View source for Calreticulin

<StructureSection load='6eny' size='340' side='right' caption='Human calreticulin (gold) complex with β-microglobulin (green), tapasin (pink),  protein disulfide-isomerase (yellow) MHC class I antigen (cyan) (PDB code [[6eny]]) ' scene=''>


== Function ==

'''Calreticulin''' (CALR) is a multifunction calcium-binding chaperone.  CALR is a molecular chaperone, an extracellular lectin, an intracellular mediator of integrin function, an inhibitor of steroid hormone-regulated gene expression and a C1q-binding protein<ref>PMID:9693955</ref>.

== Disease ==

Most patients with essential thrombocythemia or primary myelofibrosis not associated with JAK2 or MPL mutation have CALR mutation<ref>PMID:24325356</ref>.

== Relevance ==

CALR is active in regulating intracellular Ca+2 homeostasis<ref>PMID:22373697</ref>.

== Structural highlights ==

<scene name='77/776393/Cv/1'>CALR structure consists of 3 domains</scene>: N-terminal globular domain which has chaperone function; P-domain which is proline-rich, binds Ca+2 with high affinity and possesses a lectin-like chaperone function; C-terminal domain containing an ER retention signal.

== 3D Structures of calreticulin ==
[[Calreticulin 3D structures]]

</StructureSection>

== References ==
<references/>

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