Q9XF98 · CALR_PRUAR

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.

142150100150200250300350400
TypeIDPosition(s)Description
Binding site114an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site116an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site133an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site140an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site323an 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

  • Taxonomic identifier
  • Strain
    • cv. Bergeron
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus

Accessions

  • Primary accession
    Q9XF98

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_000000419423-421Calreticulin
Glycosylation56N-linked (GlcNAc...) asparagine
Disulfide bond110↔142
Glycosylation156N-linked (GlcNAc...) asparagine

Keywords

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Repeat196-2071-1
Region196-2614 X approximate repeats
Repeat215-2261-2
Compositional bias217-255Basic and acidic residues
Region217-283Disordered
Repeat232-2431-3
Repeat250-2611-4
Repeat265-2752-1
Region265-3033 X approximate repeats
Repeat279-2892-2
Repeat293-3032-3
Compositional bias350-377Basic and acidic residues
Region350-421Disordered
Compositional bias378-403Acidic residues
Compositional bias404-421Basic and acidic residues
Motif418-421Prevents 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    421
  • Mass (Da)
    48,416
  • Last updated
    1999-11-01 v1
  • Checksum
    4F5F94CBAA6C6690
MAFRVPNSSLLSLILLSLLAIASAKVFFEERFEDGWDKRWVTSEWKKDENLAGEWNYTSGKWNGDPNDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYIKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILNYNNTNNLIKKDVPCETDQLTHVYTFIIRPDATYSILIDNLEKQTGSLYSDWDLLPAKKIKDPEAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGEWKPKKIKNPNFKGKWKAPLIDNPEFKDDPELYVYPNLKYVGIELWQVKSGTLFDNILITDEPEYAKQLAEETWGKQKDAEKAAFEELEKKLQEEESKEDPVDSDAEDDDNEAEDGEESDSESKPDSTEESAETEAEKHDEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias217-255Basic and acidic residues
Compositional bias350-377Basic and acidic residues
Compositional bias378-403Acidic residues
Compositional bias404-421Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF134733
EMBL· GenBank· DDBJ
AAD32207.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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