CALR_BETVU
ID CALR_BETVU Reviewed; 416 AA.
AC O81919;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
OS Beta vulgaris (Sugar beet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX NCBI_TaxID=161934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=VV-D/ZR5; TISSUE=Leaf;
RA Viereck R.;
RT "Nucleotide sequence from sugar beet 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}.
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DR EMBL; AJ002057; CAA05161.1; -; mRNA.
DR PIR; T14554; T14554.
DR RefSeq; NP_001289994.1; NM_001303065.1.
DR AlphaFoldDB; O81919; -.
DR SMR; O81919; -.
DR EnsemblPlants; KMT13833; KMT13833; BVRB_4g076780.
DR GeneID; 104890403; -.
DR Gramene; KMT13833; KMT13833; BVRB_4g076780.
DR KEGG; bvg:104890403; -.
DR PhylomeDB; O81919; -.
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; 2.10.250.10; -; 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; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..416
FT /note="Calreticulin"
FT /id="PRO_0000004188"
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 217..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..304
FT /note="3 X approximate repeats"
FT REGION 351..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 217..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..416
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"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..143
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 48136 MW; 565FEC3489F77CA7 CRC64;
MENRGRNPSF LSLLLLLSLF AIASAKVFFE ERFEDGWEKR WVKSEWKKDE SMAGEWNYTS
GKWNGDANDK GIQTSEDYRF YAISAEFPEF SNKDNTLVFQ FSVKHEQKLD CGGGYMKLLS
GEVDQKKFGG DTPYSIMFGP DICGYSTKKV HAIFNYNDTN HLIKKDVPCE TDQLTHVYTF
ILRPDATYSI LIDNQEKQTG SLYTDWDLLP AKKIKDPEAK KPEDWDDKEF IPDPEDKKPE
GYDDIPAEIT DPEAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKAKKIKNP NYKGKWKAPM
IDNPEFKDDP ELYVYPKLRY VGVELWQVKS GTLFDNVLVC DDPEYAKQLA EETWGKQKDA
EKAAFEELEK KREEEETKDD PVESDAEDED EAEADDSDKD DADKSDDKDD DQHDEL
