ID   CALR_CANLF              Reviewed;          24 AA.
AC   P28490;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 82.
DE   RecName: Full=Calreticulin;
DE   AltName: Full=CRP55;
DE   AltName: Full=Calregulin;
DE   AltName: Full=Endoplasmic reticulum resident protein 60;
DE            Short=ERp60;
DE   AltName: Full=HACBP;
DE   Flags: Fragment;
GN   Name=CALR;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Pancreas;
RX   PubMed=1915668; DOI=10.1016/0014-4827(91)90484-c;
RA   Michalak M., Baksh S., Opas M.;
RT   "Identification and immunolocalization of calreticulin in pancreatic cells:
RT   no evidence for 'calciosomes'.";
RL   Exp. Cell Res. 197:91-99(1991).
CC   -!- FUNCTION: Calcium-binding chaperone that promotes folding, oligomeric
CC       assembly and quality control in the endoplasmic reticulum (ER) via the
CC       calreticulin/calnexin cycle (PubMed:1915668). This lectin interacts
CC       transiently with almost all of the monoglucosylated glycoproteins that
CC       are synthesized in the ER. Interacts with the DNA-binding domain of
CC       NR3C1 and mediates its nuclear export (By similarity). Involved in
CC       maternal gene expression regulation. May participate in oocyte
CC       maturation via the regulation of calcium homeostasis (By similarity).
CC       Present in the cortical granules of non-activated oocytes, is
CC       exocytosed during the cortical reaction in response to oocyte
CC       activation and might participate in the block to polyspermy (By
CC       similarity). {ECO:0000250|UniProtKB:P27797,
CC       ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7,
CC       ECO:0000269|PubMed:1915668}.
CC   -!- SUBUNIT: Monomer. Component of an EIF2 complex at least composed of
CC       CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts
CC       with PDIA3/ERp57 and SPACA9 (By similarity). Interacts with TRIM21.
CC       Interacts with NR3C1. Interacts with PPIB. Interacts (via P-domain)
CC       with PDIA5. Interacts with CLCC1 (By similarity).
CC       {ECO:0000250|UniProtKB:P14211, ECO:0000250|UniProtKB:P18418,
CC       ECO:0000250|UniProtKB:P27797}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:1915668}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P27797}. Cytolytic granule
CC       {ECO:0000250|UniProtKB:P27797}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface
CC       {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle,
CC       Cortical granule {ECO:0000250|UniProtKB:Q8K3H7}. Note=Also found in
CC       cell surface (T cells), cytosol and extracellular matrix. During oocyte
CC       maturation and after parthenogenetic activation accumulates in cortical
CC       granules. In pronuclear and early cleaved embryos localizes weakly to
CC       cytoplasm around nucleus and more strongly in the region near the
CC       cortex (By similarity). In cortical granules of non-activated oocytes,
CC       is exocytosed during the cortical reaction in response to oocyte
CC       activation (By similarity). {ECO:0000250|UniProtKB:P27797,
CC       ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7}.
CC   -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:1915668}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   PIR; A61141; A61141.
DR   IntAct; P28490; 1.
DR   PRIDE; P28490; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR   GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Calcium; Chaperone; Cytoplasm; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endoplasmic reticulum; Extracellular matrix;
KW   Lectin; Lysosome; Metal-binding; Reference proteome;
KW   Sarcoplasmic reticulum; Secreted; Zinc.
FT   CHAIN           1..>24
FT                   /note="Calreticulin"
FT                   /id="PRO_0000208520"
FT   NON_TER         24
SQ   SEQUENCE   24 AA;  2855 MW;  D5C76F2CB94B5C40 CRC64;
     EPAIYFKEQF LDGXGFTDXR IKEK