| General information | | DisProt: | DP00353 | | Name: | Protein URE2 | | Synonym(s): | URE2_YEAST
Ure2p
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P23202 | | UniGene: | | | SwissProt: | URE2_YEAST | | TrEMBL: | | | NCBI (GI): | 137083 | | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | | Sequence length: | 354 | | Percent disordered: | 25% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MMNNNGNQVS NLSNALRQVN IGSRNSNTTT DQSNINFEFS TGVNNNNNNN SSSNNNNVQN - 60
NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS RITKFFQEQP LEGYTLFSHR - 120
SAPNGFKVAI VLSELGFHYN TIFLDFNLGE HRAPEFVSVN PNARVPALID HGMDNLSIWE - 180
SGAILLHLVN KYYKETGNPL LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK - 240
IASAVERYTD EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW - 300
LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA LRGE
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| Functional narrative |
Regulator of nitrogen catabolism in Saccharomyces cerevisiae.Ure2p is a cytoplasmic homodimeric protein, whose C-terminal domain (91-354, globular protein with a GST-like fold) interacts with the GATA transcription factor Gln3p, preventing its entry into the nucleus. The prion domain (1-90) is responsible for filament formation. In the prion state, Ure2p aggregates into filaments, and its effect on Gln3p is suppressed. Plays an important role in the cellular response to the nitrogen source. URE2 gene plays a major part in the repression of GLN1 and GDH2 genes by glutamine, and is required for the inactivation of glutamine synthetase. URE2 gene product may catalytically inactivate GLN3 in response to an increase in the intracellular concentration of glutamine.
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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: | prion domain | | Location: | 1 - 90 | | Length: | 90 | | Region sequence: |
MMNNNGNQVSNLSNALRQVNIGSRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQN
NNSGRNGSQNNDNENNIKNTLEQHRQQQQA | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Polymerization
Protein-protein binding
| Detection methods:
- Sensitivity to proteolysis (310 K; pH: 7.5; Proteinase K (protease) 2.4 microg/ml; Trypsin (protease) 1.5 microg/ml)
- Fluorescence, intrinsic (293 K; )
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.5; )
- Nuclear magnetic resonance (NMR)
| References:
- Pierce MM, Baxa U, Steven AC, Bax A, Wickner RB. "Is the prion domain of soluble Ure2p unstructured?" Biochemistry. 2005; 44(1): 321-8. PubMed: 15628874
- Thual C, Bousset L, Komar AA, Walter S, Buchner J, Cullin C, Melki R. "Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p." Biochemistry. 2001; 40(6): 1764-73. PubMed: 11327838
- Thual C, Komar AA, Bousset L, Fernandez-Bellot E, Cullin C, Melki R. "Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2." 1999; 274(19): 13666-74. PubMed: 10224139
| Comments:
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| References |
- Wickner RB, Taylor KL, Edskes HK, Maddelein ML, Moriyama H, Roberts BT. "Prions of yeast as heritable amyloidoses." J Struct Biol. 2000; 130(2-3): 310-22. PubMed: 10940235
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