CALR_EUGGR
ID CALR_EUGGR Reviewed; 401 AA.
AC Q9ZNY3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Navazzio L., Baldan B., Martin W., Mariani P.;
RT "Evidence for conservation of a calcium homeostat component: purification
RT characterization and cloning of calreticulin from Euglena gracilis.";
RL Submitted (DEC-1996) 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; Y09816; CAA70945.1; -; mRNA.
DR AlphaFoldDB; Q9ZNY3; -.
DR SMR; Q9ZNY3; -.
DR ELM; Q9ZNY3; -.
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; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 2: Evidence at transcript level;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Lectin;
KW Metal-binding; Repeat; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..401
FT /note="Calreticulin"
FT /id="PRO_0000004190"
FT REPEAT 187..198
FT /note="1-1"
FT REPEAT 206..217
FT /note="1-2"
FT REPEAT 223..234
FT /note="1-3"
FT REPEAT 241..252
FT /note="1-4"
FT REPEAT 256..266
FT /note="2-1"
FT REPEAT 270..280
FT /note="2-2"
FT REPEAT 284..294
FT /note="2-3"
FT REGION 187..252
FT /note="4 X approximate repeats"
FT REGION 199..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..294
FT /note="3 X approximate repeats"
FT REGION 341..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 398..401
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 199..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..401
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 109
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 125
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 132
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 314
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT DISULFID 103..134
FT /evidence="ECO:0000250"
SQ SEQUENCE 401 AA; 45911 MW; 056B074C16292674 CRC64;
MRKELWLGLL LSSQAVLSTI YYKETFEPDW ETRWTHSTAK SDYGKFKLTS GKFYGDKAKD
AGIQTSQDAK FYAISSPIAS SFSNEGKDLV LQFSVKHEQD IDCGGGYLKL LPSVDAAKFT
GDTPYHIMFG PDICGATKKI HFILTYKGKN LLWKKEPRCE TDTLSHTYTA VIKADRTYEV
LVDQVKKESG TLEEDWEILK PKTIPDPEDK KPADWVDEPD MVDPEDKKPE DWDKEPAQIP
DPDATQPDDW DEEEDGKWEA PMISNPKYKG EWKAKKIPNP AYKGVWKPRD IPNPEYEADD
KVHIFDEIAA VGFDLWQVKS GTIFDNIIVT DSLAEAKAFY DQTNGATKDA EKKAFDSAEA
DKRKKEEDER KKQEEEEKKT AEEDEDDDDE EEEEDDKKDE L
