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Parts of this article (those related to PMID 17658730 and PMID 18425604) are outdated. Please update this article to reflect recent events or newly available information. (November 2010) |
The outer and inner segments of vertebrate retina rod photoreceptor cells contain phosducin, a soluble phosphoprotein that complexes with the beta/gamma-subunits of the guanosine triphosphate-binding protein, transducin. Light-induced changes in cyclic nucleotide levels modulate the phosphorylation of phosducin by protein kinase A.[1] The protein is thought to participate in the regulation of visual phototransduction or in the integration of photo-receptor metabolism. Similar proteins have been isolated from the pineal gland and it is believed that the function of the protein is the same in both retina and pineal gland.[2]
[edit] Human proteins containing this domain
| Gene |
Aliases |
Protein |
| PDC |
MEKA |
phosducin |
| PDCL |
PhLP1 |
phosducin-like |
| PDCL2 |
GCPHLP |
phosducin-like 2 |
| PDCL3 |
PhLP2A |
phosducin-like 3 |
| TXNDC9 |
PhLP3 |
thioredoxin domain containing 9 |
[edit] References
- ^ Craft CM, Lee RH, Fowler A, Lolley RN, McGinnis JF (1990). "Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein from photoreceptor cells". J. Biol. Chem. 265 (26): 15867–15873. PMID 2203790.
- ^ Takagi T, Abe T, Nakabayashi H, Tamada H, Sakuragi S, Yamaki K, Shinohara T (1990). "Analysis of the human, bovine and rat 33-kDa proteins and cDNA in retina and pineal gland". Gene 91 (2): 209–215. doi:10.1016/0378-1119(90)90090-E. PMID 2210381.
This article incorporates text from the public domain Pfam and InterPro IPR001200
