CALR_RICCO
ID CALR_RICCO Reviewed; 415 AA.
AC P93508;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9290642; DOI=10.1023/a:1005822327479;
RA Coughlan S.J., Hastings C., Winfrey R. Jr.;
RT "Cloning and characterization of the calreticulin gene from Ricinus
RT communis L.";
RL Plant Mol. Biol. 34:897-911(1997).
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.
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; U74631; AAB71420.1; -; Genomic_DNA.
DR EMBL; U74630; AAB71419.1; -; mRNA.
DR PIR; T10172; T10172.
DR RefSeq; NP_001310652.1; NM_001323723.1.
DR AlphaFoldDB; P93508; -.
DR SMR; P93508; -.
DR STRING; 3988.XP_002512501.1; -.
DR PRIDE; P93508; -.
DR GeneID; 8269812; -.
DR KEGG; rcu:8269812; -.
DR eggNOG; KOG0674; Eukaryota.
DR OrthoDB; 822188at2759; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..415
FT /note="Calreticulin"
FT /id="PRO_0000004195"
FT REPEAT 192..203
FT /note="1-1"
FT REPEAT 211..222
FT /note="1-2"
FT REPEAT 228..239
FT /note="1-3"
FT REPEAT 246..257
FT /note="1-4"
FT REPEAT 261..271
FT /note="2-1"
FT REPEAT 275..285
FT /note="2-2"
FT REPEAT 289..299
FT /note="2-3"
FT REGION 192..257
FT /note="4 X approximate repeats"
FT REGION 208..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..299
FT /note="3 X approximate repeats"
FT REGION 347..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 412..415
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 208..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..415
FT /note="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 129
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 136
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 319
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..138
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 47522 MW; DD5F452E76CC7F8C CRC64;
MANPKSLSLF LLSLLAIASA EVFFEERFED GWENRWVKSD WKKDENTAGE WNYTSGKWNG
DPNDKGIQTS EDYRFYAISA EFPEFSNKDK TLVFQFSVKH EQKLDCGGGY MKLLSSSTDQ
KKFGGDTPYS IMFGPDICGY STKKVHAILN YNDTNHLIKK EVPCETDQLT HVYTLVIRPD
ATYSILIDNV EKQTGSLYTD WDLLPPKKIK DPEAKKPEDW DEKEYIPDPE DKKPEGYDDI
PKEIPDPDAK KPEDWDDEED GEWTAPTIAN PEYKGPWKPK KIKNPNYKGK WKAPMIDNPD
FKDDPEIYVY PNLKYVGIEL WQVKSGTLFD NVLICNDPEY AKQLAEETWG KNKDAEKAAF
EEAEKKKEEE ESKDDPADSD ADEDDDDADD TEGEDDGESK SDAAEDSAED VHDEL
