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1K9C

Solution Structure of Calreticulin P-domain subdomain (residues 189-261)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005783cellular_componentendoplasmic reticulum
A0006457biological_processprotein folding
A0051082molecular_functionunfolded protein binding
Functional Information from PROSITE/UniProt
site_idPS00805
Number of Residues13
DetailsCALRETICULIN_REPEAT Calreticulin family repeated motif signature. IkDpDaaKPEDWD
ChainResidueDetails
AILE191-ASP203
AILE208-ASP220
AILE225-ASP237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues11
DetailsRepeat: {"description":"1-2"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues11
DetailsRepeat: {"description":"1-3"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues11
DetailsRepeat: {"description":"1-4"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsRepeat: {"description":"2-1"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues33
DetailsRegion: {"description":"Interaction with PPIB","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues44
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues9
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27797","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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