A0A172DYZ9 · A0A172DYZ9_CENAM

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.

Features

Showing features for binding site.

142850100150200250300350400
TypeIDPosition(s)Description
Binding site115an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site117an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site134an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site141an alpha-D-glucoside (UniProtKB | ChEBI)
Binding site324an alpha-D-glucoside (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum lumen
Cellular Componentendoplasmic reticulum membrane
Molecular Functioncalcium ion binding
Molecular Functionunfolded protein binding
Biological Processprotein folding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Calreticulin

Gene names

    • Name
      CRT

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Panicodae > Paniceae > Cenchrinae > Cenchrus

Accessions

  • Primary accession
    A0A172DYZ9

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-25
ChainPRO_500794803026-428Calreticulin
Disulfide bond111↔143

Keywords

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias213-256Basic and acidic residues
Region213-286Disordered
Compositional bias356-378Basic and acidic residues
Region356-428Disordered
Compositional bias379-415Acidic residues

Sequence similarities

Belongs to the calreticulin family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    428
  • Mass (Da)
    48,687
  • Last updated
    2016-09-07 v1
  • Checksum
    321F73E6BC662972
MAIRRGSSCAIAALLALASVAAVAGEVFFQEKFEDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDAEDKGIQTSEDYRFYAISAEYPEFSNKGKTLVLQFSVKHEQKLDCGGGYVKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILTKDGKNHLIKKDVPCETDQLTHVYTLVIRPDATYSILIDNEEKQTGSVYEHWDILPPKQIKDPEAKKPEDWDDKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKQKKIKNPNYQGKWKAPMIDNPDFKDDPYIYAFDNLKYIGIELWQVKSGTLFDNIIITDDPALAKTFAEETWGKHKEAEKAAFDEAEKKKEEEEAAKGGDDEDDDLEDDEDDDKADEDKADSDVEDDGDDSDDENPRLVPSSRWRG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias213-256Basic and acidic residues
Compositional bias356-378Basic and acidic residues
Compositional bias379-415Acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JX099538
EMBL· GenBank· DDBJ
AFM55036.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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