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Filensin

Function

Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373). Involved in altering the calcium regulation of MIP water permeability (PubMed:30790544).

Involvement in disease

Cataract 33, multiple types

CTRCT33

An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT33 has juvenile-onset and the opacities are restricted to the cortex of the lens, not involving the nucleus.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

Proteolytically cleaved during lens cell fiber differentiation with increased fragmentation as fiber cell age increases.

Filensin C-terminal fragment

Myristoylated at Gly-434 following proteolytic cleavage at Asp-433.

Filensin N-terminal fragment

Acetylated at Ala-42 following proteolytic cleavage at Leu-41.

Sequence similarities

Belongs to the intermediate filament family.

Tissue specificity

Expressed in the cortex and nucleus of the retina lens (at protein level).

Cellular localization

  • Cell membrane
  • Peripheral membrane protein
  • Cytoplasmic side
  • Cytoplasm
  • Cytoplasm
  • Cytoskeleton
  • Cytoplasm
  • Cell cortex

Alternative names

  • Filensin
  • Beaded filament structural protein 1
  • Lens fiber cell beaded-filament structural protein CP 115
  • Lens intermediate filament-like heavy
  • CP115
  • LIFL-H
  • BFSP1

Target type

Proteins

Primary research area

Neuroscience

Molecular weight

74544Da

We found 2 products in 1 category

Primary Antibodies

Target

Application

Reactive species

Search our catalogue for 'Filensin' (2)

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