Guimbal C, Kilimann M W
Institut für Physiologische Chemie, Medizinische Fakultät Ruhr-Universität Bochum, Germany.
J Mol Biol. 1994 Aug 12;241(2):317-24. doi: 10.1006/jmbi.1994.1507.
A family of homologous, Na+/Cl- dependent plasma membrane transporters catalyze the uptake of a number of neurotransmitters and structurally related compounds into cells. Here, we report the cDNA cloning, sequencing and functional characterization of a non-mammalian member of this transporter family. A creatine transporter from the electric ray, Torpedo marmorata, displays 64% amino acid identity with its rabbit counterpart and has a similar substrate affinity and specificity. Sequence similarity generally is lowest in those regions where also the sequences of other members of the family, transporting different substrates, diverge. Only a few amino acids are better conserved between the two creatine transporters than with the other family members and are candidates for a role in conferring substrate specificity.
一类同源的、依赖Na⁺/Cl⁻的质膜转运蛋白催化多种神经递质和结构相关化合物进入细胞。在此,我们报道了该转运蛋白家族一个非哺乳动物成员的cDNA克隆、测序及功能特性。电鳐(Torpedo marmorata)的肌酸转运蛋白与其兔源对应物具有64%的氨基酸同一性,且具有相似的底物亲和力和特异性。一般来说,在该家族中转运不同底物的其他成员序列也存在差异的那些区域,序列相似性最低。在这两种肌酸转运蛋白之间,只有少数氨基酸比与其他家族成员的氨基酸保守性更好,这些氨基酸是赋予底物特异性的候选氨基酸。