CALR_BOVIN
ID CALR_BOVIN Reviewed; 417 AA.
AC P52193; P28489; P42918; Q8SQ53;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Calreticulin;
DE AltName: Full=CRP55;
DE AltName: Full=Calregulin;
DE AltName: Full=HACBP;
DE Flags: Precursor;
GN Name=CALR; Synonyms=CRT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8373827; DOI=10.1016/0167-4838(93)90064-x;
RA Liu N., Fine R.E., Johnson R.J.;
RT "Comparison of cDNAs from bovine brain coding for two isoforms of
RT calreticulin.";
RL Biochim. Biophys. Acta 1202:70-76(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Hossain M.A., Takuwa K., Minakata H., Nakajima T.;
RT "Bovine brain calreticulin.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 18-417.
RC TISSUE=Brain;
RX PubMed=8135753; DOI=10.1042/bj2980435;
RA Matsuoka K., Seta K., Yamakawa Y., Okuyama T., Shinoda T., Isobe T.;
RT "Covalent structure of bovine brain calreticulin.";
RL Biochem. J. 298:435-442(1994).
RN [4]
RP PROTEIN SEQUENCE OF 18-30.
RC TISSUE=Liver;
RX PubMed=2016321; DOI=10.1016/s0021-9258(20)89624-0;
RA Milner R.E., Baksh S., Shemanko C., Carpenter M.R., Smillie L., Vance J.E.,
RA Opas M., Michalak M.;
RT "Calreticulin, and not calsequestrin, is the major calcium binding protein
RT of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum.";
RL J. Biol. Chem. 266:7155-7165(1991).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX PubMed=12782144; DOI=10.1016/s0945-053x(02)00117-8;
RA Somogyi E., Petersson U., Hultenby K., Wendel M.;
RT "Calreticulin -- an endoplasmic reticulum protein with calcium-binding
RT activity is also found in the extracellular matrix.";
RL Matrix Biol. 22:179-191(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13462; AAC37307.1; -; mRNA.
DR EMBL; AB067687; BAB86913.1; -; mRNA.
DR PIR; A33208; A33208.
DR PIR; S36799; S36799.
DR PIR; S43376; S43376.
DR RefSeq; NP_776425.1; NM_174000.2.
DR AlphaFoldDB; P52193; -.
DR SMR; P52193; -.
DR IntAct; P52193; 2.
DR STRING; 9913.ENSBTAP00000020111; -.
DR PaxDb; P52193; -.
DR PeptideAtlas; P52193; -.
DR PRIDE; P52193; -.
DR GeneID; 281036; -.
DR KEGG; bta:281036; -.
DR CTD; 811; -.
DR eggNOG; KOG0674; Eukaryota.
DR InParanoid; P52193; -.
DR OrthoDB; 822188at2759; -.
DR Proteomes; UP000009136; 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:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Lectin; Lysosome;
KW Metal-binding; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2016321,
FT ECO:0000269|PubMed:8135753"
FT CHAIN 18..417
FT /note="Calreticulin"
FT /id="PRO_0000004170"
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..270
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 CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 137..163
FT CONFLICT 1..99
FT /note="MLLPVPLLLGLLGLAAADPTVYFKEQFLDGDGWTERWIESKHKPDFGKFVLS
FT SGKFYGDQEKDKGLQTSQDARFYALSARFEPFSNKGQTLVVQFTVKH -> MCLNHFLL
FT SLVLSIVLLFHFVFYICLHHIVTFLREETVFFSEQFLTLDLKYKASKLSSIREALSMSK
FT VGIIENFCFSEISFLQESIKSHGRRTLVGCSPWGHE (in Ref. 1; AAC37307)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..21
FT /note="DPTV -> EPAI (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="KL -> NV (in Ref. 1; AAC37307)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="V -> L (in Ref. 1; AAC37307)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> E (in Ref. 1; AAC37307)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="G -> A (in Ref. 1; AAC37307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 48039 MW; 7BF812C7B5417BE9 CRC64;
MLLPVPLLLG LLGLAAADPT VYFKEQFLDG DGWTERWIES KHKPDFGKFV LSSGKFYGDQ
EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPAGLDQT
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPNN
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD DRAKIDDPTD SKPEDWDKPE
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPEYKGIWI HPEIDNPEYS
PDSNIYAYEN FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK
QDEEQRLHEE EEEKKGKEEE EADKDDDEDK DEDEEDEDEK EEEEEEDAAA GQAKDEL
