| General information | | DisProt: | DP00638 | | Name: | Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma | | Synonym(s): | CNRG_BOVIN
GMP-PDE gamma
EC=3.1.4.17
PDE6
| | First appeared in release: | Release 5.2 (08/07/2010) | | UniProt: | P04972 | | UniGene: | Bt.54 | | SwissProt: | CNRG_BOVIN | | TrEMBL: | | | NCBI (GI): | 116582 | | Source organism: | Bos taurus (Bovine) | | Sequence length: | 87 | | Percent disordered: | 41% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MNLEPPKAEI RSATRVMGGP VTPRKGPPKF KQRQTRQFKS KPPKKGVQGF GDDIPGMEGL - 60
GTDITVICPW EAFNHLELHE LAQYGII
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| Functional narrative |
Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated photo-transduction in vertebrate rods and cones.It is intrinsically disordered but exhibits transient secondary structure in solution.
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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: | Central polycationic region | | Location: | 24 - 45 | | Length: | 22 | | Region sequence: |
RKGPPKFKQRQTRQFKSKPPKK | | Modification type: | Native
| | PDB: | 2JU4:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Intraprotein interaction
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 4; A64-PDE{gamma} (or mPROXYL-PDE{gamma}) 50 uM; H2O/D2O (90%/10%); Protein concentration range: 50 -90 uM)
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.5; MOPS 20 mM; NaCl 200 mM; PDE{gamma} (Wild-type in Pf1 bacteriophage))
| References:
- Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. "Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure." Proc Natl Acad Sci U S A. 2008; 105(5): 1505-10. PubMed: 18230733
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | C-terminal region | | Location: | 74 - 87 | | Length: | 14 | | Region sequence: |
NHLELHELAQYGII | | Modification type: | Engineered
Fragment
| | PDB: | 2JU4:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Intraprotein interaction
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 4; A64-PDE{gamma} (or mPROXYL-PDE{gamma}) 50 uM; H2O/D2O (90%/10%); Protein concentration range: 50 -90 uM)
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.5; MOPS 20 mM; NaCl 200 mM; PDE{gamma} (Wild-type in Pf1 bacteriophage))
| References:
- Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. "Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure." Proc Natl Acad Sci U S A. 2008; 105(5): 1505-10. PubMed: 18230733
| Comments:
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| References |
- Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. "Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure." Proc Natl Acad Sci U S A. 2008; 105(5): 1505-10. PubMed: 18230733
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| Comments |
AV (8-1-2010) PubMed: 18230733
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