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An ABC transporter homologous to TAP proteins
Author(s) -
Yamaguchi Yoko,
Kasano Miki,
Terada Tomoyuki,
Sato Ryuichiro,
Maeda Masatomo
Publication year - 1999
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/s0014-5793(99)01042-x
Subject(s) - complementary dna , transporter associated with antigen processing , biology , peptide sequence , transmembrane domain , atp binding cassette transporter , biochemistry , microbiology and biotechnology , amino acid , coding region , gene , transmembrane protein , nucleic acid sequence , alternative splicing , rna splicing , gene isoform , transporter , genetics , mhc class i , major histocompatibility complex , rna , receptor
Polymerase chain reaction amplification of cDNA from rat intestine revealed the expression of a novel ABC transporter, TAPL (TAP‐like). Subsequently, the protein sequence was deduced from the nucleotide sequence of cDNA carrying the entire coding region. TAPL is transcribed ubiquitously in various rat tissues. The protein, with 762 amino acid residues, has potential transmembrane domains, and an ATP‐binding domain in its amino and carboxyl terminal regions, respectively, and is highly homologous to TAP1 and TAP2 (transporters associated with antigen presentation/processing): pairwise comparisons with TAPL demonstrated 39 and 41% of the residues are identical, respectively. These numerical values are essentially the same as that for TAP1 and TAP2 (39%), and the hydropathy profiles of TAPL, TAP1 and TAP2 are quite similar. The similarity among these three proteins suggests that they could be derived from a common ancestral gene. Furthermore, we found that there is a potential splicing isoform, sharing the amino terminal 720 amino acid residues of TAPL.