): 160 kDa neurofilament protein Neurofilament 3 Neurofilament triplet M protein | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 846 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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, AND MASS SPECTROMETRY. |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Intermediate filament |
| Domain | Coiled coil |
| PTM | Acetylation Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | axon Inferred from direct assay PubMed 20118926. Source: BHF-UCL cytoskeletonInferred from direct assay Ref.2. Source: UniProtKB intermediate filamentInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | structural molecule activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 846 | 845 | Neurofilament medium polypeptide | PRO_0000063798 | |||||
Regions | |||||||||
| Region | 2 – 104 | 103 | Head | ||||||
| Region | 104 – 411 | 308 | Rod | ||||||
| Region | 104 – 135 | 32 | Coil 1A | ||||||
| Region | 136 – 148 | 13 | Linker 1 | ||||||
| Region | 149 – 247 | 99 | Coil 1B | ||||||
| Region | 248 – 264 | 17 | Linker 12 | ||||||
| Region | 265 – 286 | 22 | Coil 2A | ||||||
| Region | 287 – 290 | 4 | Linker 2 | ||||||
| Region | 291 – 411 | 121 | Coil 2B | ||||||
| Region | 412 – 845 | 434 | Tail | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.6 | ||||||
| Modified residue | 319 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 503 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 507 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 537 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 545 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 551 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 604 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 609 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 643 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 667 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 687 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 713 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 767 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 48 | 1 | O-linked (GlcNAc) Ref.5 | CAR_000130 | |||||
| Glycosylation | 431 | 1 | O-linked (GlcNAc) Ref.5 | CAR_000131 | |||||
Experimental info | |||||||||
| Sequence conflict | 18 | 1 | Missing in CAA78136. Ref.2 | ||||||
| Sequence conflict | 22 | 1 | R → P in CAA78136. Ref.2 | ||||||
| Sequence conflict | 205 | 1 | V → L in CAA78136. Ref.2 | ||||||
| Sequence conflict | 501 | 1 | Missing in AAA41696. Ref.1 | ||||||
Sequences
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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, 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, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M18628 mRNA. Translation: AAA41696.1. Z12152 mRNA. Translation: CAA78136.1. |
| IPI | IPI00325609. |
| PIR | A45669. |
| RefSeq | NP_058725.1. NM_017029.2. |
| UniGene | Rn.10971. |
3D structure databases | |
| ProteinModelPortal | P12839. |
| SMR | P12839. Positions 98-135, 329-406. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-208N. |
| STRING | 10116.ENSRNOP00000018637. |
PTM databases | |
| GlycoSuiteDB | P12839. |
| PhosphoSite | P12839. |
2D gel databases | |
| World-2DPAGE | 0004:P12839. |
Proteomic databases | |
| PaxDb | P12839. |
| PRIDE | P12839. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 24588. |
| KEGG | rno:24588. |
| UCSC | RGD:3160. rat. |
Organism-specific databases | |
| CTD | 4741. |
| RGD | 3160. Nefm. |
Phylogenomic databases | |
| eggNOG | NOG264891. |
| HOGENOM | HOG000230977. |
| HOVERGEN | HBG013015. |
| InParanoid | P12839. |
| KO | K04573. |
| OrthoDB | EOG4VMFFD. |
Gene expression databases | |
| Genevestigator | P12839. |
| GermOnline | ENSRNOG00000013916. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR016044. F. IPR001664. IF. IPR006821. Intermed_filament_DNA-bd. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. [Graphical view] |
| PANTHER | PTHR23239. PTHR23239. 1 hit. |
| Pfam | PF00038. Filament. 1 hit. PF04732. Filament_head. 1 hit. [Graphical view] |
| PRINTS | PR01248. TYPE1KERATIN. |
| PROSITE | PS00226. IF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 603770. |
Entry information
| Entry name | NFM_RAT | ||||||||
| Accession | Primary (citable) accession number: P12839 Secondary accession number(s): Q63370 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
