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neurofilament medium polypeptide; NF-M; neurofilament triplet M protein; 160 kD neurofilament protein; neurofilament 3 (NEFM NEF3 NFM)

Function: - neurofilament protein - can form neurofilaments in association with neurofilament L [3] - role in maintenance of neuronal caliber - phosphorylated on a number of the Ser in K-S-P repeats - phosphorylation results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber - phosphorylation seems to play a major role in functioning of the larger neurofilament polypeptides (NF-M & NF-H); levels of phosphorylation are altered developmentally & coincide with a change in the neurofilament function Structure: - repeats containing tripeptide K-S-P - belongs to the intermediate filament family Laboratory: - neurofilament medium chain Ab in CSF

Interactions

molecular events

General

neurofilament protein

Properties

SIZE: entity length = 916 aa MW = 102 kD COMPARTMENT: cytoplasm CELL: neuron MOTIF: Head {2-104} acetylation site SITE: N-TERMINUS EFFECTOR-BOUND: acetyl Thr glycosylation site {T47} Rod {105-412} MOTIF: Coil 1A {105-136} Linker 1 {137-149} Coil 1B {150-248} Linker 12 {249-265} Coil 2A {266-287} Linker 2 {288-291} Coil 2B {292-412} Tyr phosphorylation site {Y320} Tail {413-916} MOTIF: Thr glycosylation site {T431} Ser phosphorylation site {S511} Ser phosphorylation site {S545} Ser phosphorylation site {S553} Ser phosphorylation site {S559} consensus repeat {614-691} (6) Ser phosphorylation site {S680} Ser phosphorylation site {S685} Ser phosphorylation site {S736} Ser phosphorylation site {S783} Ser phosphorylation site {S788} Ser phosphorylation site {S837}

Database Correlations

OMIM 162250 UniProt P07197 PFAM correlations

References

  1. Alperts et al Molecular Biology of the Cell, Garland Publishing, New York, NY 1989 pg 662
  2. Wang KK et al Calmodulin-binding proteins as calpain substrates. Biochem J 262:693 1989 PMID: 2556106
  3. Cairns NJ, Lee VM, Trojanowski JQ. The cytoskeleton in neurodegenerative diseases. J Pathol. 2004 Nov;204(4):438-49. Review. PMID: 15495240
  4. UniProt :accession P07197
  5. Human intermediate Filament mutation Database http://www.interfil.org