ID CALR_MAIZE Reviewed; 420 AA. AC Q9SP22; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 127. DE RecName: Full=Calreticulin; DE Flags: Precursor; GN Name=CRT; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11874098; DOI=10.1023/a:1013917701701; RA Wyatt S.E., Tsou P.-L., Robertson D.; RT "Expression of the high capacity calcium-binding domain of calreticulin RT increases bioavailable calcium stores in plants."; RL Transgenic Res. 11:1-10(2002). 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; AF190454; AAF01470.1; -; mRNA. DR AlphaFoldDB; Q9SP22; -. DR SMR; Q9SP22; -. DR STRING; 4577.Q9SP22; -. DR GlyCosmos; Q9SP22; 1 site, No reported glycans. DR PaxDb; 4577-GRMZM2G358059_P01; -. DR eggNOG; KOG0674; Eukaryota. DR InParanoid; Q9SP22; -. DR Proteomes; UP000007305; Unplaced. DR ExpressionAtlas; Q9SP22; baseline and differential. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central. 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; PS00805; CALRETICULIN_REPEAT; 2. DR PROSITE; PS00014; ER_TARGET; 1. PE 2: Evidence at transcript level; KW Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein; Lectin; KW Metal-binding; Reference proteome; Repeat; Signal; Zinc. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..420 FT /note="Calreticulin" FT /id="PRO_0000004191" FT REPEAT 197..208 FT /note="1-1" FT REPEAT 216..227 FT /note="1-2" FT REPEAT 233..244 FT /note="1-3" FT REPEAT 251..262 FT /note="1-4" FT REPEAT 266..276 FT /note="2-1" FT REPEAT 280..290 FT /note="2-2" FT REPEAT 294..304 FT /note="2-3" FT REGION 197..262 FT /note="4 X approximate repeats" FT REGION 213..285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 266..304 FT /note="3 X approximate repeats" FT REGION 355..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 213..256 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 355..378 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 379..409 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 115 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 117 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 134 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 141 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 324 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT CARBOHYD 57 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 420 AA; 47940 MW; E73B7F43E7494735 CRC64; MAIRKGSSYA VAALLALASV AAVAGEVFFQ EKFEDGWESR WVKSEWKKDE NMAGEWNHTS GKWNGDAEDK GIQTSEDYRF YAISAEYPEF SNKDKTLVLQ FSVKHEQKLD CGGGYVKLLG GDVDQKTLGG DTSYSIISRP DISRYSTKKV HTILTKDGKN HLIKKDVPCQ TDQLTHVYTF IIRPDATYSI LIDNEEKHTG SIYEHWDILP PKKIKDPEAK KPEDWDDKEY IPDPEDKKPE GYDDIPKEIP DPDAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKQKKIKNP NYQGKWKAPM IDNPDFKDDP YIYAFDSLKY IGIELWQVKS GTLFDNIIIT DDPALAKTFA EETWGKHKEA EKAAFDEAEK KKEEEDAAKG GDDEDDDLED EEDDEKADED KADSDAEDGK DSDDEKHDEL //