Source:http://linkedlifedata.com/resource/pubmed/id/12532265
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2003-1-17
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pubmed:databankReference | |
pubmed:abstractText |
The P-type ATPases comprise a well-studied family of proteins involved in the active transport of charged substrates across biological membranes. Starting from a mouse bone marrow-derived macrophage cDNA library and using a signal peptide trapping strategy, we identified a new P-type ATPase family member. We characterized the genomic structure of this gene, named Atp10d, as well as its human counterpart. The presence of P-type ATPase consensus motifs and phylogenetic analysis showed that this gene is a member of the type IV, putative amphipath transporters subfamily. We showed that this gene is expressed in kidney and placenta. We also found that the C57BL/6 strain carries a constitutive stop codon in the sequence of Atp10d exon 12, whereas 14 other inbred mouse strains show an uninterrupted reading frame at this location. This mutation in C57BL/6 should lead to a non-functional protein, suggesting that this gene may not be essential. We discuss the involvement of the Atp10d gene in the fat-prone phenotype of the C57BL/6 strain and its physical mapping within a QTL associated with HDL-cholesterol levels.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Transfer Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0938-8990
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21-30
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12532265-Adenosine Triphosphatases,
pubmed-meshheading:12532265-Animals,
pubmed-meshheading:12532265-Carrier Proteins,
pubmed-meshheading:12532265-Computational Biology,
pubmed-meshheading:12532265-Humans,
pubmed-meshheading:12532265-Macaca fascicularis,
pubmed-meshheading:12532265-Macrophages,
pubmed-meshheading:12532265-Membrane Proteins,
pubmed-meshheading:12532265-Mice,
pubmed-meshheading:12532265-Mice, Inbred C57BL,
pubmed-meshheading:12532265-Molecular Sequence Data,
pubmed-meshheading:12532265-Peptide Library,
pubmed-meshheading:12532265-Phospholipid Transfer Proteins,
pubmed-meshheading:12532265-Phylogeny,
pubmed-meshheading:12532265-Protein Sorting Signals,
pubmed-meshheading:12532265-Sequence Analysis, DNA
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pubmed:year |
2003
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pubmed:articleTitle |
Characterization of a putative type IV aminophospholipid transporter P-type ATPase.
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pubmed:affiliation |
Hôpital Necker-Enfants Malades, INSERM U393, Tour Lavoisier, 2 ème étage, 149 rue de Sèvres, 75015 Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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