CALR_MAIZE
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 03-AUG-2022, entry version 121.
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}.
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DR EMBL; AF190454; AAF01470.1; -; mRNA.
DR AlphaFoldDB; Q9SP22; -.
DR SMR; Q9SP22; -.
DR STRING; 4577.GRMZM2G358059_P01; -.
DR PaxDb; Q9SP22; -.
DR PRIDE; Q9SP22; -.
DR eggNOG; KOG0674; Eukaryota.
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; 2.10.250.10; -; 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; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 2.
DR PIRSF; PIRSF002356; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF63887; SSF63887; 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
