ID   CALR_MACFU              Reviewed;         417 AA.
AC   Q2HWU3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   22-FEB-2023, entry version 73.
DE   RecName: Full=Calreticulin;
DE   Flags: Precursor;
GN   Name=CALR; Synonyms=CRT;
OS   Macaca fuscata fuscata (Japanese macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17214666; DOI=10.1111/j.1600-0684.2006.00186.x;
RA   Higashino A., Fukuhara R., Tezuka T., Kageyama T.;
RT   "Molecular cloning and gene expression of endoplasmic reticulum stress
RT   proteins in Japanese monkey, Macaca fuscata.";
RL   J. Med. Primatol. 35:376-383(2006).
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. This lectin interacts transiently with
CC       almost all of the monoglucosylated glycoproteins that are synthesized
CC       in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates
CC       its nuclear export (By similarity). Involved in maternal gene
CC       expression regulation. May participate in oocyte maturation via the
CC       regulation of calcium homeostasis (By similarity). Present in the
CC       cortical granules of non-activated oocytes, is exocytosed during the
CC       cortical reaction in response to oocyte activation and might
CC       participate in the block to polyspermy (By similarity).
CC       {ECO:0000250|UniProtKB:P27797, ECO:0000250|UniProtKB:P28491,
CC       ECO:0000250|UniProtKB:Q8K3H7}.
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 GABARAP. Interacts with CLCC1 (By
CC       similarity). {ECO:0000250|UniProtKB:P14211,
CC       ECO:0000250|UniProtKB:P18418, ECO:0000250|UniProtKB:P27797}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:P27797}. Cytoplasm, cytosol
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}. Cytolytic granule
CC       {ECO:0000250|UniProtKB:P27797}. Note=Also found in cell surface (T
CC       cells), cytosol and extracellular matrix. During oocyte maturation and
CC       after parthenogenetic activation accumulates in cortical granules. In
CC       pronuclear and early cleaved embryos localizes weakly to cytoplasm
CC       around nucleus and more strongly in the region near the cortex (By
CC       similarity). In cortical granules of non-activated oocytes, is
CC       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   -!- 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   -!- DOMAIN: Associates with PDIA3 through the tip of the extended arm
CC       formed by the P-domain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   EMBL; AB232155; BAE79725.1; -; mRNA.
DR   AlphaFoldDB; Q2HWU3; -.
DR   SMR; Q2HWU3; -.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 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:SF16; CALRETICULIN; 1.
DR   PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1.
DR   Pfam; PF00262; Calreticulin; 2.
DR   PIRSF; PIRSF002356; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 1.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Calcium; Chaperone; Cytoplasm; Cytoplasmic vesicle;
KW   Disulfide bond; Endoplasmic reticulum; Extracellular matrix; Hydroxylation;
KW   Lectin; Lysosome; Metal-binding; Repeat; Sarcoplasmic reticulum; Secreted;
KW   Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..417
FT                   /note="Calreticulin"
FT                   /id="PRO_0000246151"
FT   REPEAT          191..202
FT                   /note="1-1"
FT   REPEAT          210..221
FT                   /note="1-2"
FT   REPEAT          227..238
FT                   /note="1-3"
FT   REPEAT          244..255
FT                   /note="1-4"
FT   REPEAT          259..269
FT                   /note="2-1"
FT   REPEAT          273..283
FT                   /note="2-2"
FT   REPEAT          287..297
FT                   /note="2-3"
FT   REGION          18..197
FT                   /note="N-domain"
FT   REGION          191..255
FT                   /note="4 X approximate repeats"
FT   REGION          193..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..308
FT                   /note="P-domain"
FT   REGION          237..270
FT                   /note="Interaction with PPIB"
FT                   /evidence="ECO:0000250"
FT   REGION          259..297
FT                   /note="3 X approximate repeats"
FT   REGION          309..417
FT                   /note="C-domain"
FT   REGION          350..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           414..417
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        199..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..417
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         111
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         128
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         135
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         317
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         328
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         48
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27797"
FT   MOD_RES         64
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27797"
FT   MOD_RES         159
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27797"
FT   MOD_RES         209
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27797"
FT   DISULFID        105..137
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  48114 MW;  65506C9D1C341804 CRC64;
     MLLSVPLLLG LLGLAAAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV LSSGKFYGDE
     EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPNSLDQT
     DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN
     TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE
     HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
     PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK
     QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED KEEDEEEDVP GQAKDEL
//