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Primary structure of a novel ABC transporter with a chromosomal localization on the band encoding the multidrug resistance‐associated protein
Author(s) -
Klugbauer Norbert,
Hofmann Franz
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00700-4
Subject(s) - multiple drug resistance , atp binding cassette transporter , encoding (memory) , primary (astronomy) , transporter , genetics , biology , gene , computational biology , drug resistance , neuroscience , physics , astronomy
Complementary DNA clones encoding a novel protein, ABC‐C, with the typical structural features of the ABC transporter family were identified in a human medullary thyroid carcinoma cell line. The transporter consists of 1704 amino acid residues with two homologous repeats, each harboring six putative transmembrane helices and an ATP‐binding cassette motif. The mRNA is expressed highest in normal lung, but also in varying amounts in other tissues and in C‐cell carcinoma. The ABC‐C gene is mapped on chromosome 16p13.3, in close physical proximity to another ABC transporter, the multidrug resistance‐associated protein. This related protein is assumed to confer resistance to chemotherapeutic drugs in small cell lung carcinoma. The genomic clustering of both transporters, typical also for other members of the ABC family, supports the notion that ABC‐C may be involved in development of resistance to xenobiotics.