CALR_CRIGR
ID CALR_CRIGR Reviewed; 417 AA.
AC Q8K3H7;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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: Precursor;
GN Name=CALR; Synonyms=CRT {ECO:0000303|PubMed:11599052};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chung J.Y., Lee G.M.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11599052; DOI=10.1002/mrd.1103;
RA Munoz-Gotera R.J., Hernandez-Gonzalez E.O., Mendoza-Hernandez G.,
RA Contreras R.G., Mujica A.;
RT "Exocytosis of a 60 kDa protein (calreticulin) from activated hamster
RT oocytes.";
RL Mol. Reprod. Dev. 60:405-413(2001).
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. Involved in maternal gene expression regulation.
CC May participate in oocyte maturation via the regulation of calcium
CC homeostasis (By similarity). Present in the cortical granules of non-
CC activated oocytes, is exocytosed during the cortical reaction in
CC response to oocyte activation and might participate in the block to
CC polyspermy (PubMed:11599052). {ECO:0000250|UniProtKB:P27797,
CC ECO:0000250|UniProtKB:P28491, ECO:0000269|PubMed:11599052}.
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.
CC {ECO:0000250|UniProtKB:P14211, ECO:0000250|UniProtKB:P18418,
CC ECO:0000250|UniProtKB:P27797}.
CC -!- INTERACTION:
CC Q8K3H7; PRO_0000000091 [P05067]: APP; Xeno; NbExp=2; IntAct=EBI-9005068, EBI-3894543;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P27797}. 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:0000269|PubMed:11599052}. Note=Also found in cell
CC 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 (PubMed:11599052). {ECO:0000250|UniProtKB:P27797,
CC ECO:0000250|UniProtKB:P28491, ECO:0000269|PubMed:11599052}.
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; AY100688; AAM48568.1; -; mRNA.
DR RefSeq; NP_001231051.1; NM_001244122.1.
DR AlphaFoldDB; Q8K3H7; -.
DR SMR; Q8K3H7; -.
DR IntAct; Q8K3H7; 1.
DR STRING; 10029.NP_001231051.1; -.
DR GeneID; 100689096; -.
DR KEGG; cge:100689096; -.
DR CTD; 811; -.
DR eggNOG; KOG0674; Eukaryota.
DR OrthoDB; 822188at2759; -.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0060473; C:cortical granule; IDA: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:0030496; C:midbody; IDA:UniProtKB.
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; 2.10.250.10; -; 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; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein 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_0000004172"
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; 48243 MW; D617DA37D14F2D45 CRC64;
MLLSVPLLLG LLGLAAAEPA VYFKEQFLDG DDWTNRWVES KHKSDFGKFV LSSGKFYGDQ
EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPGSLDQK
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KASEKQMKDK
QDEEQRLKEE EEDKKRKEEE EAEDKEDEDD RDEDEEDEDE KEEDEEDTTP GQTKDEL
