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
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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)
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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.
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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:
- Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; H2O/D2O (90%/10%); sodium acetate 10 mM; sodium azide 0.05 %)
- Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; D2O 99.9 %; sodium acetate 10 mM; sodium azide 0.05 %)
| References:
- 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:
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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:
- Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; H2O/D2O (90%/10%); sodium acetate 10 mM; sodium azide 0.05 %)
- Nuclear magnetic resonance (NMR) (293 K; pH: 4.5; D2O 99.9 %; sodium acetate 10 mM; sodium azide 0.05 %)
| References:
- 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:
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Comments |
Additional UniGene IDs: Hs.610285, Hs.707152, Hs.714553
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