Primary structure and chromosomal localization of human and mouse rod photoreceptor cGMP-gated cation channel.

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Citation

Pittler SJ, Lee AK, Altherr MR, Howard TA, Seldin MF, Hurwitz RL, Wasmuth JJ, Baehr W

Primary structure and chromosomal localization of human and mouse rod photoreceptor cGMP-gated cation channel.

J Biol Chem. 1992 Mar 25;267(9):6257-62.

PubMed ID
1372902 [ View in PubMed
]
Abstract

We have determined the primary structures of the human and mouse retinal rod cGMP-gated cation channel by analysis of cDNA clones and amplified DNA. The open reading frames predicted polypeptides of 690 and 683 residues exhibiting 88% sequence similarity. Sequence comparison indicated that the rod channels consist of a variable 90-residue N-terminal region, a short highly charged segment rich in lysine and glutamate, and a 540-residue C-terminal portion that is well conserved in three mammalian species. Significant sequence similarity (59%) of the visual cGMP-gated channel to the olfactory cAMP-gated channel established the existence of a family of cyclic nucleotide-gated ion channel genes. RNA blot analysis revealed transcripts of 3.2 kilobases (kb) in human, mouse, and dog, 3.2, 4.6, and 5.2 kb in bovine, and 3.6 kb in fish. The human channel gene was mapped by polymerase chain reaction of somatic cell hybrid DNAs to chromosome 4 (p14-q13) near the centromere. The mouse channel gene locus (Cncg) was mapped by interspecific backcross haplotype analysis 0.9 centimorgan proximal of the Kit locus on chromosome 5.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
cGMP-gated cation channel alpha-1P29973Details