Reanalysis of ATP11B, a type IV P-type ATPase
| Autor: | Margaret S. Halleck, Patrick Williamson, Robert A. Schlegel |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
DNA
Complementary Transcription Genetic ATPase Molecular Sequence Data Biology Biochemistry Polymerase Chain Reaction Substrate Specificity Exon Mice Animals Humans Amino Acid Sequence RNA Messenger Molecular Biology Ion transporter Phylogeny Adenosine Triphosphatases Cell Nucleus Expressed Sequence Tags Models Genetic Sequence Homology Amino Acid cDNA library Alternative splicing Cell Biology Exons Molecular biology Cell biology Protein Structure Tertiary Transmembrane domain Protein Transport Proton-Translocating ATPases ATP11B P-type ATPase biology.protein Rabbits Schizosaccharomyces pombe Proteins Molecular Chaperones |
| Zdroj: | The Journal of biological chemistry. 277(12) |
| ISSN: | 0021-9258 |
| Popis: | P-type ATPases are a venerable family of ATP-dependent ion transporters. Recently, evidence was presented that a rabbit gene in the type IV subfamily of P-type ATPases was missing a transmembrane helix (transmembrane domain 4) thought to be critical for ion transport, a deletion that would place the two major catalytic loops of the enzyme on opposite sides of the membrane. It was proposed that the resulting protein was a RING finger-binding protein that targets transcription factors to specific domains within the nucleus. From analysis of human genomic sequence data, it is shown here that the region containing transmembrane domain 4, corresponding to exon 12, is present in the human homolog of the gene, ATP11B. PCR analysis indicates that the predominant Atp11b transcripts in a rabbit cDNA library and in a mouse cDNA library also contain exon 12. The results suggest that the transcript proposed to encode the RING finger-binding protein is a minor rabbit-specific splice variant. The ATP11B gene thus may not encode a protein with a function radically different from that of other P-type ATPase transporters. |
| Databáze: | OpenAIRE |
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