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Calreticulin (CRP55) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) (grp60)

 CALR_HUMAN              Reviewed;         417 AA.
P27797; Q6IAT4; Q9UDG2;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
22-NOV-2017, entry version 214.
RecName: Full=Calreticulin;
AltName: Full=CRP55;
AltName: Full=Calregulin;
AltName: Full=Endoplasmic reticulum resident protein 60;
Short=ERp60;
AltName: Full=HACBP;
AltName: Full=grp60;
Flags: Precursor;
Name=CALR; Synonyms=CRTC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2332496; DOI=10.1172/JCI114582;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1919005;
Rokeach L.A., Haselby J.A., Meilof J.F., Smeenk R.J., Unnasch T.R.,
Greene B.M., Hoch S.O.;
"Characterization of the autoantigen calreticulin.";
J. Immunol. 147:3031-3039(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1733953;
McCauliffe D.P., Yang Y.S., Wilson J., Sontheimer R.D., Capra J.D.;
"The 5'-flanking region of the human calreticulin gene shares homology
with the human GRP78, GRP94, and protein disulfide isomerase
promoters.";
J. Biol. Chem. 267:2557-2562(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Liu J., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, Pancreas, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 18-48; 65-92; 96-114; 168-205 AND 257-354.
TISSUE=Placenta;
PubMed=7841019;
Houen G., Koch C.;
"Human placental calreticulin: purification, characterization and
association with other proteins.";
Acta Chem. Scand. 48:905-911(1994).
[12]
PROTEIN SEQUENCE OF 18-41.
PubMed=3260607; DOI=10.1172/JCI113607;
Lieu T.-S., Newkirk M.M., Capra J.D., Sontheimer R.D.;
"Molecular characterization of human Ro/SS-A antigen. Amino terminal
sequence of the protein moiety of human Ro/SS-A antigen and
immunological activity of a corresponding synthetic peptide.";
J. Clin. Invest. 82:96-101(1988).
[13]
PROTEIN SEQUENCE OF 18-36.
PubMed=1911778; DOI=10.1021/bi00105a008;
Rojiani M.V., Finlay B.B., Gray V., Dedhar S.;
"In vitro interaction of a polypeptide homologous to human Ro/SS-A
antigen (calreticulin) with a highly conserved amino acid sequence in
the cytoplasmic domain of integrin alpha subunits.";
Biochemistry 30:9859-9866(1991).
[14]
PROTEIN SEQUENCE OF 18-32.
PubMed=2400400; DOI=10.1042/bj2700545;
Krause K.-H., Simmerman H.K.B., Jones L.R., Campbell K.P.;
"Sequence similarity of calreticulin with a Ca2(+)-binding protein
that co-purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60
cells.";
Biochem. J. 270:545-548(1990).
[15]
PROTEIN SEQUENCE OF 18-28.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[16]
PROTEIN SEQUENCE OF 25-36; 74-111 AND 208-222, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[17]
PROTEIN SEQUENCE OF 25-34; 56-62; 208-221 AND 273-278.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[18]
PROTEIN SEQUENCE OF 18-27, AND SUBCELLULAR LOCATION.
PubMed=8418194; DOI=10.1084/jem.177.1.1;
Dupuis M., Schaerer E., Krause K.-H., Tschopp J.;
"The calcium-binding protein calreticulin is a major constituent of
lytic granules in cytolytic T lymphocytes.";
J. Exp. Med. 177:1-7(1993).
[19]
PROTEIN SEQUENCE OF 18-26.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[20]
FUNCTION.
PubMed=7876246; DOI=10.1074/jbc.270.9.4741;
Nauseef W.M., McCormick S.J., Clark R.A.;
"Calreticulin functions as a molecular chaperone in the biosynthesis
of myeloperoxidase.";
J. Biol. Chem. 270:4741-4747(1995).
[21]
INTERACTION WITH TRIM21.
PubMed=8666824;
Cheng S.T., Nguyen T.Q., Yang Y.S., Capra J.D., Sontheimer R.D.;
"Calreticulin binds hYRNA and the 52-kDa polypeptide component of the
Ro/SS-A ribonucleoprotein autoantigen.";
J. Immunol. 156:4484-4491(1996).
[22]
SUBCELLULAR LOCATION.
PubMed=10358038; DOI=10.1074/jbc.274.24.16917;
Arosa F.A., de Jesus O., Porto G., Carmo A.M., de Sousa M.;
"Calreticulin is expressed on the cell surface of activated human
peripheral blood T lymphocytes in association with major
histocompatibility complex class I molecules.";
J. Biol. Chem. 274:16917-16922(1999).
[23]
FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION, AND MASS
SPECTROMETRY.
PubMed=11149926; DOI=10.1083/jcb.152.1.127;
Holaska J.M., Black B.E., Love D.C., Hanover J.A., Leszyk J.,
Paschal B.M.;
"Calreticulin is a receptor for nuclear export.";
J. Cell Biol. 152:127-140(2001).
[24]
PARTIAL PROTEIN SEQUENCE, DISULFIDE BOND, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Placenta;
PubMed=11322874; DOI=10.1046/j.1432-1327.2001.02138.x;
Hoejrup P., Roepstorff P., Houen G.;
"Human placental calreticulin characterization of domain structure and
post-translational modifications.";
Eur. J. Biochem. 268:2558-2565(2001).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
INTERACTION WITH PPIB.
PubMed=20801878; DOI=10.1074/jbc.M110.160101;
Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A.,
Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.;
"Structural basis of cyclophilin B binding by the
calnexin/calreticulin P-domain.";
J. Biol. Chem. 285:35551-35557(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[30]
INTERACTION WITH PDIA5.
PubMed=23614004; DOI=10.1371/journal.pone.0062021;
Vinaik R., Kozlov G., Gehring K.;
"Structure of the non-catalytic domain of the protein disulfide
isomerase-related protein (PDIR) reveals function in protein
binding.";
PLoS ONE 8:E62021-E62021(2013).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-17, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[33]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 195-205 IN COMPLEX WITH
GABARAP, AND INTERACTION WITH GABARAP.
PubMed=19154346; DOI=10.1111/j.1742-4658.2008.06857.x;
Thielmann Y., Weiergraber O.H., Mohrluder J., Willbold D.;
"Structural framework of the GABARAP-calreticulin interface
-- implications for substrate binding to endoplasmic reticulum
chaperones.";
FEBS J. 276:1140-1152(2009).
[34]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-368 IN COMPLEX WITH
CALCIUM IONS, AND DISULFIDE BOND.
PubMed=21423620; DOI=10.1371/journal.pone.0017886;
Chouquet A., Paidassi H., Ling W.L., Frachet P., Houen G.,
Arlaud G.J., Gaboriaud C.;
"X-ray structure of the human calreticulin globular domain reveals a
peptide-binding area and suggests a multi-molecular mechanism.";
PLoS ONE 6:E17886-E17886(2011).
-!- FUNCTION: Calcium-binding chaperone that promotes folding,
oligomeric assembly and quality control in the endoplasmic
reticulum (ER) via the calreticulin/calnexin cycle. This lectin
interacts transiently with almost all of the monoglucosylated
glycoproteins that are synthesized in the ER. Interacts with the
DNA-binding domain of NR3C1 and mediates its nuclear export.
Involved in maternal gene expression regulation. May participate
in oocyte maturation via the regulation of calcium homeostasis (By
similarity). {ECO:0000250, ECO:0000269|PubMed:11149926,
ECO:0000269|PubMed:7876246}.
-!- SUBUNIT: Monomer. Component of an EIF2 complex at least composed
of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
Interacts with PDIA3/ERp57 and SPACA9 (By similarity). Interacts
with TRIM21 (PubMed:8666824). Interacts with NR3C1
(PubMed:11149926). Interacts with PPIB (PubMed:20801878).
Interacts (via P-domain) with PDIA5 (PubMed:23614004). Interacts
with GABARAP (PubMed:19154346). {ECO:0000250|UniProtKB:P14211,
ECO:0000250|UniProtKB:P18418, ECO:0000269|PubMed:11149926,
ECO:0000269|PubMed:19154346, ECO:0000269|PubMed:20801878,
ECO:0000269|PubMed:23614004, ECO:0000269|PubMed:8666824}.
-!- INTERACTION:
P05067:APP; NbExp=2; IntAct=EBI-1049597, EBI-77613;
O95166:GABARAP; NbExp=4; IntAct=EBI-1049597, EBI-712001;
P04792:HSPB1; NbExp=2; IntAct=EBI-1049597, EBI-352682;
Q53T94:TAF1B; NbExp=4; IntAct=EBI-1049597, EBI-1560239;
Q03518:TAP1; NbExp=2; IntAct=EBI-1049597, EBI-747259;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:10358038, ECO:0000269|PubMed:11149926}.
Cytoplasm, cytosol {ECO:0000269|PubMed:11149926}. Secreted,
extracellular space, extracellular matrix {ECO:0000305}. Cell
surface {ECO:0000269|PubMed:10358038}. Sarcoplasmic reticulum
lumen {ECO:0000250|UniProtKB:P28491}. Note=Also found in cell
surface (T cells), cytosol and extracellular matrix
(PubMed:10358038). Associated with the lytic granules in the
cytolytic T-lymphocytes. {ECO:0000269|PubMed:10358038,
ECO:0000269|PubMed:8418194}.
-!- DOMAIN: Can be divided into a N-terminal globular domain, a
proline-rich P-domain forming an elongated arm-like structure and
a C-terminal acidic domain. The P-domain binds one molecule of
calcium with high affinity, whereas the acidic C-domain binds
multiple calcium ions with low affinity.
-!- DOMAIN: The interaction with glycans occurs through a binding site
in the globular lectin domain.
-!- DOMAIN: The zinc binding sites are localized to the N-domain.
-!- DOMAIN: Associates with PDIA3 through the tip of the extended arm
formed by the P-domain.
-!- MASS SPECTROMETRY: Mass=46879; Method=MALDI; Range=18-417;
Evidence={ECO:0000269|PubMed:11149926};
-!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be the 52 kDa Ro autoantigen.
{ECO:0000305|PubMed:2332496}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Calreticulin entry;
URL="https://en.wikipedia.org/wiki/Calreticulin";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Calreticulin;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_405";
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EMBL; M32294; AAA36582.1; -; mRNA.
EMBL; M84739; AAA51916.1; -; mRNA.
EMBL; AY047586; AAL13126.1; -; mRNA.
EMBL; AB451408; BAG70222.1; -; mRNA.
EMBL; BT007448; AAP36116.1; -; mRNA.
EMBL; CR457070; CAG33351.1; -; mRNA.
EMBL; AD000092; AAB51176.1; -; Genomic_DNA.
EMBL; CH471106; EAW84331.1; -; Genomic_DNA.
EMBL; BC002500; AAH02500.1; -; mRNA.
EMBL; BC007911; AAH07911.1; -; mRNA.
EMBL; BC020493; AAH20493.1; -; mRNA.
CCDS; CCDS12288.1; -.
PIR; A42330; A37047.
RefSeq; NP_004334.1; NM_004343.3.
UniGene; Hs.515162; -.
PDB; 2CLR; X-ray; 2.00 A; C/F=1-10.
PDB; 3DOW; X-ray; 2.30 A; B=195-205.
PDB; 3POS; X-ray; 1.65 A; A/B/C=18-204, A/B/C=302-368.
PDB; 3POW; X-ray; 1.55 A; A=18-204, A=302-368.
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.
PDB; 5V90; X-ray; 3.25 A; B/D=238-273.
PDBsum; 2CLR; -.
PDBsum; 3DOW; -.
PDBsum; 3POS; -.
PDBsum; 3POW; -.
PDBsum; 5LK5; -.
PDBsum; 5V90; -.
DisProt; DP00333; -.
ProteinModelPortal; P27797; -.
SMR; P27797; -.
BioGrid; 107262; 140.
CORUM; P27797; -.
DIP; DIP-104N; -.
IntAct; P27797; 49.
MINT; MINT-101756; -.
STRING; 9606.ENSP00000320866; -.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
DrugBank; DB01065; Melatonin.
DrugBank; DB00031; Tenecteplase.
iPTMnet; P27797; -.
PhosphoSitePlus; P27797; -.
SwissPalm; P27797; -.
BioMuta; CALR; -.
DMDM; 117501; -.
DOSAC-COBS-2DPAGE; P27797; -.
OGP; P27797; -.
REPRODUCTION-2DPAGE; IPI00020599; -.
SWISS-2DPAGE; P27797; -.
UCD-2DPAGE; P27797; -.
EPD; P27797; -.
PaxDb; P27797; -.
PeptideAtlas; P27797; -.
PRIDE; P27797; -.
TopDownProteomics; P27797; -.
DNASU; 811; -.
Ensembl; ENST00000316448; ENSP00000320866; ENSG00000179218.
GeneID; 811; -.
KEGG; hsa:811; -.
CTD; 811; -.
DisGeNET; 811; -.
EuPathDB; HostDB:ENSG00000179218.13; -.
GeneCards; CALR; -.
HGNC; HGNC:1455; CALR.
HPA; CAB001513; -.
HPA; CAB019952; -.
HPA; HPA002242; -.
MalaCards; CALR; -.
MIM; 109091; gene.
neXtProt; NX_P27797; -.
OpenTargets; ENSG00000179218; -.
Orphanet; 3318; Essential thrombocythemia.
Orphanet; 824; Myelofibrosis with myeloid metaplasia.
PharmGKB; PA26046; -.
eggNOG; KOG0674; Eukaryota.
eggNOG; ENOG410XRR7; LUCA.
GeneTree; ENSGT00430000030841; -.
HOGENOM; HOG000192435; -.
HOVERGEN; HBG005407; -.
InParanoid; P27797; -.
KO; K08057; -.
OMA; DTWIYSK; -.
OrthoDB; EOG091G0AP1; -.
PhylomeDB; P27797; -.
TreeFam; TF338438; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
Reactome; R-HSA-901042; Calnexin/calreticulin cycle.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
ChiTaRS; CALR; human.
EvolutionaryTrace; P27797; -.
GeneWiki; Calreticulin; -.
GenomeRNAi; 811; -.
PRO; PR:P27797; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000179218; -.
CleanEx; HS_CALR; -.
ExpressionAtlas; P27797; baseline and differential.
Genevisible; P27797; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0009986; C:cell surface; TAS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005622; C:intracellular; TAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0042824; C:MHC class I peptide loading complex; ISS:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005844; C:polysome; IDA:BHF-UCL.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0050681; F:androgen receptor binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; TAS:BHF-UCL.
GO; GO:0051087; F:chaperone binding; TAS:BHF-UCL.
GO; GO:0001849; F:complement component C1q binding; TAS:BHF-UCL.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0042562; F:hormone binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0044183; F:protein binding involved in protein folding; TAS:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; TAS:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; TAS:BHF-UCL.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0036500; P:ATF6-mediated unfolded protein response; TAS:Reactome.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:UniProtKB.
GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; IGI:BHF-UCL.
GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; TAS:BHF-UCL.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IGI:BHF-UCL.
GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:BHF-UCL.
GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0017148; P:negative regulation of translation; IDA:BHF-UCL.
GO; GO:1901164; P:negative regulation of trophoblast cell migration; IMP:CAFA.
GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISS:BHF-UCL.
GO; GO:0045787; P:positive regulation of cell cycle; IGI:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:BHF-UCL.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IGI:BHF-UCL.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:CAFA.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; ISS:BHF-UCL.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:BHF-UCL.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0051208; P:sequestering of calcium ion; TAS:BHF-UCL.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:1990668; P:vesicle fusion with endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane; TAS:Reactome.
InterPro; IPR001580; Calret/calnex.
InterPro; IPR018124; Calret/calnex_CS.
InterPro; IPR009169; Calreticulin.
InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
InterPro; IPR013320; ConA-like_dom_sf.
PANTHER; PTHR11073; PTHR11073; 1.
Pfam; PF00262; Calreticulin; 2.
PIRSF; PIRSF002356; Calreticulin; 1.
PRINTS; PR00626; CALRETICULIN.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF63887; SSF63887; 1.
PROSITE; PS00803; CALRETICULIN_1; 1.
PROSITE; PS00804; CALRETICULIN_2; 1.
PROSITE; PS00805; CALRETICULIN_REPEAT; 3.
PROSITE; PS00014; ER_TARGET; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Chaperone; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Lectin;
Metal-binding; Reference proteome; Repeat; Sarcoplasmic reticulum;
Secreted; Signal; Zinc.
SIGNAL 1 17 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:1911778,
ECO:0000269|PubMed:2400400,
ECO:0000269|PubMed:3260607,
ECO:0000269|PubMed:7841019,
ECO:0000269|PubMed:8418194,
ECO:0000269|PubMed:9150948}.
CHAIN 18 417 Calreticulin.
/FTId=PRO_0000004173.
REPEAT 191 202 1-1.
REPEAT 210 221 1-2.
REPEAT 227 238 1-3.
REPEAT 244 255 1-4.
REPEAT 259 269 2-1.
REPEAT 273 283 2-2.
REPEAT 287 297 2-3.
REGION 18 197 N-domain.
REGION 191 255 4 X approximate repeats.
REGION 198 308 P-domain.
REGION 237 270 Interaction with PPIB. {ECO:0000250}.
REGION 259 297 3 X approximate repeats.
REGION 309 417 C-domain.
MOTIF 414 417 Prevents secretion from ER.
COMPBIAS 351 408 Asp/Glu/Lys-rich.
METAL 26 26 Calcium; via carbonyl oxygen.
METAL 62 62 Calcium; via carbonyl oxygen.
METAL 64 64 Calcium; via carbonyl oxygen.
METAL 328 328 Calcium.
BINDING 109 109 Carbohydrate. {ECO:0000250}.
BINDING 111 111 Carbohydrate. {ECO:0000250}.
BINDING 128 128 Carbohydrate. {ECO:0000250}.
BINDING 135 135 Carbohydrate. {ECO:0000250}.
BINDING 317 317 Carbohydrate. {ECO:0000250}.
MOD_RES 48 48 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 159 159 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 209 209 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 105 137 {ECO:0000269|PubMed:11322874,
ECO:0000269|PubMed:21423620}.
STRAND 20 25 {ECO:0000244|PDB:3POW}.
HELIX 30 35 {ECO:0000244|PDB:3POW}.
STRAND 37 39 {ECO:0000244|PDB:3POW}.
STRAND 42 44 {ECO:0000244|PDB:3POW}.
STRAND 49 52 {ECO:0000244|PDB:3POW}.
TURN 60 63 {ECO:0000244|PDB:3POW}.
STRAND 65 68 {ECO:0000244|PDB:3POW}.
STRAND 70 84 {ECO:0000244|PDB:3POW}.
STRAND 91 98 {ECO:0000244|PDB:3POW}.
STRAND 104 107 {ECO:0000244|PDB:3POW}.
STRAND 110 113 {ECO:0000244|PDB:3POW}.
HELIX 119 121 {ECO:0000244|PDB:3POW}.
STRAND 129 138 {ECO:0000244|PDB:3POW}.
STRAND 142 150 {ECO:0000244|PDB:3POW}.
STRAND 153 156 {ECO:0000244|PDB:3POW}.
STRAND 166 176 {ECO:0000244|PDB:3POW}.
STRAND 180 186 {ECO:0000244|PDB:3POW}.
STRAND 189 195 {ECO:0000244|PDB:3POW}.
HELIX 196 199 {ECO:0000244|PDB:3POW}.
STRAND 201 203 {ECO:0000244|PDB:3DOW}.
TURN 303 306 {ECO:0000244|PDB:5LK5}.
STRAND 311 322 {ECO:0000244|PDB:3POW}.
STRAND 326 334 {ECO:0000244|PDB:3POW}.
HELIX 336 345 {ECO:0000244|PDB:3POW}.
HELIX 347 366 {ECO:0000244|PDB:3POW}.
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


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