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XB-ART-54060
Neuron 1994 Aug 01;132:395-404.
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Molecular cloning and characterization of retinal photoreceptor guanylyl cyclase-activating protein.

Palczewski K , Subbaraya I , Gorczyca WA , Helekar BS , Ruiz CC , Ohguro H , Huang J , Zhao X , Crabb JW , Johnson RS .


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Guanylyl cyclase-activating protein (GCAP) is thought to mediate Ca(2+)-sensitive regulation of guanylyl cyclase (GC), a key event in recovery of the dark state of rod photoreceptors following light exposure. Here, we characterize GCAP from several vertebrate species by molecular cloning and provide evidence that GCAP contains a heterogeneously acylated N-terminal region that interacts with GC. Vertebrate GCAPs consist of 201-205 amino acids, and sequence analysis indicates the presence fo three EF hand Ca(2+)-binding motifs. These results establish that GCAP is a novel photoreceptor-specific member of a large family of Ca(2+)-binding proteins and suggest that it participates in the Ca(2+)-binding proteins and suggest that it participates in the Ca(2+)-sensitive activation of GC.

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Species referenced: Xenopus
Genes referenced: guca1a