Fetuin-B-type cystatin domain (IPR025764)

Short name: Cystatin_Fetuin_B

Domain relationships


The cystatin superfamily consists of a large group of cystatin domain- containing proteins, most of which are reversible and tight-binding inhibitors of the papain (C1) and legumain (C13) families of cysteine proteases. Fetuins have been identified as main members of the cystatin superfamily and are composed of fetuin-A and fetuin-B. Fetuins are characterised by the presence of 2 N-terminally located cystatin-like repeats and a unique C-terminal domain which is not present in other proteins of the cystatin family [PMID: 19919722, PMID: 1372866, PMID: 1373325].

Fetuin-B has been suggested to be involved in systemic inflammation, as a tumor suppressor, and as a basic calcium phosphate precipitation inhibitor [PMID: 10947975, PMID: 18751887].

The cystatin fold is formed by a five stranded anti-parallel beta-sheet wrapped around a five-turn alpha-helix [PMID: 19919722]. Fetuin contains twelve conserved cysteines involved in six disulphide bonds. Eleven of the twelve invariant cysteines are located within the cystatin-like repeats. The 12th cysteine is located near the C terminus of the protein, separated by a region of variable length.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles