ID CALR_RICCO Reviewed; 415 AA. AC P93508; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 24-JAN-2024, entry version 125. DE RecName: Full=Calreticulin; DE Flags: Precursor; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae; OC Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=9290642; DOI=10.1023/a:1005822327479; RA Coughlan S.J., Hastings C., Winfrey R. Jr.; RT "Cloning and characterization of the calreticulin gene from Ricinus RT communis L."; RL Plant Mol. Biol. 34:897-911(1997). 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. 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; U74631; AAB71420.1; -; Genomic_DNA. DR EMBL; U74630; AAB71419.1; -; mRNA. DR PIR; T10172; T10172. DR RefSeq; NP_001310652.1; NM_001323723.1. DR AlphaFoldDB; P93508; -. DR SMR; P93508; -. DR GeneID; 8269812; -. DR KEGG; rcu:8269812; -. DR eggNOG; KOG0674; Eukaryota. DR OrthoDB; 5489154at2759; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. 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..20 FT /evidence="ECO:0000255" FT CHAIN 21..415 FT /note="Calreticulin" FT /id="PRO_0000004195" FT REPEAT 192..203 FT /note="1-1" FT REPEAT 211..222 FT /note="1-2" FT REPEAT 228..239 FT /note="1-3" FT REPEAT 246..257 FT /note="1-4" FT REPEAT 261..271 FT /note="2-1" FT REPEAT 275..285 FT /note="2-2" FT REPEAT 289..299 FT /note="2-3" FT REGION 192..257 FT /note="4 X approximate repeats" FT REGION 208..276 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..299 FT /note="3 X approximate repeats" FT REGION 347..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 412..415 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT COMPBIAS 208..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 347..373 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 374..415 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 110 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 112 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 129 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 136 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 319 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT CARBOHYD 52 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 152 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 106..138 FT /evidence="ECO:0000250" SQ SEQUENCE 415 AA; 47522 MW; DD5F452E76CC7F8C CRC64; MANPKSLSLF LLSLLAIASA EVFFEERFED GWENRWVKSD WKKDENTAGE WNYTSGKWNG DPNDKGIQTS EDYRFYAISA EFPEFSNKDK TLVFQFSVKH EQKLDCGGGY MKLLSSSTDQ KKFGGDTPYS IMFGPDICGY STKKVHAILN YNDTNHLIKK EVPCETDQLT HVYTLVIRPD ATYSILIDNV EKQTGSLYTD WDLLPPKKIK DPEAKKPEDW DEKEYIPDPE DKKPEGYDDI PKEIPDPDAK KPEDWDDEED GEWTAPTIAN PEYKGPWKPK KIKNPNYKGK WKAPMIDNPD FKDDPEIYVY PNLKYVGIEL WQVKSGTLFD NVLICNDPEY AKQLAEETWG KNKDAEKAAF EEAEKKKEEE ESKDDPADSD ADEDDDDADD TEGEDDGESK SDAAEDSAED VHDEL //