ID CALR_PRUAR Reviewed; 421 AA. AC Q9XF98; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 22-FEB-2023, entry version 105. DE RecName: Full=Calreticulin; DE Flags: Precursor; OS Prunus armeniaca (Apricot) (Armeniaca vulgaris). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus. OX NCBI_TaxID=36596; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Bergeron; TISSUE=Endocarp, and Mesocarp; RA Mbeguie-A-Mbeguie D., Fils-Lycaon B.R.; RT "Molecular cloning and nucleotide sequence of a calreticulin from apricot RT (Prunus armeniaca cv. Bergeron)."; RL Submitted (MAR-1999) 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; AF134733; AAD32207.1; -; mRNA. DR AlphaFoldDB; Q9XF98; -. DR SMR; Q9XF98; -. 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..22 FT /evidence="ECO:0000255" FT CHAIN 23..421 FT /note="Calreticulin" FT /id="PRO_0000004194" FT REPEAT 196..207 FT /note="1-1" FT REPEAT 215..226 FT /note="1-2" FT REPEAT 232..243 FT /note="1-3" FT REPEAT 250..261 FT /note="1-4" FT REPEAT 265..275 FT /note="2-1" FT REPEAT 279..289 FT /note="2-2" FT REPEAT 293..303 FT /note="2-3" FT REGION 196..261 FT /note="4 X approximate repeats" FT REGION 217..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 265..303 FT /note="3 X approximate repeats" FT REGION 350..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 418..421 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT COMPBIAS 217..255 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 350..377 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 378..403 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 404..421 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 114 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 116 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 133 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 140 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 323 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT CARBOHYD 56 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 156 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 110..142 FT /evidence="ECO:0000250" SQ SEQUENCE 421 AA; 48416 MW; 4F5F94CBAA6C6690 CRC64; MAFRVPNSSL LSLILLSLLA IASAKVFFEE RFEDGWDKRW VTSEWKKDEN LAGEWNYTSG KWNGDPNDKG IQTSEDYRFY AISAEFPEFS NKDKTLVFQF SVKHEQKLDC GGGYIKLLSG DVDQKKFGGD TPYSIMFGPD ICGYSTKKVH AILNYNNTNN LIKKDVPCET DQLTHVYTFI IRPDATYSIL IDNLEKQTGS LYSDWDLLPA KKIKDPEAKK PEDWEDQEYI PDPEDKKPEG YDDIPKEITD PDAKKPEDWD DEEDGEWTAP TIPNPEYKGE WKPKKIKNPN FKGKWKAPLI DNPEFKDDPE LYVYPNLKYV GIELWQVKSG TLFDNILITD EPEYAKQLAE ETWGKQKDAE KAAFEELEKK LQEEESKEDP VDSDAEDDDN EAEDGEESDS ESKPDSTEES AETEAEKHDE L //