ID CALR_NICPL Reviewed; 416 AA. AC Q40401; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 22-FEB-2023, entry version 113. DE RecName: Full=Calreticulin; DE Flags: Precursor; GN Name=CAL1; OS Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4092; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9821685; DOI=10.1007/s004250050427; RA Borisjuk N., Sitailo L., Adler K., Malysheva L., Tewes A., Borisjuk L., RA Manteuffel R.; RT "Calreticulin expression in plant cells: developmental regulation, tissue RT specificity and intracellular distribution."; RL Planta 206:504-514(1998). 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; Z71395; CAA95999.1; -; mRNA. DR PIR; T16968; T16968. DR AlphaFoldDB; Q40401; -. DR SMR; Q40401; -. DR GlyCosmos; Q40401; 2 sites, No reported glycans. 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..27 FT /evidence="ECO:0000255" FT CHAIN 28..416 FT /note="Calreticulin" FT /id="PRO_0000004192" FT REPEAT 199..210 FT /note="1-1" FT REPEAT 218..229 FT /note="1-2" FT REPEAT 235..246 FT /note="1-3" FT REPEAT 253..264 FT /note="1-4" FT REPEAT 268..278 FT /note="2-1" FT REPEAT 282..292 FT /note="2-2" FT REPEAT 296..306 FT /note="2-3" FT REGION 199..264 FT /note="4 X approximate repeats" FT REGION 215..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 268..306 FT /note="3 X approximate repeats" FT REGION 355..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 216..258 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 355..381 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 382..405 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 117 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 119 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 143 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 326 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT CARBOHYD 59 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 113..145 FT /evidence="ECO:0000250" SQ SEQUENCE 416 AA; 47481 MW; 5026F3152B8828C0 CRC64; MATQRRANPS SLHLITVFSL LVAVVSAEVF FEESFNDGWE SRWVKSEWKK DENMAGEWNH TSGKWNGDAN DKGIQTSEDY RFYAISAEFP EFSNKGKNLV FQFSVKHEQK LDCGGGYMKL LSGDVDQKKF GGDTPYSIMF GPDICGYSTK KVHAILTYND TNHLIKKEVP CETDQLTHVY TFILRPDATY SILIDNVEKQ SGSLYSDWDL LPPKTIKDPS AKKPEDWDEK EFIDDPEDKK PEGYDDIPEE ITDPDAKKPE DWDDEEDGEW TAPTIPNPEY KGPWKPKKIK NPNYKGKWKA PLIDNPDFKD DPDLYVFPKL KYVGVELWQV KSGTLFDNIV ICDDPEYAKA IAEETWGKQK DAEKAAFEEA EKKREEEESK AAPADSDAEE DDDADDDSDD ADDKSESKDD EAHDEL //