A0A172DYZ9 · A0A172DYZ9_CENAM
- ProteinCalreticulin
- GeneCRT
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids428 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 115 | an alpha-D-glucoside (UniProtKB | ChEBI) | |||
Binding site | 117 | an alpha-D-glucoside (UniProtKB | ChEBI) | |||
Binding site | 134 | an alpha-D-glucoside (UniProtKB | ChEBI) | |||
Binding site | 141 | an alpha-D-glucoside (UniProtKB | ChEBI) | |||
Binding site | 324 | an alpha-D-glucoside (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | unfolded protein binding | |
Biological Process | protein folding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCalreticulin
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Panicodae > Paniceae > Cenchrinae > Cenchrus
Accessions
- Primary accessionA0A172DYZ9
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-25 | ||||
Chain | PRO_5007948030 | 26-428 | Calreticulin | ||
Disulfide bond | 111↔143 | ||||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 213-256 | Basic and acidic residues | |||
Region | 213-286 | Disordered | |||
Compositional bias | 356-378 | Basic and acidic residues | |||
Region | 356-428 | Disordered | |||
Compositional bias | 379-415 | Acidic residues | |||
Sequence similarities
Belongs to the calreticulin family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)48,687
- Last updated2016-09-07 v1
- Checksum321F73E6BC662972
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 213-256 | Basic and acidic residues | |||
Compositional bias | 356-378 | Basic and acidic residues | |||
Compositional bias | 379-415 | Acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JX099538 EMBL· GenBank· DDBJ | AFM55036.1 EMBL· GenBank· DDBJ | mRNA |