ID CALR_CHLRE Reviewed; 420 AA. AC Q9STD3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=Calreticulin; DE Flags: Precursor; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=137c / CC-125; RA Zuppini A., Kaydamov C.; RT "Cloning and characterization of a cDNA encoding Chlamydomonas reinhardtii RT calreticulin."; RL Submitted (OCT-1997) 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; AJ000765; CAB54526.1; -; mRNA. DR RefSeq; XP_001689661.1; XM_001689609.1. DR AlphaFoldDB; Q9STD3; -. DR SMR; Q9STD3; -. DR PaxDb; 3055-EDP09399; -. DR ProMEX; Q9STD3; -. DR EnsemblPlants; PNW88643; PNW88643; CHLRE_01g038400v5. DR GeneID; 5715514; -. DR Gramene; PNW88643; PNW88643; CHLRE_01g038400v5. DR KEGG; cre:CHLRE_01g038400v5; -. DR eggNOG; KOG0674; Eukaryota. DR HOGENOM; CLU_018224_0_2_1; -. DR OMA; NWVYSEH; -. DR OrthoDB; 5489154at2759; -. 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 GO; GO:0050896; P:response to stimulus; IEA:UniProt. 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:SF45; CALRETICULIN; 1. DR PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 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; 1. DR PROSITE; PS00014; ER_TARGET; 1. PE 2: Evidence at transcript level; KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Lectin; KW Metal-binding; Repeat; Signal; Zinc. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..420 FT /note="Calreticulin" FT /id="PRO_0000004189" 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 210..272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 263..301 FT /note="3 X approximate repeats" FT REGION 357..420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 417..420 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT COMPBIAS 210..258 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..379 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 383..398 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 399..420 FT /note="Basic and 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 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 DISULFID 106..140 FT /evidence="ECO:0000250" SQ SEQUENCE 420 AA; 47328 MW; DD3BA3AFFBF61C9B CRC64; MKWGVVAVLA TLVVAASAKD YFKETFDGSW ADRWTKSSWK VSDGSAGEFK LTAGKWYGDA EADKGIQTGP DSKFFAISAP LATVFDNTGK DTVVQFSVKH EQDLDCGGGY IKVVPATSEK QMGEFGGDTP YSIMFGPDIC GYSTRKVHVI LTYKGKNYLI KKDIKAETDQ LTHVYTLVIK PDNTYQVLID LKEVASGSLY EDWDMLPPKT IKDPKASKPE DWDEREEIAD PEDKKPEGWD DIPATIADKD AKKPEDWDDE EDGTWEPPMI PNPEYKGEWK AKMIKNPAYK GIWVAPDIDN PDYVHDDKLY NFKDLKFVGF ELWQVKSGSI FDNILVTDDL EAAKKFAEDT WGKHKDEEKA MFDKVKKEED EKKAKDAPPP PVDAEAAEEE DDEYEDKEEP SGMGSIKIPK EEEESGHDEL //