CALR_BERST
ID CALR_BERST Reviewed; 416 AA.
AC Q9ZPP1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
OS Berberis stolonifera (Barberry).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Berberidoideae;
OC Berberis.
OX NCBI_TaxID=33814;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chou W.-M., Kutchan T.M.;
RT "Calreticulin from Berberis stolonifera.";
RL Submitted (MAR-1998) 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; AF052040; AAD17490.1; -; mRNA.
DR AlphaFoldDB; Q9ZPP1; -.
DR SMR; Q9ZPP1; -.
DR PRIDE; Q9ZPP1; -.
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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..416
FT /note="Calreticulin"
FT /id="PRO_0000004187"
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 209..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..301
FT /note="3 X approximate repeats"
FT REGION 349..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 209..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 114
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 CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..140
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 47927 MW; 08AC46885BF69114 CRC64;
MAIAERRSRS HLALRVRDRV SAEVFFEERF EDGWESKWVK SDWKRDENMA GEWNFTSGKW
NGDANDKGIQ TSEDYRFYAI SAAFPEFSNK GKTLVFQFSV KHEQKLDCGG GYMKLLSGDV
DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI LTKGETNHLI KKDVPCETDQ LTHVYTFILR
PDASYSILID NVEKQSGSVY TDWDILPPKQ IKDPEAKKPE DWEDKEYIPD PEDKKPEGYD
DIPKEITDPE AKKPEDWDDE EDGEWTAPTI PNPDYKGEWK PKKIKNPNFK GKWKAPMIDN
PDFKDDPDIY VFPKLKYVGI ELWQVKSGTM FDNVLICDDP DYAKKLAEET WGKNKDAEKA
AFDEAEKKKE EEEAKDDPTE SDDEKPDEEG ESDGEGDDES KDIDNEEDDE DVHDEL
