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DP00466: Major prion proteinFASTA viewXML view

General information
DisProt:DP00466
Name:Major prion protein
Synonym(s):PRIO_HUMAN
PrP
PrP27-30
PrP33-35C
ASCR
Antigen CD230
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P04156
UniGene:Hs.472010
SwissProt: PRIO_HUMAN
TrEMBL:  
NCBI (GI): 130912
Source organism:Homo sapiens (Human)
Sequence length:253
Percent disordered:41%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MANLGCWMLV LFVATWSDLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGGWGQP - 60
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN KPSKPKTNMK HMAGAAAAGA - 120
VVGGLGGYML GSAMSRPIIH FGSDYEDRYY RENMHRYPNQ VYYRPMDEYS NQNNFVHDCV - 180
NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCITQYER ESQAYYQRGS SMVLFSSPPV - 240
ILLISFLIFL IVG



Functional narrative    

The physiological function of PrP is not known.

The function of PrP is still under debate. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis By similarity. Isoform 2 may act as a growth suppressor by arresting the cell cycle at the G0/G1 phase. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). (UniProt)

Region 1: 23-121 Region 2: 167-171

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
Name: 
Location:23 - 121
Length:99
Region sequence:

KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWG
QPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAV

Modification type: Fragment
Monomeric
Native
PDB: 1QLX:A, 1QLZ:A, 1QM0:A, 1QM1:A, 1QM2:A, 1QM3:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; H2O/D2O (90%/10%); sodium acetate 10 mM; sodium azide 0.05 %)

  2. Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; D2O 99.9 %; sodium acetate 10 mM; sodium azide 0.05 %)

References:
  1. Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K. "NMR solution structure of the human prion protein." Proc Natl Acad Sci U S A. 2000; 97(1): 145-50. PubMed: 10618385

Comments:
 



Region 2
Type:Disordered
Name:disordered loop
Location:167 - 171
Length:5
Region sequence:

DEYSN

Modification type: Fragment
Monomeric
Native
PDB: 1QLX:A, 1QLZ:A, 1QM0:A, 1QM1:A, 1QM2:A, 1QM3:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; H2O/D2O (90%/10%); sodium acetate 10 mM; sodium azide 0.05 %)

  2. Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; D2O 99.9 %; sodium acetate 10 mM; sodium azide 0.05 %)

References:
  1. Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K. "NMR solution structure of the human prion protein." Proc Natl Acad Sci U S A. 2000; 97(1): 145-50. PubMed: 10618385

Comments:
 



Comments


Additional UniGene IDs: Hs.610285, Hs.707152, Hs.714553


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