Dematin (DMTN) Antibody – Rabbit Polyclonal

The protein encoded by this gene is an actin binding and bundling protein that plays a structural role in erythrocytes, by stabilizing and attaching the spectrin/actin cytoskeleton to the erythrocyte membrane in a phosphorylation-dependent manner. This protein contains a core domain in the N-terminus, and a headpiece domain in the C-terminus that binds F-actin. When purified from erythrocytes, this protein exists as a trimer composed of two 48 kDa polypeptides and a 52 kDa polypeptide. The different subunits arise from alternative splicing in the 3' coding region, where the headpiece domain is located. Disruption of this gene has been correlated with the autosomal dominant Marie Unna hereditary hypotrichosis disease, while loss of heterozygosity of this gene is thought to play a role in prostate cancer progression. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Nov 2014]

dematin: a probable DNA binding protein, with a Myb-like DNA-binding and ELM2 domain.

Protein type: Actin-binding; Tumor suppressor; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 8p21.1

Cellular Component: actin cytoskeleton; actin filament; cell projection membrane; cortical cytoskeleton; cytoplasmic membrane-bound vesicle; cytosol; endomembrane system; perinuclear region of cytoplasm; plasma membrane

Molecular Function: actin binding; protein binding; protein self-association; receptor binding; spectrin binding

Biological Process: actin cytoskeleton organization and biogenesis; actin filament bundle formation; actin filament capping; cytoskeleton organization and biogenesis; erythrocyte development; negative regulation of focal adhesion formation; negative regulation of peptidyl-serine phosphorylation; negative regulation of peptidyl-tyrosine phosphorylation; positive regulation of blood coagulation; protein complex assembly; regulation of actin cytoskeleton organization and biogenesis; regulation of cell shape; regulation of filopodium formation; transmembrane transport