CALR_CHLRE
ID CALR_CHLRE Reviewed; 420 AA.
AC Q9STD3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=137c / CC-125;
RA Zuppini A., Kaydamov C.;
RT "Cloning and characterization of a cDNA encoding Chlamydomonas reinhardtii
RT 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; AJ000765; CAB54526.1; -; mRNA.
DR RefSeq; XP_001689661.1; XM_001689609.1.
DR AlphaFoldDB; Q9STD3; -.
DR SMR; Q9STD3; -.
DR STRING; 3055.EDP09399; -.
DR PRIDE; Q9STD3; -.
DR ProMEX; Q9STD3; -.
DR EnsemblPlants; PNW88643; PNW88643; CHLRE_01g038400v5.
DR GeneID; 5715514; -.
DR Gramene; PNW88643; PNW88643; CHLRE_01g038400v5.
DR KEGG; cre:CHLRE_01g038400v5; -.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR OMA; DYKDDPY; -.
DR OrthoDB; 822188at2759; -.
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..420
FT /note="Calreticulin"
FT /id="PRO_0000004189"
FT REPEAT 194..205
FT /note="1-1"
FT REPEAT 213..224
FT /note="1-2"
FT REPEAT 230..241
FT /note="1-3"
FT REPEAT 248..259
FT /note="1-4"
FT REPEAT 263..273
FT /note="2-1"
FT REPEAT 277..287
FT /note="2-2"
FT REPEAT 291..301
FT /note="2-3"
FT REGION 194..259
FT /note="4 X approximate repeats"
FT REGION 210..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..301
FT /note="3 X approximate repeats"
FT REGION 357..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 210..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 112
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 131
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 138
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 321
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT DISULFID 106..140
FT /evidence="ECO:0000250"
SQ SEQUENCE 420 AA; 47328 MW; DD3BA3AFFBF61C9B CRC64;
MKWGVVAVLA TLVVAASAKD YFKETFDGSW ADRWTKSSWK VSDGSAGEFK LTAGKWYGDA
EADKGIQTGP DSKFFAISAP LATVFDNTGK DTVVQFSVKH EQDLDCGGGY IKVVPATSEK
QMGEFGGDTP YSIMFGPDIC GYSTRKVHVI LTYKGKNYLI KKDIKAETDQ LTHVYTLVIK
PDNTYQVLID LKEVASGSLY EDWDMLPPKT IKDPKASKPE DWDEREEIAD PEDKKPEGWD
DIPATIADKD AKKPEDWDDE EDGTWEPPMI PNPEYKGEWK AKMIKNPAYK GIWVAPDIDN
PDYVHDDKLY NFKDLKFVGF ELWQVKSGSI FDNILVTDDL EAAKKFAEDT WGKHKDEEKA
MFDKVKKEED EKKAKDAPPP PVDAEAAEEE DDEYEDKEEP SGMGSIKIPK EEEESGHDEL
