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MUC16

Domain

Composed of three domains, a Ser-, Thr-rich N-terminal domain, a repeated domain containing between 12 and 60 partially conserved tandem repeats of 156 amino acids and a C-terminal transmembrane contain domain with a short cytoplasmic tail.

Function

Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.

Post-translational modifications

Heavily O-glycosylated; expresses both type 1 and type 2 core glycans.

Heavily N-glycosylated; expresses primarily high mannose and complex bisecting type N-linked glycans.

May be phosphorylated. Phosphorylation of the intracellular C-terminal domain may induce proteolytic cleavage and the liberation of the extracellular domain into the extracellular space.

May contain numerous disulfide bridges. Association of several molecules of the secreted form may occur through interchain disulfide bridges providing an extraordinarily large gel-like matrix in the extracellular space or in the lumen of secretory ducts.

Tissue specificity

Expressed in corneal and conjunctival epithelia (at protein level). Overexpressed in ovarian carcinomas and ovarian low malignant potential (LMP) tumors as compared to the expression in normal ovarian tissue and ovarian adenomas.

Cellular localization

  • Cell membrane
  • Single-pass type I membrane protein
  • Secreted
  • Extracellular space
  • May be liberated into the extracellular space following the phosphorylation of the intracellular C-terminus which induces the proteolytic cleavage and liberation of the extracellular domain.

Alternative names

  • Mucin-16
  • MUC-16
  • Ovarian cancer-related tumor marker CA125
  • Ovarian carcinoma antigen CA125
  • CA-125
  • MUC16
  • CA125

Target type

Proteins

Primary research area

Oncology

Other research areas

  • Immuno-oncology

Molecular weight

1519175Da