Full text data of CALR
CALR
(CRTC)
[Confidence: high (present in two of the MS resources)]
Calreticulin (CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP; grp60; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Calreticulin (CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP; grp60; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00020599
IPI00020599 Calreticulin precursor Calreticulin precursor membrane 1 2 2 n/a 2 n/a 1 n/a 1 n/a 3 1 3 1 n/a 2 1 2 2 1 ER lumen, cell curface, extracellular, cytosol n/a expected molecular weight found in band between 49-62 kDa
IPI00020599 Calreticulin precursor Calreticulin precursor membrane 1 2 2 n/a 2 n/a 1 n/a 1 n/a 3 1 3 1 n/a 2 1 2 2 1 ER lumen, cell curface, extracellular, cytosol n/a expected molecular weight found in band between 49-62 kDa
UniProt
P27797
ID CALR_HUMAN Reviewed; 417 AA.
AC P27797; Q6IAT4; Q9UDG2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 171.
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 AltName: Full=grp60;
DE Flags: Precursor;
GN Name=CALR; Synonyms=CRTC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT human 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;
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
RT with the human GRP78, GRP94, and protein disulfide isomerase
RT 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.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-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
RT 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
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
RT immunological 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
RT antigen (calreticulin) with a highly conserved amino acid sequence in
RT the cytoplasmic domain of integrin alpha subunits.";
RL Biochemistry 30:9859-9866(1991).
RN [14]
RP PROTEIN SEQUENCE OF 18-32.
RX PubMed=2400400;
RA Krause K.-H., Simmerman H.K.B., Jones L.R., Campbell K.P.;
RT "Sequence similarity of calreticulin with a Ca2(+)-binding protein
RT that co-purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60
RT 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 MASS 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
RT protein 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
RT lytic 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
RT of 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 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
RT histocompatibility complex class I molecules.";
RL J. Biol. Chem. 274:16917-16922(1999).
RN [23]
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.,
RA Paschal B.M.;
RT "Calreticulin is a receptor for nuclear export.";
RL J. Cell Biol. 152:127-140(2001).
RN [24]
RP PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND DISULFIDE BOND.
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 [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [27]
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.,
RA Buerckstuemmer T., 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 [28]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 195-205 IN COMPLEX WITH
RP GABARAP, 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 --
RT implications for substrate binding to endoplasmic reticulum
RT chaperones.";
RL FEBS J. 276:1140-1152(2009).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-368 IN COMPLEX WITH
RP CALCIUM 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.,
RA Arlaud G.J., 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).
CC -!- FUNCTION: Calcium-binding chaperone that promotes folding,
CC oligomeric assembly and quality control in the endoplasmic
CC reticulum (ER) via the calreticulin/calnexin cycle. This lectin
CC interacts transiently with almost all of the monoglucosylated
CC glycoproteins that are synthesized in the ER. Interacts with the
CC DNA-binding domain of NR3C1 and mediates its nuclear export.
CC Involved in maternal gene expression regulation. May participate
CC in oocyte maturation via the regulation of calcium homeostasis (By
CC similarity).
CC -!- SUBUNIT: Monomer. Component of an EIF2 complex at least composed
CC of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC Interacts with PDIA3/ERp57 (By similarity). Interacts with NR3C1
CC and TRIM21. Interacts with GABARAP.
CC -!- INTERACTION:
CC Q03518:TAP1; NbExp=2; IntAct=EBI-1049597, EBI-747259;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Cytoplasm,
CC cytosol. Secreted, extracellular space, extracellular matrix. Cell
CC surface. Sarcoplasmic reticulum lumen (By similarity). Note=Also
CC found in cell surface (T cells), cytosol and extracellular matrix.
CC Associated with the lytic granules in the cytolytic T-lymphocytes.
CC -!- DOMAIN: Can be divided into a N-terminal globular domain, a
CC proline-rich P-domain forming an elongated arm-like structure and
CC a C-terminal acidic domain. The P-domain binds one molecule of
CC calcium with high affinity, whereas the acidic C-domain binds
CC multiple calcium ions with low affinity.
CC -!- DOMAIN: The interaction with glycans occurs through a binding site
CC in 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; Range=18-417;
CC Source=PubMed:11149926;
CC -!- SIMILARITY: Belongs to the calreticulin family.
CC -!- CAUTION: Was originally (PubMed:2332496) thought to be the 52 kDa
CC Ro autoantigen.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calreticulin entry;
CC URL="http://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";
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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 PIR; A42330; A37047.
DR RefSeq; NP_004334.1; NM_004343.3.
DR UniGene; Hs.515162; -.
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=18-368.
DR PDB; 3POW; X-ray; 1.55 A; A=18-368.
DR PDBsum; 2CLR; -.
DR PDBsum; 3DOW; -.
DR PDBsum; 3POS; -.
DR PDBsum; 3POW; -.
DR DisProt; DP00333; -.
DR ProteinModelPortal; P27797; -.
DR SMR; P27797; 18-367.
DR DIP; DIP-104N; -.
DR IntAct; P27797; 24.
DR MINT; MINT-101756; -.
DR STRING; 9606.ENSP00000320866; -.
DR DrugBank; DB00009; Alteplase.
DR DrugBank; DB00029; Anistreplase.
DR DrugBank; DB00025; Antihemophilic Factor.
DR DrugBank; DB00015; Reteplase.
DR DrugBank; DB00031; Tenecteplase.
DR PhosphoSite; P27797; -.
DR DMDM; 117501; -.
DR DOSAC-COBS-2DPAGE; P27797; -.
DR OGP; P27797; -.
DR REPRODUCTION-2DPAGE; IPI00020599; -.
DR SWISS-2DPAGE; P27797; -.
DR UCD-2DPAGE; P27797; -.
DR PaxDb; P27797; -.
DR PRIDE; P27797; -.
DR DNASU; 811; -.
DR Ensembl; ENST00000316448; ENSP00000320866; ENSG00000179218.
DR GeneID; 811; -.
DR KEGG; hsa:811; -.
DR UCSC; uc002mvu.2; human.
DR CTD; 811; -.
DR GeneCards; GC19P013049; -.
DR HGNC; HGNC:1455; CALR.
DR HPA; CAB001513; -.
DR HPA; CAB019952; -.
DR HPA; HPA002242; -.
DR MIM; 109091; gene.
DR neXtProt; NX_P27797; -.
DR PharmGKB; PA26046; -.
DR eggNOG; NOG305105; -.
DR HOGENOM; HOG000192435; -.
DR HOVERGEN; HBG005407; -.
DR InParanoid; P27797; -.
DR KO; K08057; -.
DR OMA; VKLFPDG; -.
DR OrthoDB; EOG77126Z; -.
DR PhylomeDB; P27797; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_160300; Binding and Uptake of Ligands by Scavenger Receptors.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; CALR; human.
DR EvolutionaryTrace; P27797; -.
DR GeneWiki; Calreticulin; -.
DR GenomeRNAi; 811; -.
DR NextBio; 3292; -.
DR PRO; PR:P27797; -.
DR ArrayExpress; P27797; -.
DR Bgee; P27797; -.
DR CleanEx; HS_CALR; -.
DR Genevestigator; P27797; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; TAS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0042824; C:MHC class I peptide loading complex; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005844; C:polysome; ISS:BHF-UCL.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0050681; F:androgen receptor binding; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; TAS:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; TAS:BHF-UCL.
DR GO; GO:0001849; F:complement component C1q binding; TAS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0042562; F:hormone binding; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0044183; F:protein binding involved in protein folding; TAS:BHF-UCL.
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:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007050; P:cell cycle arrest; IGI:BHF-UCL.
DR GO; GO:0071285; P:cellular response to lithium ion; 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:0042921; P:glucocorticoid receptor signaling pathway; TAS: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 from RNA polymerase II promoter; IDA:BHF-UCL.
DR GO; GO:0017148; P:negative regulation of translation; ISS:BHF-UCL.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISS:BHF-UCL.
DR GO; GO:0045787; P:positive regulation of cell cycle; IGI:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IGI:BHF-UCL.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IGI:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; 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:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0040020; P:regulation of meiosis; IEA:Ensembl.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0051208; P:sequestering of calcium ion; TAS:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009169; Calreticulin.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Lectin;
KW Metal-binding; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW Secreted; Signal; Zinc.
FT SIGNAL 1 17
FT CHAIN 18 417 Calreticulin.
FT /FTId=PRO_0000004173.
FT REPEAT 191 202 1-1.
FT REPEAT 210 221 1-2.
FT REPEAT 227 238 1-3.
FT REPEAT 244 255 1-4.
FT REPEAT 259 269 2-1.
FT REPEAT 273 283 2-2.
FT REPEAT 287 297 2-3.
FT REGION 18 197 N-domain.
FT REGION 191 255 4 X approximate repeats.
FT REGION 198 308 P-domain.
FT REGION 259 297 3 X approximate repeats.
FT REGION 309 417 C-domain.
FT MOTIF 414 417 Prevents secretion from ER.
FT COMPBIAS 351 408 Asp/Glu/Lys-rich.
FT METAL 26 26 Calcium; via carbonyl oxygen.
FT METAL 62 62 Calcium; via carbonyl oxygen.
FT METAL 64 64 Calcium; via carbonyl oxygen.
FT METAL 328 328 Calcium.
FT BINDING 109 109 Carbohydrate (By similarity).
FT BINDING 111 111 Carbohydrate (By similarity).
FT BINDING 128 128 Carbohydrate (By similarity).
FT BINDING 135 135 Carbohydrate (By similarity).
FT BINDING 317 317 Carbohydrate (By similarity).
FT MOD_RES 48 48 N6-acetyllysine.
FT MOD_RES 159 159 N6-acetyllysine.
FT MOD_RES 209 209 N6-acetyllysine.
FT CARBOHYD 344 344 N-linked (GlcNAc...).
FT DISULFID 105 137
FT STRAND 20 25
FT HELIX 30 35
FT STRAND 37 39
FT STRAND 42 44
FT STRAND 49 52
FT TURN 60 63
FT STRAND 65 68
FT STRAND 70 84
FT STRAND 91 98
FT STRAND 104 107
FT STRAND 110 113
FT HELIX 119 121
FT STRAND 129 138
FT STRAND 142 150
FT STRAND 153 156
FT STRAND 166 176
FT STRAND 180 186
FT STRAND 189 195
FT HELIX 196 199
FT STRAND 201 203
FT STRAND 311 322
FT STRAND 326 334
FT HELIX 336 345
FT HELIX 347 366
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
//
ID CALR_HUMAN Reviewed; 417 AA.
AC P27797; Q6IAT4; Q9UDG2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 171.
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 AltName: Full=grp60;
DE Flags: Precursor;
GN Name=CALR; Synonyms=CRTC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT human 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;
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
RT with the human GRP78, GRP94, and protein disulfide isomerase
RT 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.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-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
RT 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
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
RT immunological 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
RT antigen (calreticulin) with a highly conserved amino acid sequence in
RT the cytoplasmic domain of integrin alpha subunits.";
RL Biochemistry 30:9859-9866(1991).
RN [14]
RP PROTEIN SEQUENCE OF 18-32.
RX PubMed=2400400;
RA Krause K.-H., Simmerman H.K.B., Jones L.R., Campbell K.P.;
RT "Sequence similarity of calreticulin with a Ca2(+)-binding protein
RT that co-purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60
RT 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 MASS 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
RT protein 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
RT lytic 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
RT of 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 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
RT histocompatibility complex class I molecules.";
RL J. Biol. Chem. 274:16917-16922(1999).
RN [23]
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.,
RA Paschal B.M.;
RT "Calreticulin is a receptor for nuclear export.";
RL J. Cell Biol. 152:127-140(2001).
RN [24]
RP PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND DISULFIDE BOND.
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 [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [27]
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.,
RA Buerckstuemmer T., 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 [28]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 195-205 IN COMPLEX WITH
RP GABARAP, 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 --
RT implications for substrate binding to endoplasmic reticulum
RT chaperones.";
RL FEBS J. 276:1140-1152(2009).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-368 IN COMPLEX WITH
RP CALCIUM 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.,
RA Arlaud G.J., 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).
CC -!- FUNCTION: Calcium-binding chaperone that promotes folding,
CC oligomeric assembly and quality control in the endoplasmic
CC reticulum (ER) via the calreticulin/calnexin cycle. This lectin
CC interacts transiently with almost all of the monoglucosylated
CC glycoproteins that are synthesized in the ER. Interacts with the
CC DNA-binding domain of NR3C1 and mediates its nuclear export.
CC Involved in maternal gene expression regulation. May participate
CC in oocyte maturation via the regulation of calcium homeostasis (By
CC similarity).
CC -!- SUBUNIT: Monomer. Component of an EIF2 complex at least composed
CC of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC Interacts with PDIA3/ERp57 (By similarity). Interacts with NR3C1
CC and TRIM21. Interacts with GABARAP.
CC -!- INTERACTION:
CC Q03518:TAP1; NbExp=2; IntAct=EBI-1049597, EBI-747259;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Cytoplasm,
CC cytosol. Secreted, extracellular space, extracellular matrix. Cell
CC surface. Sarcoplasmic reticulum lumen (By similarity). Note=Also
CC found in cell surface (T cells), cytosol and extracellular matrix.
CC Associated with the lytic granules in the cytolytic T-lymphocytes.
CC -!- DOMAIN: Can be divided into a N-terminal globular domain, a
CC proline-rich P-domain forming an elongated arm-like structure and
CC a C-terminal acidic domain. The P-domain binds one molecule of
CC calcium with high affinity, whereas the acidic C-domain binds
CC multiple calcium ions with low affinity.
CC -!- DOMAIN: The interaction with glycans occurs through a binding site
CC in 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; Range=18-417;
CC Source=PubMed:11149926;
CC -!- SIMILARITY: Belongs to the calreticulin family.
CC -!- CAUTION: Was originally (PubMed:2332496) thought to be the 52 kDa
CC Ro autoantigen.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calreticulin entry;
CC URL="http://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";
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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 PIR; A42330; A37047.
DR RefSeq; NP_004334.1; NM_004343.3.
DR UniGene; Hs.515162; -.
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=18-368.
DR PDB; 3POW; X-ray; 1.55 A; A=18-368.
DR PDBsum; 2CLR; -.
DR PDBsum; 3DOW; -.
DR PDBsum; 3POS; -.
DR PDBsum; 3POW; -.
DR DisProt; DP00333; -.
DR ProteinModelPortal; P27797; -.
DR SMR; P27797; 18-367.
DR DIP; DIP-104N; -.
DR IntAct; P27797; 24.
DR MINT; MINT-101756; -.
DR STRING; 9606.ENSP00000320866; -.
DR DrugBank; DB00009; Alteplase.
DR DrugBank; DB00029; Anistreplase.
DR DrugBank; DB00025; Antihemophilic Factor.
DR DrugBank; DB00015; Reteplase.
DR DrugBank; DB00031; Tenecteplase.
DR PhosphoSite; P27797; -.
DR DMDM; 117501; -.
DR DOSAC-COBS-2DPAGE; P27797; -.
DR OGP; P27797; -.
DR REPRODUCTION-2DPAGE; IPI00020599; -.
DR SWISS-2DPAGE; P27797; -.
DR UCD-2DPAGE; P27797; -.
DR PaxDb; P27797; -.
DR PRIDE; P27797; -.
DR DNASU; 811; -.
DR Ensembl; ENST00000316448; ENSP00000320866; ENSG00000179218.
DR GeneID; 811; -.
DR KEGG; hsa:811; -.
DR UCSC; uc002mvu.2; human.
DR CTD; 811; -.
DR GeneCards; GC19P013049; -.
DR HGNC; HGNC:1455; CALR.
DR HPA; CAB001513; -.
DR HPA; CAB019952; -.
DR HPA; HPA002242; -.
DR MIM; 109091; gene.
DR neXtProt; NX_P27797; -.
DR PharmGKB; PA26046; -.
DR eggNOG; NOG305105; -.
DR HOGENOM; HOG000192435; -.
DR HOVERGEN; HBG005407; -.
DR InParanoid; P27797; -.
DR KO; K08057; -.
DR OMA; VKLFPDG; -.
DR OrthoDB; EOG77126Z; -.
DR PhylomeDB; P27797; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_160300; Binding and Uptake of Ligands by Scavenger Receptors.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; CALR; human.
DR EvolutionaryTrace; P27797; -.
DR GeneWiki; Calreticulin; -.
DR GenomeRNAi; 811; -.
DR NextBio; 3292; -.
DR PRO; PR:P27797; -.
DR ArrayExpress; P27797; -.
DR Bgee; P27797; -.
DR CleanEx; HS_CALR; -.
DR Genevestigator; P27797; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; TAS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0042824; C:MHC class I peptide loading complex; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005844; C:polysome; ISS:BHF-UCL.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0050681; F:androgen receptor binding; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; TAS:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; TAS:BHF-UCL.
DR GO; GO:0001849; F:complement component C1q binding; TAS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0042562; F:hormone binding; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0044183; F:protein binding involved in protein folding; TAS:BHF-UCL.
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:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007050; P:cell cycle arrest; IGI:BHF-UCL.
DR GO; GO:0071285; P:cellular response to lithium ion; 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:0042921; P:glucocorticoid receptor signaling pathway; TAS: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 from RNA polymerase II promoter; IDA:BHF-UCL.
DR GO; GO:0017148; P:negative regulation of translation; ISS:BHF-UCL.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISS:BHF-UCL.
DR GO; GO:0045787; P:positive regulation of cell cycle; IGI:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IGI:BHF-UCL.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IGI:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; 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:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0040020; P:regulation of meiosis; IEA:Ensembl.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0051208; P:sequestering of calcium ion; TAS:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009169; Calreticulin.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Lectin;
KW Metal-binding; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW Secreted; Signal; Zinc.
FT SIGNAL 1 17
FT CHAIN 18 417 Calreticulin.
FT /FTId=PRO_0000004173.
FT REPEAT 191 202 1-1.
FT REPEAT 210 221 1-2.
FT REPEAT 227 238 1-3.
FT REPEAT 244 255 1-4.
FT REPEAT 259 269 2-1.
FT REPEAT 273 283 2-2.
FT REPEAT 287 297 2-3.
FT REGION 18 197 N-domain.
FT REGION 191 255 4 X approximate repeats.
FT REGION 198 308 P-domain.
FT REGION 259 297 3 X approximate repeats.
FT REGION 309 417 C-domain.
FT MOTIF 414 417 Prevents secretion from ER.
FT COMPBIAS 351 408 Asp/Glu/Lys-rich.
FT METAL 26 26 Calcium; via carbonyl oxygen.
FT METAL 62 62 Calcium; via carbonyl oxygen.
FT METAL 64 64 Calcium; via carbonyl oxygen.
FT METAL 328 328 Calcium.
FT BINDING 109 109 Carbohydrate (By similarity).
FT BINDING 111 111 Carbohydrate (By similarity).
FT BINDING 128 128 Carbohydrate (By similarity).
FT BINDING 135 135 Carbohydrate (By similarity).
FT BINDING 317 317 Carbohydrate (By similarity).
FT MOD_RES 48 48 N6-acetyllysine.
FT MOD_RES 159 159 N6-acetyllysine.
FT MOD_RES 209 209 N6-acetyllysine.
FT CARBOHYD 344 344 N-linked (GlcNAc...).
FT DISULFID 105 137
FT STRAND 20 25
FT HELIX 30 35
FT STRAND 37 39
FT STRAND 42 44
FT STRAND 49 52
FT TURN 60 63
FT STRAND 65 68
FT STRAND 70 84
FT STRAND 91 98
FT STRAND 104 107
FT STRAND 110 113
FT HELIX 119 121
FT STRAND 129 138
FT STRAND 142 150
FT STRAND 153 156
FT STRAND 166 176
FT STRAND 180 186
FT STRAND 189 195
FT HELIX 196 199
FT STRAND 201 203
FT STRAND 311 322
FT STRAND 326 334
FT HELIX 336 345
FT HELIX 347 366
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
//
MIM
109091
*RECORD*
*FIELD* NO
109091
*FIELD* TI
*109091 CALRETICULIN; CALR
;;CRT;;
AUTOANTIGEN Ro; RO;;
COMPLEMENT COMPONENT C1q RECEPTOR; CC1QR
read more*FIELD* TX
DESCRIPTION
Calreticulin is a multifunctional protein that acts as a major
Ca(2+)-binding (storage) protein in the lumen of the endoplasmic
reticulum. It is also found in the nucleus, suggesting that it may have
a role in transcription regulation (Burns et al., 1994).
CLONING
Calreticulin binds to the synthetic peptide KLGFFKR, which is almost
identical to an amino acid sequence in the DNA-binding domain of the
superfamily of nuclear receptors. McCauliffe et al. (1990) showed that
calreticulin binds to antibodies in certain sera of systemic lupus and
Sjogren patients which contain anti-Ro/SSA antibodies, that it is highly
conserved among species, and that it is located in the endoplasmic and
sarcoplasmic reticulum where it may bind calcium. With synthetic
oligonucleotides corresponding to the amino acid sequence, McCauliffe et
al. (1990) isolated full-length CALR cDNA that encodes a human Ro
ribonucleoprotein autoantigen. The deduced 417-amino acid protein has a
predicted molecular mass of 48 kD. Southern filter hybridization
analysis showed that the CALR gene is not highly polymorphic and exists
in single copy in the human genome.
Frank (1994) pointed out that the CALR gene mapped to chromosome 19p
encodes the 48-kD calreticulin, a protein with Ro/SSA properties. Itoh
et al. (1991) showed that the 52-kD and the 60-kD forms of Ro/SSA
ribonucleoproteins are encoded by separate genes mapping to chromosome
11 (TRIM21; 109092) and chromosome 1 (TROVE2; 600063), respectively.
By Northern blot analysis of human tissues, Persson et al. (2002) found
ubiquitous expression of a 1.9-kb CALR transcript.
GENE FUNCTION
Burns et al. (1994) reported that the amino terminus of calreticulin
interacts with the DNA-binding domain of the glucocorticoid receptor and
prevents the receptor from binding to its specific glucocorticoid
response element. Dedhar et al. (1994) showed that calreticulin can
inhibit the binding of androgen receptor to its hormone-responsive DNA
element and can inhibit androgen receptor and retinoic acid receptor
transcriptional activities in vivo, as well as retinoic acid-induced
neuronal differentiation. Thus, calreticulin can act as an important
modulator of the regulation of gene transcription by nuclear hormone
receptors.
Boehm et al. (1994) showed that SLE is associated with increased
autoantibody titers against calreticulin but that calreticulin is not a
Ro/SS-A antigen. Orth et al. (1996) found increased autoantibody titers
against human calreticulin in infants with complete congenital heart
block (234700) of both the IgG and IgM classes.
THBS1 (188060) or a peptide of the 19-amino acid active site in its
heparin-binding domain signals focal adhesion disassembly through
interaction with a cell surface form of CRT. Using bovine aortic
endothelial cells and wildtype and low density lipoprotein
receptor-related protein (LRP, or LRP1; 107770) -/- mouse fibroblasts,
Orr et al. (2003) showed that Lrp interacted with Crt and was required
to mediate focal adhesion disassembly and downstream signaling for
reorganization of focal adhesions. Binding of the LRP ligand RAP
(LRPAP1; 104225) to purified human LRP inhibited interaction between
recombinant human CRT and LRP.
Gardai et al. (2005) stated that calreticulin on the surface of
apoptotic cells serves as a recognition and clearance ligand by
activating the internalization receptor LRP1 (107770) on the responding
phagocyte cell surface. Using mouse and human cells, they found that the
surface expression of calreticulin increased and calreticulin was
redistributed during apoptosis, possibly enhancing stimulation of LRP1
on the phagocyte. In addition, CD47 (601028) on the apoptotic cell
surface was altered and/or lost, which reduced the activation of
SIRP-alpha (PTPNS1; 602461) on the phagocytic cell surface, resulting in
phagocytosis.
In CT26 mouse colon cancer cells, Obeid et al. (2007) demonstrated that
anthracyclins induced immunogenic cell death by way of a rapid,
preapoptotic translocation of calreticulin to the cell surface. Blockade
or knockdown of Calr suppressed phagocytosis of anthracyclin-treated
tumor cells by dendritic cells and abolished their immunogenicity in
mice. Anthracyclin-induced Calr translocation was mimicked by inhibition
of the protein phosphatase-1 (see PPP1CA; 176875)/Gadd34 (PPP1R15A;
611048) complex. Administration of recombinant Calr or inhibitors of
Pp1/Gadd34 restored immunogenicity of cell death elicited by etoposide
and mitomycin C and enhanced their antitumor effects in vivo. Obeid et
al. (2007) concluded that CALR plays a key role in determining
anticancer immune responses.
Using flow cytometric and confocal microscopy analyses, Zeng et al.
(2006) demonstrated that NYESO1 (CTAG1B; 300156) bound to immature
dendritic cells (DCs), macrophages, and monocytes, but not to T cells or
B cells. Immunoprecipitation and tandem mass spectrometric analyses
showed that CALR was the only DC surface-specific protein that
interacted with NYESO1. Anti-CALR inhibited NYESO1 binding on immature
DCs and its cross-presentation to CD8 (see 186910)-positive T cells.
Surface plasmon resonance analysis showed that NYESO1 bound to CALR, but
not to other molecular chaperones. Zeng et al. (2006) proposed that
NYESO1 binding to CALR on macrophages and DCs provides a link between
NYESO1, the innate immune system, possibly the adaptive immune response
against NYESO1.
GENE STRUCTURE
Persson et al. (2002) stated that the CALR gene contains 9 exons and
spans 4.2 kb.
MAPPING
By analysis of somatic cell hybrids, McCauliffe et al. (1990) assigned
the CALR gene to chromosome 19p. There was perfect concordance with LDLR
(606945) but discordance with C3 (120700). Thus, the calreticulin, or
RO, locus may be located in the region of chromosome 19pter-p13.2,
distal to C3 and near LDLR.
Rooke et al. (1997) mapped the mouse Calr gene to chromosome 8.
MOLECULAR GENETICS
- Somatic Mutation in Myeloproliferative Neoplasms
Klampfl et al. (2013) identified calreticulin mutations in 78 of 311
(25%) tumor samples from patients with essential thrombocythemia (see
187950), and in 72 of 203 (35%) tumor samples from patients with primary
myelofibrosis (254450). Mutations in CALR, JAK2 (147796), and MPL
(159530) were mutually exclusive. Among 289 thrombocythemia samples from
a combined cohort of patients with nonmutated JAK2 and MPL, 195 (67%)
had mutated CALR; among 120 primary myelofibrosis samples from the same
cohort, 105 (88%) had mutated CALR. A total of 36 types of insertions or
deletions were identified in exon 9 of CALR, all causing a frameshift to
the same alternative reading frame and generating a novel C-terminal
peptide in the mutant calreticulin. Overexpression of the most frequent
CALR deletion (109091.0001) caused cytokine-independent growth in vitro
owing to the activation of STAT5 (601511). Patients with mutated CALR
had a lower risk of thrombosis and longer overall survival than patients
with mutated JAK2.
Nangalia et al. (2013) identified somatic CALR mutations in 70 to 84% of
samples of myeloproliferative neoplasms with nonmutated JAK2, in 8% of
myelodysplasia samples, in occasional samples of other myeloid cancers,
and in no other hematologic cancers. A total of 148 CALR mutations were
identified with 19 distinct variants. Mutations were located in exon 9
and generated a +1 basepair frameshift, which would result in a mutant
protein with a novel C terminal. Mutant calreticulin was observed in the
endoplasmic reticulum without increased cell surface or Golgi
accumulation. Patients with myeloproliferative neoplasms carrying CALR
mutations presented with higher platelet counts and lower hemoglobin
levels than patients with mutated JAK2. Mutation of CALR was detected in
hematopoietic stem and progenitor cells. Clonal analyses showed CALR
mutations in the earliest phylogenetic node, a finding consistent with
its role as an initiating mutation in some patients.
*FIELD* AV
.0001
MYELOFIBROSIS, SOMATIC
THROMBOCYTHEMIA, SOMATIC, INCLUDED
CALR, 52-BP DEL, EX9
Klampfl et al. (2013) and Nangalia et al. (2013) identified a somatic
52-bp deletion in exon 9 of the CALR gene (1092_1143del) in patients
with myeloproliferative neoplasms, including myelofibrosis (254450) and
essential thrombocythemia (see 187950). CALR mutations and JAK2 and MPL
mutations were mutually exclusive. The 52-bp mutation resulted in
frameshift and premature termination (L367fsTer46). Klampfl et al.
(2013) identified a total of 36 types of somatic insertion or deletion
within exon 9 of CALR, all of which caused a frameshift to the same
alternative reading frame and generated a novel C-terminal peptide in
the mutant calreticulin. Klampfl et al. (2013) identified insertions or
deletions in exon 9 of CALR in 88% of individuals with primary
myelofibrosis with nonmutated JAK2 or MPL. The 52-bp deletion accounted
for 53% of all cases of mutated CALR among several types of
myoproliferative neoplasm. Overexpression of this mutation resulted in
cytokine-independent growth in vitro through the activation of STAT5
(601511). Nangalia et al. (2013) identified 23 patients with
myelofibrosis who carried the L367fsTer46 mutation. Overall, Nangalia et
al. (2013) identified 19 different somatic CALR mutations, all in exon 9
and all of which generated a +1 frameshift resulting in a mutant protein
with a novel C terminal. CALR mutations were present in 18 of 32
patients (56%) with primary myelofibrosis and in 12 of 14 patients (86%)
with progression of essential thrombocythemia to myelofibrosis. Neither
Klampfl et al. (2013) nor Nangalia et al. (2013) detected CALR mutation
in individuals with polycythemia vera.
*FIELD* RF
1. Boehm, J.; Orth, T.; Van Nguyen, P.; Soling, H. D.: Systemic lupus
erythematosus is associated with increased auto-antibody titers against
calreticulin and grp94, but calreticulin is not the Ro/SS-A antigen. Europ.
J. Clin. Invest. 24: 248-257, 1994.
2. Burns, K.; Duggan, B.; Atkinson, E. A.; Famulski, K. S.; Nemer,
M.; Bleackley, R. C.; Michalak, M.: Modulation of gene expression
by calreticulin binding to the glucocorticoid receptor. Nature 367:
476-480, 1994.
3. Dedhar, S.; Rennie, P. S.; Shago, M.; Hagesteijn, C.-Y. L.; Yang,
H.; Filmus, J.; Hawley, R. G.; Bruchovsky, N.; Cheng, H.; Matusik,
R. J.; Giguere, V.: Inhibition of nuclear hormone receptor activity
by calreticulin. Nature 367: 480-483, 1994.
4. Frank, M. B.: Personal Communication. Oklahoma City, Okla.
6/3/1994.
5. Gardai, S. J.; McPhillips, K. A.; Frasch, S. C.; Janssen, W. J.;
Starefeldt, A.; Murphy-Ullrich, J. E.; Bratton, D. L.; Oldenborg,
P.-A.; Michalak, M.; Henson, P. M.: Cell-surface calreticulin initiates
clearance of viable or apoptotic cells through trans-activation of
LRP on the phagocyte. Cell 123: 321-334, 2005.
6. Itoh, K.; Itoh, Y.; Frank, M. B.: Protein heterogeneity in the
human Ro/SSA ribonucleoproteins: the 52- and 60-kD Ro/SSA autoantigens
are encoded by separate genes. J. Clin. Invest. 87: 177-186, 1991.
7. Klampfl, T.; Gisslinger, H.; Harutyunyan, A. S.; Nivarthi, H.;
Rumi, E.; Milosevic, J. D.; Them, N. C. C.; Berg, T.; Gisslinger,
B.; Pietra, D.; Chen, D.; Vladimer, G. I.; and 17 others: Somatic
mutations of calreticulin in myeloproliferative neoplasms. New Eng.
J. Med. 369: 2379-2390, 2013.
8. McCauliffe, D. P.; Lux, F. A.; Lieu, T.-S.; Sanz, I.; Hanke, J.;
Newkirk, M. M.; Bachinski, L. L.; Itoh, Y.; Siciliano, M. J.; Reichlin,
M.; Sontheimer, R. D.; Capra, J. D.: Molecular cloning, expression,
and chromosome 19 localization of a human Ro/SS-A autoantigen. J.
Clin. Invest. 85: 1379-1391, 1990.
9. McCauliffe, D. P.; Zappi, E.; Lieu, T.-S.; Michalak, M.; Sontheimer,
R. D.; Capra, J. D.: A human Ro/SS-A autoantigen is the homologue
of calreticulin and is highly homologous with onchocercal RAL-1 antigen
and an aplysia 'memory molecule.'. J. Clin. Invest. 86: 332-335,
1990.
10. Nangalia, J.; Massie, C. E.; Baxter, E. J.; Nice, F. L.; Gundem,
G.; Wedge, D. C.; Avezov, E.; Li, J.; Kollmann, K.; Kent, D. G.; Aziz,
A.; Godfrey, A. L.; and 40 others: Somatic CALR mutations in myeloproliferative
neoplasms with nonmutated JAK2. New Eng. J. Med. 369: 2391-2405,
2013.
11. Obeid, M.; Tesniere, A.; Ghiringhelli, F.; Fimia, G. M.; Apetoh,
L.; Perfettini, J.-L.; Castedo, M.; Mignot, G.; Panaretakis, T.; Casares,
N.; Metivier, D.; Larochette, N.; van Endert, P.; Ciccosanti, F.;
Piacentini, M.; Zitvogel, L.; Kroemer, G.: Calreticulin exposure
dictates immunogenicity of cancer cell death. Nature Med. 13: 54-61,
2007.
12. Orr, A. W.; Pedraza, C. E.; Pallero, M. A.; Elzie, C. A.; Goicoechea,
S.; Strickland, D. K.; Murphy-Ullrich, J. E.: Low density lipoprotein
receptor-related protein is a calreticulin coreceptor that signals
focal adhesion disassembly. J. Cell Biol. 161: 1179-1189, 2003.
13. Orth, T.; Dorner, T.; Meyer Zum Buschenfelde, K.-H.; Mayet, W.-J.
: Complete congenital heart block is associated with increased autoantibody
titers against calreticulin. Europ. J. Clin. Invest. 26: 205-215,
1996.
14. Persson, S.; Rosenquist, M.; Sommarin, M.: Identification of
a novel calreticulin isoform (Crt2) in human and mouse. Gene 297:
151-158, 2002.
15. Rooke, K.; Briquet-Laugier, V.; Xia, Y.-R.; Lusis, A. J.; Doolittle,
M. H.: Mapping of the gene for calreticulin (Calr) to mouse chromosome
8. Mammalian Genome 8: 870-871, 1997.
16. Zeng, G.; Aldridge, M. E.; Tian, X.; Seiler, D.; Zhang, X.; Jin,
Y.; Rao, J.; Li, W.; Chen, D.; Langford, M. P.; Duggan, C.; Belldegrun,
A. S.; Dubinett, S. M.: Dendritic cell surface calreticulin is a
receptor for NY-ESO-1: direct interactions between tumor-associated
antigen and the innate immune system. J. Immun. 177: 3582-3589,
2006.
*FIELD* CN
Ada Hamosh - updated: 02/07/2014
Patricia A. Hartz - updated: 6/11/2013
Patricia A. Hartz - updated: 8/10/2007
Paul J. Converse - updated: 3/9/2007
Marla J. F. O'Neill - updated: 2/26/2007
Victor A. McKusick - updated: 11/21/1997
*FIELD* CD
Victor A. McKusick: 8/15/1990
*FIELD* ED
alopez: 02/07/2014
mgross: 6/11/2013
wwang: 9/7/2007
wwang: 8/17/2007
terry: 8/10/2007
mgross: 5/21/2007
mgross: 3/14/2007
terry: 3/9/2007
wwang: 2/26/2007
ckniffin: 6/5/2002
terry: 11/26/1997
terry: 11/21/1997
terry: 5/2/1996
mark: 4/27/1996
terry: 4/22/1996
carol: 11/30/1994
jason: 7/28/1994
mimadm: 4/21/1994
pfoster: 3/25/1994
carol: 3/1/1993
carol: 5/22/1992
*RECORD*
*FIELD* NO
109091
*FIELD* TI
*109091 CALRETICULIN; CALR
;;CRT;;
AUTOANTIGEN Ro; RO;;
COMPLEMENT COMPONENT C1q RECEPTOR; CC1QR
read more*FIELD* TX
DESCRIPTION
Calreticulin is a multifunctional protein that acts as a major
Ca(2+)-binding (storage) protein in the lumen of the endoplasmic
reticulum. It is also found in the nucleus, suggesting that it may have
a role in transcription regulation (Burns et al., 1994).
CLONING
Calreticulin binds to the synthetic peptide KLGFFKR, which is almost
identical to an amino acid sequence in the DNA-binding domain of the
superfamily of nuclear receptors. McCauliffe et al. (1990) showed that
calreticulin binds to antibodies in certain sera of systemic lupus and
Sjogren patients which contain anti-Ro/SSA antibodies, that it is highly
conserved among species, and that it is located in the endoplasmic and
sarcoplasmic reticulum where it may bind calcium. With synthetic
oligonucleotides corresponding to the amino acid sequence, McCauliffe et
al. (1990) isolated full-length CALR cDNA that encodes a human Ro
ribonucleoprotein autoantigen. The deduced 417-amino acid protein has a
predicted molecular mass of 48 kD. Southern filter hybridization
analysis showed that the CALR gene is not highly polymorphic and exists
in single copy in the human genome.
Frank (1994) pointed out that the CALR gene mapped to chromosome 19p
encodes the 48-kD calreticulin, a protein with Ro/SSA properties. Itoh
et al. (1991) showed that the 52-kD and the 60-kD forms of Ro/SSA
ribonucleoproteins are encoded by separate genes mapping to chromosome
11 (TRIM21; 109092) and chromosome 1 (TROVE2; 600063), respectively.
By Northern blot analysis of human tissues, Persson et al. (2002) found
ubiquitous expression of a 1.9-kb CALR transcript.
GENE FUNCTION
Burns et al. (1994) reported that the amino terminus of calreticulin
interacts with the DNA-binding domain of the glucocorticoid receptor and
prevents the receptor from binding to its specific glucocorticoid
response element. Dedhar et al. (1994) showed that calreticulin can
inhibit the binding of androgen receptor to its hormone-responsive DNA
element and can inhibit androgen receptor and retinoic acid receptor
transcriptional activities in vivo, as well as retinoic acid-induced
neuronal differentiation. Thus, calreticulin can act as an important
modulator of the regulation of gene transcription by nuclear hormone
receptors.
Boehm et al. (1994) showed that SLE is associated with increased
autoantibody titers against calreticulin but that calreticulin is not a
Ro/SS-A antigen. Orth et al. (1996) found increased autoantibody titers
against human calreticulin in infants with complete congenital heart
block (234700) of both the IgG and IgM classes.
THBS1 (188060) or a peptide of the 19-amino acid active site in its
heparin-binding domain signals focal adhesion disassembly through
interaction with a cell surface form of CRT. Using bovine aortic
endothelial cells and wildtype and low density lipoprotein
receptor-related protein (LRP, or LRP1; 107770) -/- mouse fibroblasts,
Orr et al. (2003) showed that Lrp interacted with Crt and was required
to mediate focal adhesion disassembly and downstream signaling for
reorganization of focal adhesions. Binding of the LRP ligand RAP
(LRPAP1; 104225) to purified human LRP inhibited interaction between
recombinant human CRT and LRP.
Gardai et al. (2005) stated that calreticulin on the surface of
apoptotic cells serves as a recognition and clearance ligand by
activating the internalization receptor LRP1 (107770) on the responding
phagocyte cell surface. Using mouse and human cells, they found that the
surface expression of calreticulin increased and calreticulin was
redistributed during apoptosis, possibly enhancing stimulation of LRP1
on the phagocyte. In addition, CD47 (601028) on the apoptotic cell
surface was altered and/or lost, which reduced the activation of
SIRP-alpha (PTPNS1; 602461) on the phagocytic cell surface, resulting in
phagocytosis.
In CT26 mouse colon cancer cells, Obeid et al. (2007) demonstrated that
anthracyclins induced immunogenic cell death by way of a rapid,
preapoptotic translocation of calreticulin to the cell surface. Blockade
or knockdown of Calr suppressed phagocytosis of anthracyclin-treated
tumor cells by dendritic cells and abolished their immunogenicity in
mice. Anthracyclin-induced Calr translocation was mimicked by inhibition
of the protein phosphatase-1 (see PPP1CA; 176875)/Gadd34 (PPP1R15A;
611048) complex. Administration of recombinant Calr or inhibitors of
Pp1/Gadd34 restored immunogenicity of cell death elicited by etoposide
and mitomycin C and enhanced their antitumor effects in vivo. Obeid et
al. (2007) concluded that CALR plays a key role in determining
anticancer immune responses.
Using flow cytometric and confocal microscopy analyses, Zeng et al.
(2006) demonstrated that NYESO1 (CTAG1B; 300156) bound to immature
dendritic cells (DCs), macrophages, and monocytes, but not to T cells or
B cells. Immunoprecipitation and tandem mass spectrometric analyses
showed that CALR was the only DC surface-specific protein that
interacted with NYESO1. Anti-CALR inhibited NYESO1 binding on immature
DCs and its cross-presentation to CD8 (see 186910)-positive T cells.
Surface plasmon resonance analysis showed that NYESO1 bound to CALR, but
not to other molecular chaperones. Zeng et al. (2006) proposed that
NYESO1 binding to CALR on macrophages and DCs provides a link between
NYESO1, the innate immune system, possibly the adaptive immune response
against NYESO1.
GENE STRUCTURE
Persson et al. (2002) stated that the CALR gene contains 9 exons and
spans 4.2 kb.
MAPPING
By analysis of somatic cell hybrids, McCauliffe et al. (1990) assigned
the CALR gene to chromosome 19p. There was perfect concordance with LDLR
(606945) but discordance with C3 (120700). Thus, the calreticulin, or
RO, locus may be located in the region of chromosome 19pter-p13.2,
distal to C3 and near LDLR.
Rooke et al. (1997) mapped the mouse Calr gene to chromosome 8.
MOLECULAR GENETICS
- Somatic Mutation in Myeloproliferative Neoplasms
Klampfl et al. (2013) identified calreticulin mutations in 78 of 311
(25%) tumor samples from patients with essential thrombocythemia (see
187950), and in 72 of 203 (35%) tumor samples from patients with primary
myelofibrosis (254450). Mutations in CALR, JAK2 (147796), and MPL
(159530) were mutually exclusive. Among 289 thrombocythemia samples from
a combined cohort of patients with nonmutated JAK2 and MPL, 195 (67%)
had mutated CALR; among 120 primary myelofibrosis samples from the same
cohort, 105 (88%) had mutated CALR. A total of 36 types of insertions or
deletions were identified in exon 9 of CALR, all causing a frameshift to
the same alternative reading frame and generating a novel C-terminal
peptide in the mutant calreticulin. Overexpression of the most frequent
CALR deletion (109091.0001) caused cytokine-independent growth in vitro
owing to the activation of STAT5 (601511). Patients with mutated CALR
had a lower risk of thrombosis and longer overall survival than patients
with mutated JAK2.
Nangalia et al. (2013) identified somatic CALR mutations in 70 to 84% of
samples of myeloproliferative neoplasms with nonmutated JAK2, in 8% of
myelodysplasia samples, in occasional samples of other myeloid cancers,
and in no other hematologic cancers. A total of 148 CALR mutations were
identified with 19 distinct variants. Mutations were located in exon 9
and generated a +1 basepair frameshift, which would result in a mutant
protein with a novel C terminal. Mutant calreticulin was observed in the
endoplasmic reticulum without increased cell surface or Golgi
accumulation. Patients with myeloproliferative neoplasms carrying CALR
mutations presented with higher platelet counts and lower hemoglobin
levels than patients with mutated JAK2. Mutation of CALR was detected in
hematopoietic stem and progenitor cells. Clonal analyses showed CALR
mutations in the earliest phylogenetic node, a finding consistent with
its role as an initiating mutation in some patients.
*FIELD* AV
.0001
MYELOFIBROSIS, SOMATIC
THROMBOCYTHEMIA, SOMATIC, INCLUDED
CALR, 52-BP DEL, EX9
Klampfl et al. (2013) and Nangalia et al. (2013) identified a somatic
52-bp deletion in exon 9 of the CALR gene (1092_1143del) in patients
with myeloproliferative neoplasms, including myelofibrosis (254450) and
essential thrombocythemia (see 187950). CALR mutations and JAK2 and MPL
mutations were mutually exclusive. The 52-bp mutation resulted in
frameshift and premature termination (L367fsTer46). Klampfl et al.
(2013) identified a total of 36 types of somatic insertion or deletion
within exon 9 of CALR, all of which caused a frameshift to the same
alternative reading frame and generated a novel C-terminal peptide in
the mutant calreticulin. Klampfl et al. (2013) identified insertions or
deletions in exon 9 of CALR in 88% of individuals with primary
myelofibrosis with nonmutated JAK2 or MPL. The 52-bp deletion accounted
for 53% of all cases of mutated CALR among several types of
myoproliferative neoplasm. Overexpression of this mutation resulted in
cytokine-independent growth in vitro through the activation of STAT5
(601511). Nangalia et al. (2013) identified 23 patients with
myelofibrosis who carried the L367fsTer46 mutation. Overall, Nangalia et
al. (2013) identified 19 different somatic CALR mutations, all in exon 9
and all of which generated a +1 frameshift resulting in a mutant protein
with a novel C terminal. CALR mutations were present in 18 of 32
patients (56%) with primary myelofibrosis and in 12 of 14 patients (86%)
with progression of essential thrombocythemia to myelofibrosis. Neither
Klampfl et al. (2013) nor Nangalia et al. (2013) detected CALR mutation
in individuals with polycythemia vera.
*FIELD* RF
1. Boehm, J.; Orth, T.; Van Nguyen, P.; Soling, H. D.: Systemic lupus
erythematosus is associated with increased auto-antibody titers against
calreticulin and grp94, but calreticulin is not the Ro/SS-A antigen. Europ.
J. Clin. Invest. 24: 248-257, 1994.
2. Burns, K.; Duggan, B.; Atkinson, E. A.; Famulski, K. S.; Nemer,
M.; Bleackley, R. C.; Michalak, M.: Modulation of gene expression
by calreticulin binding to the glucocorticoid receptor. Nature 367:
476-480, 1994.
3. Dedhar, S.; Rennie, P. S.; Shago, M.; Hagesteijn, C.-Y. L.; Yang,
H.; Filmus, J.; Hawley, R. G.; Bruchovsky, N.; Cheng, H.; Matusik,
R. J.; Giguere, V.: Inhibition of nuclear hormone receptor activity
by calreticulin. Nature 367: 480-483, 1994.
4. Frank, M. B.: Personal Communication. Oklahoma City, Okla.
6/3/1994.
5. Gardai, S. J.; McPhillips, K. A.; Frasch, S. C.; Janssen, W. J.;
Starefeldt, A.; Murphy-Ullrich, J. E.; Bratton, D. L.; Oldenborg,
P.-A.; Michalak, M.; Henson, P. M.: Cell-surface calreticulin initiates
clearance of viable or apoptotic cells through trans-activation of
LRP on the phagocyte. Cell 123: 321-334, 2005.
6. Itoh, K.; Itoh, Y.; Frank, M. B.: Protein heterogeneity in the
human Ro/SSA ribonucleoproteins: the 52- and 60-kD Ro/SSA autoantigens
are encoded by separate genes. J. Clin. Invest. 87: 177-186, 1991.
7. Klampfl, T.; Gisslinger, H.; Harutyunyan, A. S.; Nivarthi, H.;
Rumi, E.; Milosevic, J. D.; Them, N. C. C.; Berg, T.; Gisslinger,
B.; Pietra, D.; Chen, D.; Vladimer, G. I.; and 17 others: Somatic
mutations of calreticulin in myeloproliferative neoplasms. New Eng.
J. Med. 369: 2379-2390, 2013.
8. McCauliffe, D. P.; Lux, F. A.; Lieu, T.-S.; Sanz, I.; Hanke, J.;
Newkirk, M. M.; Bachinski, L. L.; Itoh, Y.; Siciliano, M. J.; Reichlin,
M.; Sontheimer, R. D.; Capra, J. D.: Molecular cloning, expression,
and chromosome 19 localization of a human Ro/SS-A autoantigen. J.
Clin. Invest. 85: 1379-1391, 1990.
9. McCauliffe, D. P.; Zappi, E.; Lieu, T.-S.; Michalak, M.; Sontheimer,
R. D.; Capra, J. D.: A human Ro/SS-A autoantigen is the homologue
of calreticulin and is highly homologous with onchocercal RAL-1 antigen
and an aplysia 'memory molecule.'. J. Clin. Invest. 86: 332-335,
1990.
10. Nangalia, J.; Massie, C. E.; Baxter, E. J.; Nice, F. L.; Gundem,
G.; Wedge, D. C.; Avezov, E.; Li, J.; Kollmann, K.; Kent, D. G.; Aziz,
A.; Godfrey, A. L.; and 40 others: Somatic CALR mutations in myeloproliferative
neoplasms with nonmutated JAK2. New Eng. J. Med. 369: 2391-2405,
2013.
11. Obeid, M.; Tesniere, A.; Ghiringhelli, F.; Fimia, G. M.; Apetoh,
L.; Perfettini, J.-L.; Castedo, M.; Mignot, G.; Panaretakis, T.; Casares,
N.; Metivier, D.; Larochette, N.; van Endert, P.; Ciccosanti, F.;
Piacentini, M.; Zitvogel, L.; Kroemer, G.: Calreticulin exposure
dictates immunogenicity of cancer cell death. Nature Med. 13: 54-61,
2007.
12. Orr, A. W.; Pedraza, C. E.; Pallero, M. A.; Elzie, C. A.; Goicoechea,
S.; Strickland, D. K.; Murphy-Ullrich, J. E.: Low density lipoprotein
receptor-related protein is a calreticulin coreceptor that signals
focal adhesion disassembly. J. Cell Biol. 161: 1179-1189, 2003.
13. Orth, T.; Dorner, T.; Meyer Zum Buschenfelde, K.-H.; Mayet, W.-J.
: Complete congenital heart block is associated with increased autoantibody
titers against calreticulin. Europ. J. Clin. Invest. 26: 205-215,
1996.
14. Persson, S.; Rosenquist, M.; Sommarin, M.: Identification of
a novel calreticulin isoform (Crt2) in human and mouse. Gene 297:
151-158, 2002.
15. Rooke, K.; Briquet-Laugier, V.; Xia, Y.-R.; Lusis, A. J.; Doolittle,
M. H.: Mapping of the gene for calreticulin (Calr) to mouse chromosome
8. Mammalian Genome 8: 870-871, 1997.
16. Zeng, G.; Aldridge, M. E.; Tian, X.; Seiler, D.; Zhang, X.; Jin,
Y.; Rao, J.; Li, W.; Chen, D.; Langford, M. P.; Duggan, C.; Belldegrun,
A. S.; Dubinett, S. M.: Dendritic cell surface calreticulin is a
receptor for NY-ESO-1: direct interactions between tumor-associated
antigen and the innate immune system. J. Immun. 177: 3582-3589,
2006.
*FIELD* CN
Ada Hamosh - updated: 02/07/2014
Patricia A. Hartz - updated: 6/11/2013
Patricia A. Hartz - updated: 8/10/2007
Paul J. Converse - updated: 3/9/2007
Marla J. F. O'Neill - updated: 2/26/2007
Victor A. McKusick - updated: 11/21/1997
*FIELD* CD
Victor A. McKusick: 8/15/1990
*FIELD* ED
alopez: 02/07/2014
mgross: 6/11/2013
wwang: 9/7/2007
wwang: 8/17/2007
terry: 8/10/2007
mgross: 5/21/2007
mgross: 3/14/2007
terry: 3/9/2007
wwang: 2/26/2007
ckniffin: 6/5/2002
terry: 11/26/1997
terry: 11/21/1997
terry: 5/2/1996
mark: 4/27/1996
terry: 4/22/1996
carol: 11/30/1994
jason: 7/28/1994
mimadm: 4/21/1994
pfoster: 3/25/1994
carol: 3/1/1993
carol: 5/22/1992