ID CALR_HUMAN Reviewed; 417 AA. AC P27797; Q6IAT4; Q9UDG2; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 28-JAN-2026, entry version 266. DE RecName: Full=Calreticulin {ECO:0000303|PubMed:9427624}; DE AltName: Full=CRP55; DE AltName: Full=Calregulin; DE AltName: Full=Endoplasmic reticulum resident protein 60; DE Short=ERp60; DE AltName: Full=HACBP; DE AltName: Full=grp60; DE Flags: Precursor; GN Name=CALR {ECO:0000312|HGNC:HGNC:1455}; Synonyms=CRTC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2332496; DOI=10.1172/jci114582; RA McCauliffe D.P., Lux F.A., Lieu T.S., Sanz I., Hanke J., Newkirk M.M., RA Bachinski L.L., Itoh Y., Siciliano M.J., Reichlin M., Sontheimer R.D., RA Capra J.D.; RT "Molecular cloning, expression, and chromosome 19 localization of a human RT Ro/SS-A autoantigen."; RL J. Clin. Invest. 85:1379-1391(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1919005; RA Rokeach L.A., Haselby J.A., Meilof J.F., Smeenk R.J., Unnasch T.R., RA Greene B.M., Hoch S.O.; RT "Characterization of the autoantigen calreticulin."; RL J. Immunol. 147:3031-3039(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1733953; DOI=10.1016/s0021-9258(18)45916-9; RA McCauliffe D.P., Yang Y.S., Wilson J., Sontheimer R.D., Capra J.D.; RT "The 5'-flanking region of the human calreticulin gene shares homology with RT the human GRP78, GRP94, and protein disulfide isomerase promoters."; RL J. Biol. Chem. 267:2557-2562(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Liu J., Peng X., Yuan J., Qiang B.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, Pancreas, and Skin; 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 [11] RP PROTEIN SEQUENCE OF 18-48; 65-92; 96-114; 168-205 AND 257-354. RC TISSUE=Placenta; RX PubMed=7841019; DOI=10.3891/acta.chem.scand.48-0905; RA Houen G., Koch C.; RT "Human placental calreticulin: purification, characterization and RT association with other proteins."; RL Acta Chem. Scand. 48:905-911(1994). RN [12] RP PROTEIN SEQUENCE OF 18-41. RX PubMed=3260607; DOI=10.1172/jci113607; RA Lieu T.-S., Newkirk M.M., Capra J.D., Sontheimer R.D.; RT "Molecular characterization of human Ro/SS-A antigen. Amino terminal RT sequence of the protein moiety of human Ro/SS-A antigen and immunological RT activity of a corresponding synthetic peptide."; RL J. Clin. Invest. 82:96-101(1988). RN [13] RP PROTEIN SEQUENCE OF 18-36. RX PubMed=1911778; DOI=10.1021/bi00105a008; RA Rojiani M.V., Finlay B.B., Gray V., Dedhar S.; RT "In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen RT (calreticulin) with a highly conserved amino acid sequence in the RT cytoplasmic domain of integrin alpha subunits."; RL Biochemistry 30:9859-9866(1991). RN [14] RP PROTEIN SEQUENCE OF 18-32. RX PubMed=2400400; DOI=10.1042/bj2700545; RA Krause K.-H., Simmerman H.K.B., Jones L.R., Campbell K.P.; RT "Sequence similarity of calreticulin with a Ca2(+)-binding protein that co- RT purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60 cells."; RL Biochem. J. 270:545-548(1990). RN [15] RP PROTEIN SEQUENCE OF 18-28. RC TISSUE=Liver; RX PubMed=1286669; DOI=10.1002/elps.11501301201; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). RN [16] RP PROTEIN SEQUENCE OF 25-36; 74-111 AND 208-222, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [17] RP PROTEIN SEQUENCE OF 25-34; 56-62; 208-221 AND 273-278. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein RT database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [18] RP PROTEIN SEQUENCE OF 18-27, AND 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 [19] RP PROTEIN SEQUENCE OF 18-26. RC TISSUE=Colon carcinoma; RX PubMed=9150948; DOI=10.1002/elps.1150180344; RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.; RT "A two-dimensional gel database of human colon carcinoma proteins."; RL Electrophoresis 18:605-613(1997). RN [20] RP FUNCTION. RX PubMed=7876246; DOI=10.1074/jbc.270.9.4741; RA Nauseef W.M., McCormick S.J., Clark R.A.; RT "Calreticulin functions as a molecular chaperone in the biosynthesis of RT myeloperoxidase."; RL J. Biol. Chem. 270:4741-4747(1995). RN [21] RP INTERACTION WITH TRIM21. RX PubMed=8666824; RA Cheng S.T., Nguyen T.Q., Yang Y.S., Capra J.D., Sontheimer R.D.; RT "Calreticulin binds hYRNA and the 52-kDa polypeptide component of the RT Ro/SS-A ribonucleoprotein autoantigen."; RL J. Immunol. 156:4484-4491(1996). RN [22] RP SUBUNIT, AND INTERACTION WITH HLA-E. RX PubMed=9427624; DOI=10.1016/s0960-9822(98)70014-4; RA Braud V.M., Allan D.S., Wilson D., McMichael A.J.; RT "TAP- and tapasin-dependent HLA-E surface expression correlates with the RT binding of an MHC class I leader peptide."; RL Curr. Biol. 8:1-10(1998). RN [23] RP SUBUNIT, AND INTERACTION WITH HLA-G. RX PubMed=9640257; DOI=10.1046/j.1365-2567.1998.00439.x; RA Wainwright S.D., Simpson K.L., Holmes C.H.; RT "Calreticulin associates with non-HLA-A,-B class I proteins in the human RT choriocarcinoma cell lines JEG-3 and BeWo."; RL Immunology 93:437-445(1998). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=10358038; DOI=10.1074/jbc.274.24.16917; RA Arosa F.A., de Jesus O., Porto G., Carmo A.M., de Sousa M.; RT "Calreticulin is expressed on the cell surface of activated human RT peripheral blood T lymphocytes in association with major histocompatibility RT complex class I molecules."; RL J. Biol. Chem. 274:16917-16922(1999). RN [25] RP SUBUNIT, AND INTERACTION WITH HLA-F. RX PubMed=10605026; DOI=10.4049/jimmunol.164.1.319; RA Wainwright S.D., Biro P.A., Holmes C.H.; RT "HLA-F is a predominantly empty, intracellular, TAP-associated MHC class Ib RT protein with a restricted expression pattern."; RL J. Immunol. 164:319-328(2000). RN [26] RP FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION, AND MASS RP SPECTROMETRY. RX PubMed=11149926; DOI=10.1083/jcb.152.1.127; RA Holaska J.M., Black B.E., Love D.C., Hanover J.A., Leszyk J., Paschal B.M.; RT "Calreticulin is a receptor for nuclear export."; RL J. Cell Biol. 152:127-140(2001). RN [27] RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BOND, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Placenta; RX PubMed=11322874; DOI=10.1046/j.1432-1327.2001.02138.x; RA Hoejrup P., Roepstorff P., Houen G.; RT "Human placental calreticulin characterization of domain structure and RT post-translational modifications."; RL Eur. J. Biochem. 268:2558-2565(2001). RN [28] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [29] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [30] 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 [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [33] RP INTERACTION WITH PDIA5. RX PubMed=23614004; DOI=10.1371/journal.pone.0062021; RA Vinaik R., Kozlov G., Gehring K.; RT "Structure of the non-catalytic domain of the protein disulfide isomerase- RT related protein (PDIR) reveals function in protein binding."; RL PLoS ONE 8:E62021-E62021(2013). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [35] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-17, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [36] RP HYDROXYBUTYRYLATION AT LYS-64. RX PubMed=29192674; DOI=10.1038/cr.2017.149; RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J., RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.; RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation RT pathway."; RL Cell Res. 28:111-125(2018). RN [37] RP INTERACTION WITH CLCC1. RX PubMed=30157172; DOI=10.1371/journal.pgen.1007504; RA Li L., Jiao X., D'Atri I., Ono F., Nelson R., Chan C.C., Nakaya N., Ma Z., RA Ma Y., Cai X., Zhang L., Lin S., Hameed A., Chioza B.A., Hardy H., Arno G., RA Hull S., Khan M.I., Fasham J., Harlalka G.V., Michaelides M., Moore A.T., RA Coban Akdemir Z.H., Jhangiani S., Lupski J.R., Cremers F.P.M., Qamar R., RA Salman A., Chilton J., Self J., Ayyagari R., Kabir F., Naeem M.A., Ali M., RA Akram J., Sieving P.A., Riazuddin S., Baple E.L., Riazuddin S.A., RA Crosby A.H., Hejtmancik J.F.; RT "Mutation in the intracellular chloride channel CLCC1 associated with RT autosomal recessive retinitis pigmentosa."; RL PLoS Genet. 14:E1007504-E1007504(2018). RN [38] RP INVOLVEMENT IN MYELOPROLIFERATIVE NEOPLASMS. RX PubMed=24325356; DOI=10.1056/nejmoa1311347; RA Klampfl T., Gisslinger H., Harutyunyan A.S., Nivarthi H., Rumi E., RA Milosevic J.D., Them N.C., Berg T., Gisslinger B., Pietra D., Chen D., RA Vladimer G.I., Bagienski K., Milanesi C., Casetti I.C., Sant'Antonio E., RA Ferretti V., Elena C., Schischlik F., Cleary C., Six M., Schalling M., RA Schoenegger A., Bock C., Malcovati L., Pascutto C., Superti-Furga G., RA Cazzola M., Kralovics R.; RT "Somatic mutations of calreticulin in myeloproliferative neoplasms."; RL N. Engl. J. Med. 369:2379-2390(2013). RN [39] RP INVOLVEMENT IN MYELOPROLIFERATIVE NEOPLASMS. RX PubMed=24325359; DOI=10.1056/nejmoa1312542; RA Nangalia J., Massie C.E., Baxter E.J., Nice F.L., Gundem G., Wedge D.C., RA Avezov E., Li J., Kollmann K., Kent D.G., Aziz A., Godfrey A.L., Hinton J., RA Martincorena I., Van Loo P., Jones A.V., Guglielmelli P., Tarpey P., RA Harding H.P., Fitzpatrick J.D., Goudie C.T., Ortmann C.A., Loughran S.J., RA Raine K., Jones D.R., Butler A.P., Teague J.W., O'Meara S., McLaren S., RA Bianchi M., Silber Y., Dimitropoulou D., Bloxham D., Mudie L., Maddison M., RA Robinson B., Keohane C., Maclean C., Hill K., Orchard K., Tauro S., RA Du M.Q., Greaves M., Bowen D., Huntly B.J.P., Harrison C.N., Cross N.C.P., RA Ron D., Vannucchi A.M., Papaemmanuil E., Campbell P.J., Green A.R.; RT "Somatic CALR mutations in myeloproliferative neoplasms with nonmutated RT JAK2."; RL N. Engl. J. Med. 369:2391-2405(2013). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 195-205 IN COMPLEX WITH GABARAP, RP AND INTERACTION WITH GABARAP. RX PubMed=19154346; DOI=10.1111/j.1742-4658.2008.06857.x; RA Thielmann Y., Weiergraber O.H., Mohrluder J., Willbold D.; RT "Structural framework of the GABARAP-calreticulin interface -- implications RT for substrate binding to endoplasmic reticulum chaperones."; RL FEBS J. 276:1140-1152(2009). RN [41] {ECO:0007744|PDB:3POS, ECO:0007744|PDB:3POW} RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM RP IONS, AND DISULFIDE BOND. RX PubMed=21423620; DOI=10.1371/journal.pone.0017886; RA Chouquet A., Paidassi H., Ling W.L., Frachet P., Houen G., Arlaud G.J., RA Gaboriaud C.; RT "X-ray structure of the human calreticulin globular domain reveals a RT peptide-binding area and suggests a multi-molecular mechanism."; RL PLoS ONE 6:E17886-E17886(2011). RN [42] {ECO:0007744|PDB:5LK5} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 18-204 AND 303-368 OF MUTANT RP LYS-71 IN COMPLEX WITH CALCIUM, AND DISULFIDE BOND. RX PubMed=27840680; DOI=10.1107/s2052252516012847; RA Moreau C.P., Cioci G., Iannello M., Laffly E., Chouquet A., Ferreira A., RA Thielens N.M., Gaboriaud C.; RT "Structures of parasite calreticulins provide insights into their RT flexibility and dual carbohydrate/peptide-binding properties."; RL IUCrJ 3:408-419(2016). 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:7876246). Interacts with the DNA-binding domain of CC NR3C1 and mediates its nuclear export (PubMed:11149926). 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:P28491, CC ECO:0000250|UniProtKB:Q8K3H7, ECO:0000269|PubMed:11149926, CC ECO:0000269|PubMed:7876246}. 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 (PubMed:8666824). Interacts with NR3C1 (PubMed:11149926). Interacts CC with PPIB (PubMed:20801878). Interacts (via P-domain) with PDIA5 CC (PubMed:23614004). Interacts with GABARAP (PubMed:19154346). Interacts CC with HLA-E-B2M and HLA-G-B2M complexes (PubMed:9427624, CC PubMed:9640257). Interacts with HLA-F (PubMed:10605026). Interacts with CC CLCC1 (PubMed:30157172). {ECO:0000250|UniProtKB:P14211, CC ECO:0000250|UniProtKB:P18418, ECO:0000269|PubMed:10605026, CC ECO:0000269|PubMed:11149926, ECO:0000269|PubMed:19154346, CC ECO:0000269|PubMed:20801878, ECO:0000269|PubMed:23614004, CC ECO:0000269|PubMed:30157172, ECO:0000269|PubMed:8666824, CC ECO:0000269|PubMed:9427624, ECO:0000269|PubMed:9640257}. CC -!- INTERACTION: CC P27797; P05067: APP; NbExp=5; IntAct=EBI-1049597, EBI-77613; CC P27797; Q8N1W1-4: ARHGEF28; NbExp=3; IntAct=EBI-1049597, EBI-13062134; CC P27797; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-1049597, EBI-747505; CC P27797; O94983-5: CAMTA2; NbExp=3; IntAct=EBI-1049597, EBI-10176008; CC P27797; O75175: CNOT3; NbExp=3; IntAct=EBI-1049597, EBI-743073; CC P27797; Q6UXH1-2: CRELD2; NbExp=3; IntAct=EBI-1049597, EBI-21670927; CC P27797; P49184: DNASE1L1; NbExp=3; IntAct=EBI-1049597, EBI-20894690; CC P27797; Q8IY82: DRC7; NbExp=3; IntAct=EBI-1049597, EBI-10262896; CC P27797; Q99944: EGFL8; NbExp=3; IntAct=EBI-1049597, EBI-3924130; CC P27797; P16422: EPCAM; NbExp=3; IntAct=EBI-1049597, EBI-1171184; CC P27797; Q9NVM1: EVA1B; NbExp=3; IntAct=EBI-1049597, EBI-10314666; CC P27797; Q96GK7: FAHD2A; NbExp=3; IntAct=EBI-1049597, EBI-21647872; CC P27797; Q10981: FUT2; NbExp=3; IntAct=EBI-1049597, EBI-9090702; CC P27797; O95166: GABARAP; NbExp=4; IntAct=EBI-1049597, EBI-712001; CC P27797; P36382: GJA5; NbExp=3; IntAct=EBI-1049597, EBI-750433; CC P27797; P09471: GNAO1; NbExp=3; IntAct=EBI-1049597, EBI-715087; CC P27797; O15499: GSC2; NbExp=3; IntAct=EBI-1049597, EBI-19954058; CC P27797; P79483: HLA-DRB3; NbExp=3; IntAct=EBI-1049597, EBI-3910269; CC P27797; P14060: HSD3B1; NbExp=3; IntAct=EBI-1049597, EBI-17426018; CC P27797; P04792: HSPB1; NbExp=2; IntAct=EBI-1049597, EBI-352682; CC P27797; Q7Z6Z7-2: HUWE1; NbExp=3; IntAct=EBI-1049597, EBI-10975491; CC P27797; O75874: IDH1; NbExp=3; IntAct=EBI-1049597, EBI-715695; CC P27797; Q9ULR0: ISY1; NbExp=3; IntAct=EBI-1049597, EBI-2557660; CC P27797; A0JP07: KIAA1683; NbExp=3; IntAct=EBI-1049597, EBI-10171456; CC P27797; P26715: KLRC1; NbExp=3; IntAct=EBI-1049597, EBI-9018187; CC P27797; Q6P5S2: LEG1; NbExp=3; IntAct=EBI-1049597, EBI-11750531; CC P27797; P09382: LGALS1; NbExp=3; IntAct=EBI-1049597, EBI-1048875; CC P27797; O00214-2: LGALS8; NbExp=3; IntAct=EBI-1049597, EBI-12069522; CC P27797; P43356: MAGEA2B; NbExp=3; IntAct=EBI-1049597, EBI-5650739; CC P27797; Q7Z434: MAVS; NbExp=3; IntAct=EBI-1049597, EBI-995373; CC P27797; P11226: MBL2; NbExp=6; IntAct=EBI-1049597, EBI-5325353; CC P27797; Q8NCR3: MFI; NbExp=3; IntAct=EBI-1049597, EBI-744790; CC P27797; Q8TB02: MGC39372; NbExp=3; IntAct=EBI-1049597, EBI-25834188; CC P27797; Q96EY8: MMAB; NbExp=3; IntAct=EBI-1049597, EBI-7825413; CC P27797; P05164: MPO; NbExp=3; IntAct=EBI-1049597, EBI-2556173; CC P27797; P48039: MTNR1A; NbExp=3; IntAct=EBI-1049597, EBI-1188238; CC P27797; A2RUH7: MYBPHL; NbExp=3; IntAct=EBI-1049597, EBI-9088235; CC P27797; Q9NPC7: MYNN; NbExp=3; IntAct=EBI-1049597, EBI-3446748; CC P27797; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-1049597, EBI-11750983; CC P27797; Q8NCF5-2: NFATC2IP; NbExp=3; IntAct=EBI-1049597, EBI-12305293; CC P27797; Q96P20: NLRP3; NbExp=3; IntAct=EBI-1049597, EBI-6253230; CC P27797; Q8N323: NXPE1; NbExp=3; IntAct=EBI-1049597, EBI-25834085; CC P27797; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-1049597, EBI-9091052; CC P27797; P30101: PDIA3; NbExp=3; IntAct=EBI-1049597, EBI-979862; CC P27797; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-1049597, EBI-473160; CC P27797; Q8NBT0: POC1A; NbExp=3; IntAct=EBI-1049597, EBI-2557132; CC P27797; O14829: PPEF1; NbExp=3; IntAct=EBI-1049597, EBI-2931238; CC P27797; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-1049597, EBI-2860740; CC P27797; Q9Y617: PSAT1; NbExp=3; IntAct=EBI-1049597, EBI-709652; CC P27797; P43686: PSMC4; NbExp=3; IntAct=EBI-1049597, EBI-743997; CC P27797; Q13200: PSMD2; NbExp=3; IntAct=EBI-1049597, EBI-357648; CC P27797; Q9Y3Y4: PYGO1; NbExp=3; IntAct=EBI-1049597, EBI-3397474; CC P27797; Q13636: RAB31; NbExp=3; IntAct=EBI-1049597, EBI-725987; CC P27797; Q96E17: RAB3C; NbExp=3; IntAct=EBI-1049597, EBI-4287022; CC P27797; P61224: RAP1B; NbExp=3; IntAct=EBI-1049597, EBI-358143; CC P27797; P50749: RASSF2; NbExp=3; IntAct=EBI-1049597, EBI-960081; CC P27797; Q96I25: RBM17; NbExp=3; IntAct=EBI-1049597, EBI-740272; CC P27797; P52756: RBM5; NbExp=3; IntAct=EBI-1049597, EBI-714003; CC P27797; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-1049597, EBI-744081; CC P27797; Q02978: SLC25A11; NbExp=3; IntAct=EBI-1049597, EBI-359174; CC P27797; Q12824: SMARCB1; NbExp=5; IntAct=EBI-1049597, EBI-358419; CC P27797; Q3SY56: SP6; NbExp=3; IntAct=EBI-1049597, EBI-11175533; CC P27797; Q96L03: SPATA17; NbExp=3; IntAct=EBI-1049597, EBI-13322423; CC P27797; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-1049597, EBI-7082156; CC P27797; Q53T94: TAF1B; NbExp=3; IntAct=EBI-1049597, EBI-1560239; CC P27797; F6Y2X3: TAFAZZIN; NbExp=3; IntAct=EBI-1049597, EBI-25833693; CC P27797; Q03518: TAP1; NbExp=2; IntAct=EBI-1049597, EBI-747259; CC P27797; P48775: TDO2; NbExp=3; IntAct=EBI-1049597, EBI-743494; CC P27797; Q9BT49: THAP7; NbExp=3; IntAct=EBI-1049597, EBI-741350; CC P27797; P49746: THBS3; NbExp=3; IntAct=EBI-1049597, EBI-2530931; CC P27797; Q96JJ7-2: TMX3; NbExp=3; IntAct=EBI-1049597, EBI-25833898; CC P27797; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-1049597, EBI-12003398; CC P27797; Q68CL5-3: TPGS2; NbExp=3; IntAct=EBI-1049597, EBI-9091010; CC P27797; Q9ULW0: TPX2; NbExp=3; IntAct=EBI-1049597, EBI-1037322; CC P27797; Q9NX07: TRNAU1AP; NbExp=3; IntAct=EBI-1049597, EBI-12581310; CC P27797; P07437: TUBB; NbExp=3; IntAct=EBI-1049597, EBI-350864; CC P27797; Q7Z780: U2AF1; NbExp=3; IntAct=EBI-1049597, EBI-25833730; CC P27797; O75317: USP12; NbExp=3; IntAct=EBI-1049597, EBI-2511507; CC P27797; Q96EF9: ZHX1-C8orf76; NbExp=3; IntAct=EBI-1049597, EBI-25830993; CC P27797; Q9BQ29; NbExp=3; IntAct=EBI-1049597, EBI-22013570; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000269|PubMed:10358038, ECO:0000269|PubMed:11149926}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:11149926}. Secreted, extracellular space, CC extracellular matrix {ECO:0000305}. Cell surface CC {ECO:0000269|PubMed:10358038}. Sarcoplasmic reticulum lumen CC {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, CC Cortical granule {ECO:0000250|UniProtKB:Q8K3H7}. Cytolytic granule CC {ECO:0000269|PubMed:8418194}. Note=Also found in cell surface (T CC cells), cytosol and extracellular matrix (PubMed:10358038). During CC oocyte maturation and after parthenogenetic activation accumulates in CC cortical granules. In pronuclear and early cleaved embryos localizes CC weakly to cytoplasm around nucleus and more strongly in the region near CC the cortex (By similarity). In cortical granules of non-activated CC oocytes, is exocytosed during the cortical reaction in response to CC oocyte activation (By similarity). {ECO:0000250|UniProtKB:P28491, CC ECO:0000250|UniProtKB:Q8K3H7, ECO:0000269|PubMed:8418194}. 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. CC -!- DOMAIN: The interaction with glycans occurs through a binding site in CC the globular lectin domain. CC -!- DOMAIN: The zinc binding sites are localized to the N-domain. CC -!- DOMAIN: Associates with PDIA3 through the tip of the extended arm CC formed by the P-domain. CC -!- MASS SPECTROMETRY: Mass=46879; Method=MALDI; CC Evidence={ECO:0000269|PubMed:11149926}; CC -!- DISEASE: Note=CALR somatic mutations are frequently found in CC myeloproliferative neoplasms lacking JAK2 or MPL mutations. CC Myeloproliferative neoplasms are chronic myeloid cancers characterized CC by overproduction of mature blood cells, and may evolve into acute CC myeloid leukemia. In addition to chronic myeloid leukemia with the BCR- CC ABL fusion gene, the three most common myeloproliferative neoplasms are CC essential thrombocythemia, polycythemia vera, and myelofibrosis. CC {ECO:0000269|PubMed:24325356, ECO:0000269|PubMed:24325359}. CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to be the 52 kDa Ro autoantigen. CC {ECO:0000305|PubMed:2332496}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calreticulin entry; CC URL="https://en.wikipedia.org/wiki/Calreticulin"; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=Calreticulin; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_405"; 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; M32294; AAA36582.1; -; mRNA. DR EMBL; M84739; AAA51916.1; -; mRNA. DR EMBL; AY047586; AAL13126.1; -; mRNA. DR EMBL; AB451408; BAG70222.1; -; mRNA. DR EMBL; BT007448; AAP36116.1; -; mRNA. DR EMBL; CR457070; CAG33351.1; -; mRNA. DR EMBL; AD000092; AAB51176.1; -; Genomic_DNA. DR EMBL; CH471106; EAW84331.1; -; Genomic_DNA. DR EMBL; BC002500; AAH02500.1; -; mRNA. DR EMBL; BC007911; AAH07911.1; -; mRNA. DR EMBL; BC020493; AAH20493.1; -; mRNA. DR CCDS; CCDS12288.1; -. DR PIR; A42330; A37047. DR RefSeq; NP_004334.1; NM_004343.4. DR PDB; 2CLR; X-ray; 2.00 A; C/F=1-10. DR PDB; 3DOW; X-ray; 2.30 A; B=195-205. DR PDB; 3POS; X-ray; 1.65 A; A/B/C=18-204, A/B/C=302-368. DR PDB; 3POW; X-ray; 1.55 A; A=18-204, A=302-368. DR PDB; 5LK5; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=18-204, A/B/C/D/E/F/G/H/I/J=303-368. DR PDB; 5V90; X-ray; 3.25 A; B/D=238-273. DR PDB; 6ENY; EM; 5.80 A; G=18-417. DR PDB; 7QPD; EM; 3.73 A; C=18-417. DR PDB; 8TZO; EM; 3.10 A; C=1-417. DR PDB; 8TZR; EM; 3.50 A; C=1-417. DR PDBsum; 2CLR; -. DR PDBsum; 3DOW; -. DR PDBsum; 3POS; -. DR PDBsum; 3POW; -. DR PDBsum; 5LK5; -. DR PDBsum; 5V90; -. DR PDBsum; 6ENY; -. DR PDBsum; 7QPD; -. DR PDBsum; 8TZO; -. DR PDBsum; 8TZR; -. DR AlphaFoldDB; P27797; -. DR BMRB; P27797; -. DR EMDB; EMD-14119; -. DR EMDB; EMD-3906; -. DR EMDB; EMD-41764; -. DR EMDB; EMD-41767; -. DR SMR; P27797; -. DR BioGRID; 107262; 483. DR CORUM; P27797; -. DR DIP; DIP-104N; -. DR FunCoup; P27797; 2816. DR IntAct; P27797; 214. DR MINT; P27797; -. DR STRING; 9606.ENSP00000320866; -. DR DrugBank; DB00025; Antihemophilic factor, human recombinant. DR DrugBank; DB11093; Calcium citrate. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR DrugBank; DB09130; Copper. DR DrugBank; DB13949; Ferric cation. DR DrugBank; DB06245; Lanoteplase. DR DrugBank; DB13998; Lonoctocog alfa. DR DrugBank; DB01065; Melatonin. DR DrugBank; DB13999; Moroctocog alfa. DR DrugBank; DB14520; Tetraferric tricitrate decahydrate. DR MoonProt; P27797; -. DR TCDB; 8.A.165.1.2; the calnexin (calnexin) family. DR UniLectin; P27797; -. DR GlyConnect; 1060; 10 N-Linked glycans (1 site). DR GlyCosmos; P27797; 2 sites, 11 glycans. DR GlyGen; P27797; 4 sites, 37 N-linked glycans (1 site), 2 O-linked glycans (3 sites). DR iPTMnet; P27797; -. DR MetOSite; P27797; -. DR PhosphoSitePlus; P27797; -. DR SwissPalm; P27797; -. DR BioMuta; CALR; -. DR DMDM; 117501; -. DR OGP; P27797; -. DR REPRODUCTION-2DPAGE; IPI00020599; -. DR CPTAC; CPTAC-33; -. DR CPTAC; CPTAC-34; -. DR CPTAC; CPTAC-698; -. DR jPOST; P27797; -. DR MassIVE; P27797; -. DR PaxDb; 9606-ENSP00000320866; -. DR PeptideAtlas; P27797; -. DR PRIDE; P27797; -. DR ProteomicsDB; 54410; -. DR Pumba; P27797; -. DR TopDownProteomics; P27797; -. DR ABCD; P27797; 3 sequenced antibodies. DR Antibodypedia; 1028; 1163 antibodies from 47 providers. DR CPTC; P27797; 1 antibody. DR DNASU; 811; -. DR Ensembl; ENST00000316448.10; ENSP00000320866.4; ENSG00000179218.16. DR Ensembl; ENST00000586967.2; ENSP00000466037.2; ENSG00000179218.16. DR GeneID; 811; -. DR KEGG; hsa:811; -. DR MANE-Select; ENST00000316448.10; ENSP00000320866.4; NM_004343.4; NP_004334.1. DR AGR; HGNC:1455; -. DR CIViC; 811; 8 evidence items across 2 molecular profiles. DR ClinPGx; PA26046; -. DR CTD; 811; -. DR DisGeNET; 811; -. DR GeneCards; CALR; -. DR HGNC; HGNC:1455; CALR. DR HPA; ENSG00000179218; Low tissue specificity. DR MalaCards; CALR; -. DR MIM; 109091; gene. DR OpenTargets; ENSG00000179218; -. DR Orphanet; 131; Budd-Chiari syndrome. DR Orphanet; 3318; Essential thrombocythemia. DR Orphanet; 824; Primary myelofibrosis. DR VEuPathDB; HostDB:ENSG00000179218; -. DR eggNOG; KOG0674; Eukaryota. DR GeneTree; ENSGT00950000182915; -. DR HOGENOM; CLU_018224_0_2_1; -. DR InParanoid; P27797; -. DR OMA; KRDEICA; -. DR OrthoDB; 1938156at2759; -. DR PAN-GO; P27797; 4 GO annotations based on evolutionary models. DR PhylomeDB; P27797; -. DR PathwayCommons; P27797; -. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site. DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors. DR Reactome; R-HSA-3000484; Scavenging by Class F Receptors. DR Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes. DR Reactome; R-HSA-901042; Calnexin/calreticulin cycle. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; P27797; -. DR Agora; ENSG00000179218; -. DR BioGRID-ORCS; 811; 32 hits in 1177 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; CALR; human. DR EvolutionaryTrace; P27797; -. DR GeneWiki; Calreticulin; -. DR GenomeRNAi; 811; -. DR Pharos; P27797; Tbio. DR PRO; PR:P27797; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P27797; protein. DR Bgee; ENSG00000179218; Expressed in stromal cell of endometrium and 205 other cell types or tissues. DR ExpressionAtlas; P27797; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; TAS:BHF-UCL. 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; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:Ensembl. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IMP:CAFA. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0042824; C:MHC class I peptide loading complex; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0098794; C:postsynapse; IEA:Ensembl. DR GO; GO:0005840; C:ribosome; IDA:BHF-UCL. DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; TAS:BHF-UCL. DR GO; GO:0001849; F:complement component C1q complex binding; IPI:DisProt. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0042562; F:hormone binding; IEA:Ensembl. DR GO; GO:0005178; F:integrin binding; IPI:BHF-UCL. DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl. DR GO; GO:0140313; F:molecular sequestering activity; IDA:UniProt. DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL. DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:BHF-UCL. DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:DisProt. DR GO; GO:0042277; F:peptide binding; IEA:Ensembl. DR GO; GO:0044183; F:protein folding chaperone; IDA:BHF-UCL. DR GO; GO:0051087; F:protein-folding chaperone binding; TAS:BHF-UCL. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; TAS:BHF-UCL. DR GO; GO:0008270; F:zinc ion binding; TAS:BHF-UCL. 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:0098586; P:cellular response to virus; IEA:Ensembl. DR GO; GO:0090398; P:cellular senescence; IGI:BHF-UCL. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl. DR GO; GO:0036503; P:ERAD pathway; IBA:GO_Central. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; TAS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:BHF-UCL. DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0017148; P:negative regulation of translation; IDA:BHF-UCL. DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; IMP:CAFA. DR GO; GO:0042921; P:nuclear receptor-mediated glucocorticoid signaling pathway; TAS:BHF-UCL. DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IDA:UniProt. DR GO; GO:0045787; P:positive regulation of cell cycle; IGI:BHF-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:BHF-UCL. DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:CAFA. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:BHF-UCL. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB. DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB. DR GO; GO:0006457; P:protein folding; IDA:BHF-UCL. DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL. DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB. DR GO; GO:0051604; P:protein maturation; IDA:BHF-UCL. DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl. DR GO; GO:1904614; P:response to biphenyl; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:1903416; P:response to glycoside; IEA:Ensembl. DR GO; GO:1901652; P:response to peptide; 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:0051208; P:sequestering of calcium ion; TAS:BHF-UCL. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR DisProt; DP00333; -. DR FunFam; 2.10.250.10:FF:000002; Calreticulin; 1. DR FunFam; 2.60.120.200:FF:000113; Calreticulin 3; 1. DR FunFam; 2.60.120.200:FF:000122; Calreticulin 3; 1. 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 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; Glycoprotein; Hydroxylation; KW Lectin; Lysosome; Metal-binding; Proteomics identification; KW Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted; Signal; Zinc. FT SIGNAL 1..17 FT /evidence="ECO:0000269|PubMed:1286669, FT ECO:0000269|PubMed:1911778, ECO:0000269|PubMed:2400400, FT ECO:0000269|PubMed:3260607, ECO:0000269|PubMed:7841019, FT ECO:0000269|PubMed:8418194, ECO:0000269|PubMed:9150948, FT ECO:0007744|PubMed:25944712" FT CHAIN 18..417 FT /note="Calreticulin" FT /id="PRO_0000004173" 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 COMPBIAS 207..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 252..261 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 352..379 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 380..409 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:21423620, FT ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, FT ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:21423620, FT ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, FT ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5" FT BINDING 64 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:21423620, FT ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, FT ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5" 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:0000269|PubMed:21423620, FT ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, FT ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5" FT MOD_RES 48 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 64 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000269|PubMed:29192674" FT MOD_RES 159 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 209 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CARBOHYD 344 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 105..137 FT /evidence="ECO:0000269|PubMed:11322874, FT ECO:0000269|PubMed:21423620, ECO:0000269|PubMed:27840680, FT ECO:0007744|PDB:3POS, ECO:0007744|PDB:3POW, FT ECO:0007744|PDB:5LK5" FT STRAND 20..25 FT /evidence="ECO:0007829|PDB:3POW" FT HELIX 30..35 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:3POW" FT TURN 60..63 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 70..84 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:3POW" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 129..138 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 142..150 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 153..156 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 166..176 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 180..186 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 189..195 FT /evidence="ECO:0007829|PDB:3POW" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:3DOW" FT TURN 255..257 FT /evidence="ECO:0007829|PDB:5V90" FT TURN 303..306 FT /evidence="ECO:0007829|PDB:5LK5" FT STRAND 311..322 FT /evidence="ECO:0007829|PDB:3POW" FT STRAND 326..334 FT /evidence="ECO:0007829|PDB:3POW" FT HELIX 336..345 FT /evidence="ECO:0007829|PDB:3POW" FT HELIX 347..366 FT /evidence="ECO:0007829|PDB:3POW" SQ SEQUENCE 417 AA; 48142 MW; BC37C3C0F1054FB2 CRC64; MLLSVPLLLG LLGLAVAEPA 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 //