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Identification
HMDB Protein ID HMDBP07533
Secondary Accession Numbers
  • 13241
Name Calreticulin
Synonyms
  1. CRP55
  2. Calregulin
  3. ERp60
  4. Endoplasmic reticulum resident protein 60
  5. HACBP
  6. grp60
Gene Name CALR
Protein Type Unknown
Biological Properties
General Function Involved in calcium ion binding
Specific Function Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
endoplasmic reticulum
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
Function
ion binding
cation binding
metal ion binding
binding
unfolded protein binding
protein binding
calcium ion binding
Process
metabolic process
macromolecule metabolic process
cellular protein metabolic process
protein folding
protein metabolic process
Cellular Location
  1. Cytoplasm
  2. Secreted
  3. extracellular space
  4. cytosol
  5. Endoplasmic reticulum lumen
  6. extracellular matrix
  7. Cell surface
Gene Properties
Chromosome Location Chromosome:1
Locus 19p13.3-p13.2
SNPs CALR
Gene Sequence
>1254 bp
ATGCTGCTATCCGTGCCGCTGCTGCTCGGCCTCCTCGGCCTGGCCGTCGCCGAGCCCGCC
GTCTACTTCAAGGAGCAGTTTCTGGACGGAGACGGGTGGACTTCCCGCTGGATCGAATCC
AAACACAAGTCAGATTTTGGCAAATTCGTTCTCAGTTCCGGCAAGTTCTACGGTGACGAG
GAGAAAGATAAAGGTTTGCAGACAAGCCAGGATGCACGCTTTTATGCTCTGTCGGCCAGT
TTCGAGCCTTTCAGCAACAAAGGCCAGACGCTGGTGGTGCAGTTCACGGTGAAACATGAG
CAGAACATCGACTGTGGGGGCGGCTATGTGAAGCTGTTTCCTAATAGTTTGGACCAGACA
GACATGCACGGAGACTCAGAATACAACATCATGTTTGGTCCCGACATCTGTGGCCCTGGC
ACCAAGAAGGTTCATGTCATCTTCAACTACAAGGGCAAGAACGTGCTGATCAACAAGGAC
ATCCGTTGCAAGGATGATGAGTTTACACACCTGTACACACTGATTGTGCGGCCAGACAAC
ACCTATGAGGTGAAGATTGACAACAGCCAGGTGGAGTCCGGCTCCTTGGAAGACGATTGG
GACTTCCTGCCACCCAAGAAGATAAAGGATCCTGATGCTTCAAAACCGGAAGACTGGGAT
GAGCGGGCCAAGATCGATGATCCCACAGACTCCAAGCCTGAGGACTGGGACAAGCCCGAG
CATATCCCTGACCCTGATGCTAAGAAGCCCGAGGACTGGGATGAAGAGATGGACGGAGAG
TGGGAACCCCCAGTGATTCAGAACCCTGAGTACAAGGGTGAGTGGAAGCCCCGGCAGATC
GACAACCCAGATTACAAGGGCACTTGGATCCACCCAGAAATTGACAACCCCGAGTATTCT
CCCGATCCCAGTATCTATGCCTATGATAACTTTGGCGTGCTGGGCCTGGACCTCTGGCAG
GTCAAGTCTGGCACCATCTTTGACAACTTCCTCATCACCAACGATGAGGCATACGCTGAG
GAGTTTGGCAACGAGACGTGGGGCGTAACAAAGGCAGCAGAGAAACAAATGAAGGACAAA
CAGGACGAGGAGCAGAGGCTTAAGGAGGAGGAAGAAGACAAGAAACGCAAAGAGGAGGAG
GAGGCAGAGGACAAGGAGGATGATGAGGACAAAGATGAGGATGAGGAGGATGAGGAGGAC
AAGGAGGAAGATGAGGAGGAAGATGTCCCCGGCCAGGCCAAGGACGAGCTGTAG
Protein Properties
Number of Residues 417
Molecular Weight 48141.2
Theoretical pI 4.04
Pfam Domain Function
Signals
  • 1-17
Transmembrane Regions
  • None
Protein Sequence
>Calreticulin
MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDE
EKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQT
DMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDN
TYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPE
HIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYS
PDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDK
QDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P27797
UniProtKB/Swiss-Prot Entry Name CALR_HUMAN
PDB IDs Not Available
GenBank Gene ID M32294
GeneCard ID CALR
GenAtlas ID CALR
HGNC ID HGNC:1455
References
General References
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  3. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed:1286669 ]
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  6. 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. 2008 Dec;5(12):1011-7. [PubMed:19054851 ]
  7. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed:1286667 ]
  8. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed:9150948 ]
  9. McCauliffe DP, Lux FA, Lieu TS, Sanz I, Hanke J, Newkirk MM, Bachinski LL, Itoh Y, Siciliano MJ, Reichlin M, et al.: Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen. J Clin Invest. 1990 May;85(5):1379-91. [PubMed:2332496 ]
  10. Rokeach LA, Haselby JA, Meilof JF, Smeenk RJ, Unnasch TR, Greene BM, Hoch SO: Characterization of the autoantigen calreticulin. J Immunol. 1991 Nov 1;147(9):3031-9. [PubMed:1919005 ]
  11. McCauliffe DP, Yang YS, Wilson J, Sontheimer RD, Capra JD: The 5'-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters. J Biol Chem. 1992 Feb 5;267(4):2557-62. [PubMed:1733953 ]
  12. Houen G, Koch C: Human placental calreticulin: purification, characterization and association with other proteins. Acta Chem Scand. 1994 Nov;48(11):905-11. [PubMed:7841019 ]
  13. Lieu TS, Newkirk MM, Capra JD, Sontheimer RD: 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. 1988 Jul;82(1):96-101. [PubMed:3260607 ]
  14. Rojiani MV, Finlay BB, 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. 1991 Oct 15;30(41):9859-66. [PubMed:1911778 ]
  15. Krause KH, Simmerman HK, Jones LR, Campbell KP: 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. 1990 Sep 1;270(2):545-8. [PubMed:2400400 ]
  16. Dupuis M, Schaerer E, Krause KH, Tschopp J: The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes. J Exp Med. 1993 Jan 1;177(1):1-7. [PubMed:8418194 ]
  17. Nauseef WM, McCormick SJ, Clark RA: Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem. 1995 Mar 3;270(9):4741-7. [PubMed:7876246 ]
  18. Cheng ST, Nguyen TQ, Yang YS, Capra JD, Sontheimer RD: Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen. J Immunol. 1996 Jun 1;156(11):4484-91. [PubMed:8666824 ]
  19. Arosa FA, de Jesus O, Porto G, Carmo AM, 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. 1999 Jun 11;274(24):16917-22. [PubMed:10358038 ]
  20. Holaska JM, Black BE, Love DC, Hanover JA, Leszyk J, Paschal BM: Calreticulin Is a receptor for nuclear export. J Cell Biol. 2001 Jan 8;152(1):127-40. [PubMed:11149926 ]
  21. Hojrup P, Roepstorff P, Houen G: Human placental calreticulin characterization of domain structure and post-translational modifications. Eur J Biochem. 2001 May;268(9):2558-65. [PubMed:11322874 ]