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Opsins from the lateral eyes and ocelli of the horseshoe crab, Limulus polyphemus.


ABSTRACT: cDNA clones encoding opsins from the lateral eyes and median ocelli of the horseshoe crab, Limulus polyphemus, were isolated from cDNA libraries. The opsin cDNAs obtained from the lateral eye and ocellar libraries code for deduced proteins with 376 amino acids. The two cDNAs are 96% identical at the nucleic acid level, differing primarily at the 3' untranslated region, and are apparently the products of two separate genes. The deduced opsin proteins are 99% identical to each other, differing at only 5 amino acids. The opsins encoded by these cDNAs are most likely the protein moiety of the visible-wavelength rhodopsins in this animal. In the lateral eye, expression of the opsin gene is restricted to the photoreceptor cells of the ommatidia. Comparisons with opsins of other species show that the Limulus opsin proteins are most similar (53% identity) to the opsin from the R1-6 photoreceptors of flies.

SUBMITTER: Smith WC 

PROVIDER: S-EPMC46885 | biostudies-other | 1993 Jul

REPOSITORIES: biostudies-other

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Opsins from the lateral eyes and ocelli of the horseshoe crab, Limulus polyphemus.

Smith W C WC   Price D A DA   Greenberg R M RM   Battelle B A BA  

Proceedings of the National Academy of Sciences of the United States of America 19930701 13


cDNA clones encoding opsins from the lateral eyes and median ocelli of the horseshoe crab, Limulus polyphemus, were isolated from cDNA libraries. The opsin cDNAs obtained from the lateral eye and ocellar libraries code for deduced proteins with 376 amino acids. The two cDNAs are 96% identical at the nucleic acid level, differing primarily at the 3' untranslated region, and are apparently the products of two separate genes. The deduced opsin proteins are 99% identical to each other, differing at  ...[more]

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