Protein Information

General Information
MoonProt ID169
First appeared in release1.0
Name(s)Calreticulin CRP55 Calregulin Endoplasmic reticulum resident protein 60 ERp60 HACBP grp60 Gene Name:CALR
UniProt IDP27797 (CALR_HUMAN), Reviewed
GO termsGO:0000122 negative regulation of transcription from RNA polymerase II promoter GO:0002474 antigen processing and presentation of peptide antigen via MHC class I GO:0002479 antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent GO:0002502 peptide antigen assembly with MHC class I protein complex GO:0006355 regulation of transcription, DNA-templated GO:0006457 protein folding GO:0006611 protein export from nucleus GO:0006874 cellular calcium ion homeostasis GO:0006987 activation of signaling protein activity involved in unfolded protein response GO:0007050 cell cycle arrest GO:0007283 spermatogenesis GO:0008284 positive regulation of cell proliferation GO:0010033 response to organic substance GO:0010628 positive regulation of gene expression GO:0017148 negative regulation of translation GO:0018279 protein N-linked glycosylation via asparagine GO:0022417 protein maturation by protein folding GO:0030866 cortical actin cytoskeleton organization GO:0030968 endoplasmic reticulum unfolded protein response GO:0032355 response to estradiol GO:0033144 negative regulation of intracellular steroid hormone receptor signaling pathway GO:0033574 response to testosterone GO:0034504 protein localization to nucleus GO:0040020 regulation of meiosis GO:0042493 response to drug GO:0042590 antigen processing and presentation of exogenous peptide antigen via MHC class I GO:0042921 glucocorticoid receptor signaling pathway GO:0042981 regulation of apoptotic process GO:0043687 post-translational protein modification GO:0044267 cellular protein metabolic process GO:0045665 negative regulation of neuron differentiation GO:0045740 positive regulation of DNA replication GO:0045787 positive regulation of cell cycle GO:0045892 negative regulation of transcription, DNA-templated GO:0048387 negative regulation of retinoic acid receptor signaling pathway GO:0050766 positive regulation of phagocytosis GO:0050821 protein stabilization GO:0051208 sequestering of calcium ion GO:0055007 cardiac muscle cell differentiation GO:0061077 chaperone-mediated protein folding GO:0071285 cellular response to lithium ion GO:0071310 cellular response to organic substance GO:0090398 cellular senescence GO:1900026 positive regulation of substrate adhesion-dependent cell spreading GO:2000510 positive regulation of dendritic cell chemotaxis GO:0001849 complement component C1q binding GO:0001948 glycoprotein binding GO:0003677 DNA binding GO:0003729 mRNA binding GO:0005178 integrin binding GO:0005506 iron ion binding GO:0005509 calcium ion binding GO:0005515 protein binding GO:0008270 zinc ion binding GO:0030246 carbohydrate binding GO:0031625 ubiquitin protein ligase binding GO:0042277 peptide binding GO:0042562 hormone binding GO:0044183 protein binding involved in protein folding GO:0044822 poly(A) RNA binding GO:0046872 metal ion binding GO:0050681 androgen receptor binding GO:0051082 unfolded protein binding GO:0051087 chaperone binding GO:0001669 acrosomal vesicle GO:0005576 extracellular region GO:0005578 proteinaceous extracellular matrix GO:0005615 extracellular space GO:0005622 intracellular GO:0005634 nucleus GO:0005737 cytoplasm GO:0005783 endoplasmic reticulum GO:0005788 endoplasmic reticulum lumen GO:0005794 Golgi apparatus GO:0005829 cytosol GO:0005844 polysome GO:0009897 external side of plasma membrane GO:0009986 cell surface GO:0016529 sarcoplasmic reticulum GO:0031012 extracellular matrix GO:0033018 sarcoplasmic reticulum lumen GO:0042824 MHC class I peptide loading complex GO:0043231 intracellular membrane-bounded organelle GO:0043234 protein complex GO:0048471 perinuclear region of cytoplasm GO:0070062 extracellular vesicular exosome GO:0071556 integral component of lumenal side of endoplasmic reticulum membrane GO:0071682 endocytic vesicle lumen GO:0098631 cell adhesion mediator
Organisms for which functions have been demonstratedHomo sapiens
Sequence length417
FASTA sequence>sp|P27797|CALR_HUMAN Calreticulin OS=Homo sapiens GN=CALR PE=1 SV=1 MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL
Structure Information
PDB ID3POS, 3POW
Quaternary structure
Function 1
Function descriptionchaperone promotes protein folding and assembly of oligomers involved in protein quality control
References for functionBr√ľnagel, Gisela, et al. "Identification of calreticulin as a nuclear matrix protein associated with human colon cancer." Journal of cellular biochemistry 89.2 (2003): 238-243.
E.C. numberN/A
Location of functional site(s)Binding site:128,109,135,317,111 Metal binding site:64,62,328,26
Cellular location of functionendoplasmic reticulum
Comments
Function 2
Function descriptionadhesin
References for functionThrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. Goicoechea S, Orr AW, Pallero MA, Eggleton P, Murphy-Ullrich JE. J Biol Chem. 2000 Nov 17;275(46):36358-68. PMID: 10964924
E.C. numberN/A
Location of functional site(s)
Cellular location of functioncell surface
Comments