ID CALR_BERST Reviewed; 416 AA. AC Q9ZPP1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 22-FEB-2023, entry version 99. DE RecName: Full=Calreticulin; DE Flags: Precursor; OS Berberis stolonifera (Barberry). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Berberidoideae; OC Berberideae; Berberis. OX NCBI_TaxID=33814; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Chou W.-M., Kutchan T.M.; RT "Calreticulin from Berberis stolonifera."; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Molecular calcium-binding chaperone promoting folding, CC oligomeric assembly and quality control in the ER via the CC calreticulin/calnexin cycle. This lectin may interact transiently with CC almost all of the monoglucosylated glycoproteins that are synthesized CC in the ER (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE- CC ProRule:PRU10138}. CC -!- DOMAIN: Can be divided into a N-terminal globular domain, a proline- CC rich P-domain forming an elongated arm-like structure and a C-terminal CC acidic domain. The P-domain binds one molecule of calcium with high CC affinity, whereas the acidic C-domain binds multiple calcium ions with CC low affinity (By similarity). {ECO:0000250}. CC -!- DOMAIN: The interaction with glycans occurs through a binding site in CC the globular lectin domain. {ECO:0000250}. CC -!- DOMAIN: The zinc binding sites are localized to the N-domain. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF052040; AAD17490.1; -; mRNA. DR AlphaFoldDB; Q9ZPP1; -. DR SMR; Q9ZPP1; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 1. DR InterPro; IPR001580; Calret/calnex. DR InterPro; IPR018124; Calret/calnex_CS. DR InterPro; IPR009169; Calreticulin. DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf. DR InterPro; IPR013320; ConA-like_dom_sf. DR PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1. DR PANTHER; PTHR11073:SF2; CALRETICULIN-1; 1. DR Pfam; PF00262; Calreticulin; 2. DR PIRSF; PIRSF002356; Calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 1. DR PROSITE; PS00803; CALRETICULIN_1; 1. DR PROSITE; PS00804; CALRETICULIN_2; 1. DR PROSITE; PS00805; CALRETICULIN_REPEAT; 2. DR PROSITE; PS00014; ER_TARGET; 1. PE 2: Evidence at transcript level; KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Lectin; Metal-binding; Repeat; Signal; Zinc. FT SIGNAL 1..? FT /evidence="ECO:0000255" FT CHAIN ?..416 FT /note="Calreticulin" FT /id="PRO_0000004187" FT REPEAT 194..205 FT /note="1-1" FT REPEAT 213..224 FT /note="1-2" FT REPEAT 230..241 FT /note="1-3" FT REPEAT 248..259 FT /note="1-4" FT REPEAT 263..273 FT /note="2-1" FT REPEAT 277..287 FT /note="2-2" FT REPEAT 291..301 FT /note="2-3" FT REGION 194..259 FT /note="4 X approximate repeats" FT REGION 209..281 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 263..301 FT /note="3 X approximate repeats" FT REGION 349..416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 413..416 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT COMPBIAS 209..253 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 349..375 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 376..416 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 112 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 114 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 131 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 138 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 321 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 108..140 FT /evidence="ECO:0000250" SQ SEQUENCE 416 AA; 47927 MW; 08AC46885BF69114 CRC64; MAIAERRSRS HLALRVRDRV SAEVFFEERF EDGWESKWVK SDWKRDENMA GEWNFTSGKW NGDANDKGIQ TSEDYRFYAI SAAFPEFSNK GKTLVFQFSV KHEQKLDCGG GYMKLLSGDV DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI LTKGETNHLI KKDVPCETDQ LTHVYTFILR PDASYSILID NVEKQSGSVY TDWDILPPKQ IKDPEAKKPE DWEDKEYIPD PEDKKPEGYD DIPKEITDPE AKKPEDWDDE EDGEWTAPTI PNPDYKGEWK PKKIKNPNFK GKWKAPMIDN PDFKDDPDIY VFPKLKYVGI ELWQVKSGTM FDNVLICDDP DYAKKLAEET WGKNKDAEKA AFDEAEKKKE EEEAKDDPTE SDDEKPDEEG ESDGEGDDES KDIDNEEDDE DVHDEL //