General Information |
MoonProt ID | 169 |
First appeared in release | 1.0 |
Name(s) | Calreticulin
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
ERp60
HACBP
grp60
Gene Name:CALR |
UniProt ID | P27797 (CALR_HUMAN), Reviewed |
GO terms | GO: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 |
Organisms for which functions have been demonstrated | Homo sapiens (human, a mammal) |
Sequence length | 417 |
FASTA sequence | >sp|P27797|CALR_HUMAN Calreticulin OS=Homo sapiens GN=CALR PE=1 SV=1
MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL
|
Structure Information |
PDB ID | 3POS, 3POW |
Quaternary structure | |
SCOP | NA |
CATH | 2.60.120.200 |
TM Helix Prediction | no TM helices |
DisProt Annotation | 100% |
Predicted Disorder Regions | 1 to 4, 153-154, 213-219, 226-237, 357-417 |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | chaperone
promotes protein folding and assembly of oligomers
involved in protein quality control
|
References for function | |
E.C. number | N/A |
Location of functional site(s) | |
Cellular location of function | endoplasmic reticulum |
Comments | |
Function 2 |
Function description | adhesin
|
References for function | Thrombospondin 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. number | N/A |
Location of functional site(s) | |
Cellular location of function | cell surface |
Comments | |