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J. Biol. Chem., Vol. 277, Issue 12, 9736-9740, March 22, 2002
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§,
, and
From the 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.
Department of Biochemistry and Molecular
Biology, Penn State University, University Park, Pennsylvania 16802 and
¶ Department of Biology, Amherst College, Amherst, Massachusetts
01002
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY066014 and AY069938.
§ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, 410 South Frear Laboratory, Penn State University, University Park, PA 16802. Tel.: 814-863-1767; Fax: 814-863-7024; E-mail: msh4@psu.edu.This article has been cited by other articles:
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