The domain within your query sequence starts at position 255 and ends at position 315; the E-value for the Calreticulin domain shown below is 6.6e-7.



PFAM accession number:PF00262
Interpro abstract (IPR001580):

The calreticulin family is a family of calcium-binding ER chaperonesthat includes calreticulin, calnexin and camlegin [ (PUBMED:12401114) ].

Calreticulin (calregulin) [ (PUBMED:1497605) ] is a high-capacity calcium-binding protein which is present in most tissues and located at the periphery of the endoplasmic (ER) and the sarcoplamic reticulum (SR) membranes. It probably plays a role in the storage of calcium in the lumen of the ER and SR and it may well have other important functions.

Structurally, calreticulin is a protein of about 400 amino acid residues consisting of three domains:

  • An N-terminal, probably globular, domain of about 180 amino acid residues (N-domain).
  • A central domain of about 70 residues (P-domain) which contains three repeats of an acidic 17 amino acid motif. This region binds calcium with a low-capacity, but a high-affinity.
  • A C-terminal domain rich in acidic residues and in lysine (C-domain). This region binds calcium with a high-capacity but a low-affinity.

Calreticulin is evolutionarily related to several other calcium-binding proteins, including Onchocerca volvulus antigen RAL-1, calnexin [ (PUBMED:8203019) ] and calmegin [ (PUBMED:8126001) ].

GO process:protein folding (GO:0006457)
GO component:endoplasmic reticulum (GO:0005783)
GO function:unfolded protein binding (GO:0051082), calcium ion binding (GO:0005509)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Calreticulin