Q40401 · CALR_NICPL

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.

141650100150200250300350400
TypeIDPosition(s)Description
Binding site117an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site119an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site136an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site143an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site326an 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
Cellular Componentendoplasmic reticulum membrane
Molecular Functioncalcium ion binding
Molecular Functioncarbohydrate binding
Molecular Functionunfolded protein binding
Biological Processprotein folding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Calreticulin

Gene names

    • Name
      CAL1

Organism names

Accessions

  • Primary accession
    Q40401

Subcellular Location

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-27
ChainPRO_000000419228-416Calreticulin
Glycosylation59N-linked (GlcNAc...) asparagine
Disulfide bond113↔145
Glycosylation159N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Repeat199-2101-1
Region199-2644 X approximate repeats
Region215-286Disordered
Compositional bias216-258Basic and acidic residues
Repeat218-2291-2
Repeat235-2461-3
Repeat253-2641-4
Repeat268-2782-1
Region268-3063 X approximate repeats
Repeat282-2922-2
Repeat296-3062-3
Compositional bias355-381Basic and acidic residues
Region355-416Disordered
Compositional bias382-405Acidic residues
Motif413-416Prevents 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
    416
  • Mass (Da)
    47,481
  • Last updated
    1996-11-01 v1
  • Checksum
    5026F3152B8828C0
MATQRRANPSSLHLITVFSLLVAVVSAEVFFEESFNDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDANDKGIQTSEDYRFYAISAEFPEFSNKGKNLVFQFSVKHEQKLDCGGGYMKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILTYNDTNHLIKKEVPCETDQLTHVYTFILRPDATYSILIDNVEKQSGSLYSDWDLLPPKTIKDPSAKKPEDWDEKEFIDDPEDKKPEGYDDIPEEITDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKPKKIKNPNYKGKWKAPLIDNPDFKDDPDLYVFPKLKYVGVELWQVKSGTLFDNIVICDDPEYAKAIAEETWGKQKDAEKAAFEEAEKKREEEESKAAPADSDAEEDDDADDDSDDADDKSESKDDEAHDEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias216-258Basic and acidic residues
Compositional bias355-381Basic and acidic residues
Compositional bias382-405Acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z71395
EMBL· GenBank· DDBJ
CAA95999.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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