Annotation for this protein is in progress - please check future releases for more complete information


DP00333: CalreticulinFASTA viewXML view

General information
DisProt:DP00333
Name:Calreticulin
Synonym(s):CALR_HUMAN
CRP55
Calregulin
HACBP
Endoplasmic reticulum resident protein 60
ERp60
grp60
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P27797
UniGene:Hs.515162
SwissProt: CALR_HUMAN
TrEMBL:  
NCBI (GI): 117501
Source organism:Homo sapiens (Human)
Sequence length:417
Percent disordered:96%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MLLSVPLLLG LLGLAVAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV LSSGKFYGDE - 60
EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPNSLDQT - 120
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN - 180
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE - 240
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS - 300
PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK - 360
QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED KEEDEEEDVP GQAKDEL



Functional narrative    

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.

Region 2: 18-307 Region 1: 308-417

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered - Extended
Name: 
Location:308 - 417
Length:110
Region sequence:

YDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRL
KEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL

Modification type:  
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Size exclusion/gel filtration chromatography (298 K; Hepes (pH 7.5) 20 mM; NaCl 150 mM)

  2. Size exclusion/gel filtration chromatography (298 K; EGTA 2 mM; Hepes (pH 7.5) 20 mM; NaCl 150 mM)

  3. Size exclusion/gel filtration chromatography (298 K; CaCl2 (20-1000 uM); Hepes (pH 7.5) 20 mM; NaCl 150 mM)

  4. Size exclusion/gel filtration chromatography (298 K; Hepes (pH 7.5) 20 mM; NaCl 150 mM; ZnCl2 (20-400 uM))

  5. Circular dichroism (CD) spectroscopy, far-UV (Hepes (pH 7.5) 2 mM; NaCl 50 mM)

  6. Circular dichroism (CD) spectroscopy, near-UV (Hepes (pH 7.5) 2 mM; NaCl 50 mM)

  7. Sensitivity to proteolysis (298 K; Hepes (pH 7.5) 20 mM; NaCl 150 mM; Thermolysin (7-300 ug/ml))

  8. Analytical ultracentrifugation (293 K; Hepes (pH 7.5) 20 mM; NaCl 500 mM)
References:
  1. Bouvier M, Stafford WF. "Probing the three-dimensional structure of human calreticulin." Biochemistry. 2000; 39(48): 14950-9. PubMed: 11101311
Comments:
 



Region 2
Type:Disordered
Name: 
Location:18 - 307
Length:290
Region sequence:

EPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYAL
SASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDIC
GPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLE
DDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEM
DGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYA

Modification type:  
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Size exclusion/gel filtration chromatography (298 K; Hepes (pH 7.5) 20 mM; NaCl 150 mM)

  2. Size exclusion/gel filtration chromatography (298 K; EGTA 2 mM; Hepes (pH 7.5) 20 mM; NaCl 150 mM)

  3. Size exclusion/gel filtration chromatography (298 K; CaCl2 (20-1000 uM); Hepes (pH 7.5) 20 mM; NaCl 150 mM)

  4. Size exclusion/gel filtration chromatography (298 K; Hepes (pH 7.5) 20 mM; NaCl 150 mM; ZnCl2 (20-400 uM))

  5. Circular dichroism (CD) spectroscopy, far-UV (Hepes (pH 7.5) 2 mM; NaCl 50 mM)

  6. Circular dichroism (CD) spectroscopy, near-UV (Hepes (pH 7.5) 2 mM; NaCl 50 mM)

  7. Sensitivity to proteolysis (298 K; Hepes (pH 7.5) 20 mM; NaCl 150 mM; Thermolysin (7-300 ug/ml))

  8. Analytical ultracentrifugation (293 K; Hepes (pH 7.5) 20 mM; NaCl 500 mM)
References:
  1. Bouvier M, Stafford WF. "Probing the three-dimensional structure of human calreticulin." Biochemistry. 2000; 39(48): 14950-9. PubMed: 11101311
Comments:
 



References

  1. 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; 85(5): 1379-91. PubMed: 2332496



Comments


The sequence given includes 17 residues at the beginning of the protein that were not included in the Bouvier and Stafford paper. This was a 17-residue signal peptide.


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