O77788 (NFM_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 91.
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 | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 926 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. |
| Post-translational modification | Phosphorylated on a number of serine residues in the repeated K-S-P tripeptide motif. Phosphorylation of NFH may result in the formation of interfilament cross-links that are important in the maintenance of axonal caliber By similarity. Ref.1 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 By similarity. Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization By similarity. Ref.1 |
| Sequence similarities | Belongs to the intermediate filament family. |
| Mass spectrometry | Molecular mass is 105044 Da from positions 2 - 926. Determined by MALDI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Intermediate filament |
| Domain | Coiled coil Repeat |
| PTM | Acetylation Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | intermediate filament Inferred 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 Ref.1 | ||||||
| Chain | 2 – 926 | 925 | Neurofilament medium polypeptide | PRO_0000063793 | |||||
Regions | |||||||||
| Repeat | 512 – 516 | 5 | 1 | ||||||
| Repeat | 619 – 623 | 5 | 2 | ||||||
| Repeat | 624 – 628 | 5 | 3 | ||||||
| Repeat | 629 – 633 | 5 | 4 | ||||||
| Repeat | 634 – 638 | 5 | 5 | ||||||
| Repeat | 639 – 643 | 5 | 6 | ||||||
| Repeat | 644 – 648 | 5 | 7 | ||||||
| Repeat | 649 – 653 | 5 | 8 | ||||||
| Repeat | 654 – 658 | 5 | 9 | ||||||
| Repeat | 659 – 663 | 5 | 10 | ||||||
| Repeat | 664 – 668 | 5 | 11 | ||||||
| Repeat | 669 – 673 | 5 | 12 | ||||||
| Repeat | 674 – 678 | 5 | 13 | ||||||
| Repeat | 679 – 683 | 5 | 14 | ||||||
| Repeat | 684 – 688 | 5 | 15 | ||||||
| Repeat | 689 – 693 | 5 | 16 | ||||||
| Repeat | 694 – 698 | 5 | 17 | ||||||
| Region | 2 – 412 | 411 | Rod | ||||||
| Region | 105 – 136 | 32 | Coil 1A | ||||||
| Region | 137 – 149 | 13 | Linker 1 | ||||||
| Region | 150 – 248 | 99 | Coil 1B | ||||||
| Region | 249 – 265 | 17 | Linker 12 | ||||||
| Region | 266 – 287 | 22 | Coil 2A | ||||||
| Region | 288 – 291 | 4 | Linker 2 | ||||||
| Region | 292 – 412 | 121 | Coil 2B | ||||||
| Region | 413 – 926 | 514 | Tail | ||||||
| Region | 512 – 698 | 187 | 17 X 5 AA approximate tandem repeats of K-S-P-[TVEA]-[AKETP] | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.1 | ||||||
| Modified residue | 320 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 513 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 547 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 555 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 561 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 628 | 1 | Phosphothreonine Ref.1 | ||||||
| Modified residue | 630 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 635 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 640 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 647 | 1 | Phosphothreonine Ref.1 | ||||||
| Modified residue | 650 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 655 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 665 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 670 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 677 | 1 | Phosphothreonine Ref.1 | ||||||
| Modified residue | 680 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 685 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 690 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 695 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 727 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 751 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 757 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 771 | 1 | Phosphoserine Ref.1 | ||||||
| Modified residue | 847 | 1 | Phosphoserine Ref.1 | ||||||
| Glycosylation | 47 | 1 | O-linked (GlcNAc) By similarity | ||||||
Sequences
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References
| [1] | "Identification of endogenous phosphorylation sites of bovine medium and low molecular weight neurofilament proteins by tandem mass spectrometry." Trimpin S., Mixon A.E., Stapels M.D., Kim M.Y., Spencer P.S., Deinzer M.L. Biochemistry 43:2091-2105(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-116, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-513; SER-547; SER-555; SER-561; THR-628; SER-630; SER-635; SER-640; THR-647; SER-650; SER-655; SER-665; SER-670; THR-677; SER-680; SER-685; SER-695; SER-727; SER-751; SER-757; SER-771 AND SER-847, MASS SPECTROMETRY. |
| [2] | "The bovine neurofilament M subunit has a novel set of KSP repeats normally restricted to NF-H." Hill W.D., Zhang L., Balin B.J., Sprinkle T.J., Spicer K., Gearhart D.A. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-926. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF091342 mRNA. Translation: AAC36357.1. |
| IPI | IPI00705032. |
| UniGene | Bt.51690. |
3D structure databases | |
| ProteinModelPortal | O77788. |
| SMR | O77788. Positions 99-136, 330-407. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O77788. 1 interaction. |
| STRING | 9913.ENSBTAP00000052505. |
Proteomic databases | |
| PaxDb | O77788. |
| PRIDE | O77788. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | NOG264891. |
| HOGENOM | HOG000230977. |
| HOVERGEN | HBG013015. |
| InParanoid | O77788. |
| OrthoDB | EOG4VMFFD. |
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... |
Entry information
| Entry name | NFM_BOVIN | ||||||||
| Accession | Primary (citable) accession number: O77788 | ||||||||
| 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
