VIM

SECTIONS

1 - Domain
2 - Function
3 - Involvement in disease
4 - Post-translational modifications
5 - Sequence similarities
6 - Tissue specificity
7 - Cellular localization
8 - Alternative names
9 - Database links
10 - Target type
11 - Primary research area
12 - Other research areas
13 - Molecular weight

Domain

The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization.

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.

Function

Vimentin, a class-III intermediate filament, is present in various non-epithelial cells, particularly mesenchymal cells, and connects either laterally or terminally to the nucleus, endoplasmic reticulum, and mitochondria. It is involved with LARP6 in stabilizing type I collagen mRNAs for CO1A1 and CO1A2. This supplementary information is collated from multiple sources and compiled automatically.

Involvement in disease

Cataract 30, multiple types

CTRCT30

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.

None

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

Post-translational modifications

Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin (By similarity). One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm (PubMed:21465480). Phosphorylated by STK33 (PubMed:18811945). Phosphorylated on tyrosine residues by SRMS (PubMed:29496907).

O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.

S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.

Sequence similarities

Belongs to the intermediate filament family.

Tissue specificity

Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines.