Q9STD3 · CALR_CHLRE

Function

function

Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).

Features

Showing features for binding site.

142050100150200250300350400
TypeIDPosition(s)Description
Binding site110an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site112an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site131an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site138an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site321an alpha-D-glucoside (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum lumen
Molecular Functioncalcium ion binding
Molecular Functioncarbohydrate binding
Molecular Functionunfolded protein binding
Biological Processprotein folding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Calreticulin

Organism names

Accessions

  • Primary accession
    Q9STD3

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000000418919-420Calreticulin
Disulfide bond106↔140

Keywords

Proteomic databases

Structure

Family & Domains

Features

Showing features for repeat, region, compositional bias, motif.

TypeIDPosition(s)Description
Repeat194-2051-1
Region194-2594 X approximate repeats
Compositional bias210-258Basic and acidic residues
Region210-272Disordered
Repeat213-2241-2
Repeat230-2411-3
Repeat248-2591-4
Repeat263-2732-1
Region263-3013 X approximate repeats
Repeat277-2872-2
Repeat291-3012-3
Compositional bias357-379Basic and acidic residues
Region357-420Disordered
Compositional bias383-398Acidic residues
Compositional bias399-420Basic and acidic residues
Motif417-420Prevents secretion from ER

Domain

Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
The interaction with glycans occurs through a binding site in the globular lectin domain.
The zinc binding sites are localized to the N-domain.

Sequence similarities

Belongs to the calreticulin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    420
  • Mass (Da)
    47,328
  • Last updated
    2000-05-01 v1
  • Checksum
    DD3BA3AFFBF61C9B
MKWGVVAVLATLVVAASAKDYFKETFDGSWADRWTKSSWKVSDGSAGEFKLTAGKWYGDAEADKGIQTGPDSKFFAISAPLATVFDNTGKDTVVQFSVKHEQDLDCGGGYIKVVPATSEKQMGEFGGDTPYSIMFGPDICGYSTRKVHVILTYKGKNYLIKKDIKAETDQLTHVYTLVIKPDNTYQVLIDLKEVASGSLYEDWDMLPPKTIKDPKASKPEDWDEREEIADPEDKKPEGWDDIPATIADKDAKKPEDWDDEEDGTWEPPMIPNPEYKGEWKAKMIKNPAYKGIWVAPDIDNPDYVHDDKLYNFKDLKFVGFELWQVKSGSIFDNILVTDDLEAAKKFAEDTWGKHKDEEKAMFDKVKKEEDEKKAKDAPPPPVDAEAAEEEDDEYEDKEEPSGMGSIKIPKEEEESGHDEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias210-258Basic and acidic residues
Compositional bias357-379Basic and acidic residues
Compositional bias383-398Acidic residues
Compositional bias399-420Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ000765
EMBL· GenBank· DDBJ
CAB54526.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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