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


DP00187: Major prion proteinFASTA viewXML view

General information
DisProt:DP00187
Name:Major prion protein
Synonym(s):PRIO_MESAU
PrP
PrP27-30
PrP33-35C
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P04273
UniGene: 
SwissProt: PRIO_MESAU
TrEMBL:  
NCBI (GI): 130913
Source organism:Mesocricetus auratus (Golden hamster)
Sequence length:254
Percent disordered:38%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MANLSYWLLA LFVAMWTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGTWGQP - 60
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHNQWN KPSKPKTNMK HMAGAAAAGA - 120
VVGGLGGYML GSAMSRPMMH FGNDWEDRYY RENMNRYPNQ VYYRPVDQYN NQNNFVHDCV - 180
NITIKQHTVT TTTKGENFTE TDIKIMERVV EQMCTTQYQK ESQAYYDGRR SSAVLFSSPP - 240
VILLISFLIF LMVG

Region 2: 29-124 Region 1: 90-124

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:90 - 124
Length:35
Region sequence:

GQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGG

Modification type: Fragment
Native
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2p 90%; 2H2O 10%; sodium acetate-d5 (buffer) 20 mM; sodium azide 0.005 %)
References:
  1. Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ. "Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible." Proc Natl Acad Sci U S A. 1997; 94(25): 13452-7. PubMed: 9391046
Comments:
 



Region 2
Type:Disordered
Name:PrP(29-231)
Location:29 - 124
Length:96
Region sequence:

GGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGG
WGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGG

Modification type: Fragment
Native
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Nuclear magnetic resonance (NMR)
References:
  1. Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ. "Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible." Proc Natl Acad Sci U S A. 1997; 94(25): 13452-7. PubMed: 9391046
Comments:
 



References

  1. Taubner LM, Bienkiewicz EA, Copie V, Caughey B. "Structure of the Flexible Amino-Terminal Domain of Prion Protein Bound to a Sulfated Glycan." J Mol Biol. 2009. PubMed: 19913031


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