CALR_MOUSE
ID CALR_MOUSE Reviewed; 416 AA.
AC P14211; Q3TVD2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 222.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-48 AND 129-161.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2583110; DOI=10.1002/j.1460-2075.1989.tb08530.x;
RA Smith M.J., Koch G.L.E.;
RT "Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP),
RT a major calcium binding ER/SR protein.";
RL EMBO J. 8:3581-3586(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1398135; DOI=10.1016/0378-1119(92)90096-8;
RA Mazzarella R.A., Gold P., Cunningham M., Green M.;
RT "Determination of the sequence of an expressible cDNA clone encoding
RT ERp60/calregulin by the use of a novel nested set method.";
RL Gene 120:217-225(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 18-38.
RC TISSUE=Fibroblast;
RX PubMed=7523108; DOI=10.1002/elps.11501501101;
RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT "Separation and sequencing of familiar and novel murine proteins using
RT preparative two-dimensional gel electrophoresis.";
RL Electrophoresis 15:735-745(1994).
RN [6]
RP PROTEIN SEQUENCE OF 25-36; 56-64; 74-151; 154-159; 163-222; 225-272;
RP 323-351; 341-357 AND 392-413, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=8418194; DOI=10.1084/jem.177.1.1;
RA Dupuis M., Schaerer E., Krause K.-H., Tschopp J.;
RT "The calcium-binding protein calreticulin is a major constituent of lytic
RT granules in cytolytic T lymphocytes.";
RL J. Exp. Med. 177:1-7(1993).
RN [8]
RP IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR3; HSPA5
RP AND HSP90B1.
RX PubMed=16931514; DOI=10.1074/jbc.m605701200;
RA Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA Hershey J.W., Timchenko N.A.;
RT "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-
RT binding protein beta in old liver.";
RL J. Biol. Chem. 281:32806-32819(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH PPIB.
RX PubMed=20801878; DOI=10.1074/jbc.m110.160101;
RA Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F.,
RA Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.;
RT "Structural basis of cyclophilin B binding by the calnexin/calreticulin P-
RT domain.";
RL J. Biol. Chem. 285:35551-35557(2010).
RN [11]
RP INTERACTION WITH SPACA9.
RX PubMed=24256100; DOI=10.1186/1471-2121-14-50;
RA Bhattacharya R., Devi M.S., Dhople V.M., Jesudasan R.A.;
RT "A mouse protein that localizes to acrosome and sperm tail is regulated by
RT Y-chromosome.";
RL BMC Cell Biol. 14:50-50(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [13] {ECO:0007744|PDB:3O0V, ECO:0007744|PDB:3O0W, ECO:0007744|PDB:3O0X}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 18-368 IN COMPLEXES WITH CALCIUM
RP AND THE TETRASACCHARIDE
RP ALPHA-GLC-(1->3)-ALPHA-MAN-(1->2)-ALPHA-MAN-(1->2)-MAN, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BOND.
RX PubMed=20880849; DOI=10.1074/jbc.m110.168294;
RA Kozlov G., Pocanschi C.L., Rosenauer A., Bastos-Aristizabal S., Gorelik A.,
RA Williams D.B., Gehring K.;
RT "Structural basis of carbohydrate recognition by calreticulin.";
RL J. Biol. Chem. 285:38612-38620(2010).
RN [14] {ECO:0007744|PDB:3RG0}
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM
RP IONS, FUNCTION, AND DISULFIDE BOND.
RX PubMed=21652723; DOI=10.1074/jbc.m111.258467;
RA Pocanschi C.L., Kozlov G., Brockmeier U., Brockmeier A., Williams D.B.,
RA Gehring K.;
RT "Structural and functional relationships between the lectin and arm domains
RT of calreticulin.";
RL J. Biol. Chem. 286:27266-27277(2011).
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 (PubMed:20880849, PubMed:21652723). Interacts with the DNA-
CC binding domain of NR3C1 and mediates its nuclear export (By
CC similarity). Involved in maternal gene expression regulation. May
CC 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 (By similarity). {ECO:0000250|UniProtKB:P27797,
CC ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7,
CC ECO:0000269|PubMed:20880849, ECO:0000269|PubMed:21652723}.
CC -!- SUBUNIT: Monomer. Interacts with GABARAP, NR3C1, PDIA3/ERp57 and
CC TRIM21. Interacts (via P-domain) with PDIA5 (By similarity). Interacts
CC with PPIB (PubMed:20801878). Interacts with SPACA9 (PubMed:24256100).
CC Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR,
CC CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (PubMed:16931514). Interacts
CC with CLCC1 (By similarity). {ECO:0000250|UniProtKB:P18418,
CC ECO:0000250|UniProtKB:P27797, ECO:0000269|PubMed:16931514,
CC ECO:0000269|PubMed:20801878, ECO:0000269|PubMed:24256100}.
CC -!- INTERACTION:
CC P14211; P12023: App; NbExp=4; IntAct=EBI-644340, EBI-78814;
CC P14211; P57716: Ncstn; NbExp=2; IntAct=EBI-644340, EBI-998934;
CC P14211; P49769: Psen1; NbExp=3; IntAct=EBI-644340, EBI-990067;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:8418194}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P27797}. Cytolytic granule
CC {ECO:0000269|PubMed:8418194}. 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. Note=Also found in cell surface (T cells), cytosol
CC and extracellular matrix. During oocyte maturation and after
CC 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; X14926; CAA33053.1; -; mRNA.
DR EMBL; M92988; AAA37569.1; -; mRNA.
DR EMBL; AK075605; BAC35852.1; -; mRNA.
DR EMBL; AK160197; BAE35687.1; -; mRNA.
DR EMBL; BC003453; AAH03453.1; -; mRNA.
DR CCDS; CCDS22479.1; -.
DR PIR; S06763; S06763.
DR RefSeq; NP_031617.1; NM_007591.3.
DR PDB; 3O0V; X-ray; 2.30 A; A=18-206, A=301-368.
DR PDB; 3O0W; X-ray; 1.95 A; A=18-206, A=301-368.
DR PDB; 3O0X; X-ray; 2.01 A; A/B=18-206, A/B=301-368.
DR PDB; 3RG0; X-ray; 2.57 A; A=18-238, A=273-368.
DR PDBsum; 3O0V; -.
DR PDBsum; 3O0W; -.
DR PDBsum; 3O0X; -.
DR PDBsum; 3RG0; -.
DR AlphaFoldDB; P14211; -.
DR BMRB; P14211; -.
DR SMR; P14211; -.
DR BioGRID; 198458; 32.
DR IntAct; P14211; 13.
DR MINT; P14211; -.
DR STRING; 10090.ENSMUSP00000003912; -.
DR UniLectin; P14211; -.
DR CarbonylDB; P14211; -.
DR GlyConnect; 2175; 1 N-Linked glycan (1 site).
DR GlyGen; P14211; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P14211; -.
DR PhosphoSitePlus; P14211; -.
DR SwissPalm; P14211; -.
DR COMPLUYEAST-2DPAGE; P14211; -.
DR REPRODUCTION-2DPAGE; IPI00123639; -.
DR REPRODUCTION-2DPAGE; P14211; -.
DR SWISS-2DPAGE; P14211; -.
DR CPTAC; non-CPTAC-3966; -.
DR EPD; P14211; -.
DR jPOST; P14211; -.
DR MaxQB; P14211; -.
DR PaxDb; P14211; -.
DR PeptideAtlas; P14211; -.
DR PRIDE; P14211; -.
DR ProteomicsDB; 265512; -.
DR TopDownProteomics; P14211; -.
DR Antibodypedia; 1028; 1147 antibodies from 47 providers.
DR DNASU; 12317; -.
DR Ensembl; ENSMUST00000003912; ENSMUSP00000003912; ENSMUSG00000003814.
DR GeneID; 12317; -.
DR KEGG; mmu:12317; -.
DR UCSC; uc009mnp.1; mouse.
DR CTD; 811; -.
DR MGI; MGI:88252; Calr.
DR VEuPathDB; HostDB:ENSMUSG00000003814; -.
DR eggNOG; KOG0674; Eukaryota.
DR GeneTree; ENSGT00950000182915; -.
DR HOGENOM; CLU_018224_0_2_1; -.
DR InParanoid; P14211; -.
DR OMA; MMWCKTV; -.
DR OrthoDB; 822188at2759; -.
DR PhylomeDB; P14211; -.
DR TreeFam; TF338438; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
DR Reactome; R-MMU-901042; Calnexin/calreticulin cycle.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 12317; 13 hits in 77 CRISPR screens.
DR ChiTaRS; Calr; mouse.
DR PRO; PR:P14211; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P14211; protein.
DR Bgee; ENSMUSG00000003814; Expressed in ectoplacental cone and 244 other tissues.
DR ExpressionAtlas; P14211; baseline and differential.
DR Genevisible; P14211; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0042824; C:MHC class I peptide loading complex; IMP:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; ISO:MGI.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IMP:BHF-UCL.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:BHF-UCL.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IDA:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:1903416; P:response to glycoside; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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 3D-structure; Acetylation; Calcium; Chaperone; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Extracellular matrix; Hydroxylation; Lectin;
KW Lysosome; Metal-binding; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Secreted; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2583110,
FT ECO:0000269|PubMed:7523108"
FT CHAIN 18..416
FT /note="Calreticulin"
FT /id="PRO_0000004174"
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:0000269|PubMed:20801878"
FT REGION 259..297
FT /note="3 X approximate repeats"
FT REGION 309..416
FT /note="C-domain"
FT REGION 350..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 413..416
FT /note="Prevents secretion from ER"
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..416
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:0000269|PubMed:20880849"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20880849"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20880849"
FT BINDING 109
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000269|PubMed:20880849,
FT ECO:0007744|PDB:3O0W"
FT BINDING 111
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000269|PubMed:20880849,
FT ECO:0007744|PDB:3O0W"
FT BINDING 128
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000269|PubMed:20880849,
FT ECO:0007744|PDB:3O0W"
FT BINDING 135
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000269|PubMed:20880849,
FT ECO:0007744|PDB:3O0W"
FT BINDING 317
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000269|PubMed:20880849,
FT ECO:0007744|PDB:3O0W"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20880849"
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:0007744|PubMed:23806337"
FT DISULFID 105..137
FT /evidence="ECO:0000269|PubMed:20880849,
FT ECO:0000269|PubMed:21652723"
FT CONFLICT 272
FT /note="K -> R (in Ref. 3; BAE35687)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="E -> Q (in Ref. 3; BAE35687)"
FT /evidence="ECO:0000305"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:3O0W"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3O0V"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3O0W"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 70..84
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:3O0W"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:3O0W"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3O0W"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3RG0"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3RG0"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 311..322
FT /evidence="ECO:0007829|PDB:3O0W"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:3O0W"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:3O0W"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:3O0W"
SQ SEQUENCE 416 AA; 47995 MW; 24C03B00913408D8 CRC64;
MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV LSSGKFYGDL
EKDKGLQTSQ DARFYALSAK FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPSGLDQK
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK
QDEEQRLKEE EEDKKRKEEE EAEDKEDDDD RDEDEDEEDE KEEDEEESPG QAKDEL
