1. Isolation of a cDNA encoding the human brain serotonin transporter
- Author
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Klaus-Peter Lesch, Peter Riederer, D. L. Murphy, H. C. Estler, and Benjamin Wolozin
- Subjects
Serotonin ,Molecular Sequence Data ,Nerve Tissue Proteins ,Biology ,Polymerase Chain Reaction ,Open Reading Frames ,Rapid amplification of cDNA ends ,Complementary DNA ,Consensus Sequence ,Animals ,Amino Acid Sequence ,Phosphorylation ,Protein kinase A ,Protein Kinase C ,Biological Psychiatry ,Protein kinase C ,Serotonin Plasma Membrane Transport Proteins ,chemistry.chemical_classification ,Binding Sites ,Membrane Glycoproteins ,Base Sequence ,Nucleic acid sequence ,Membrane Transport Proteins ,DNA ,Molecular biology ,Rats ,Amino acid ,Molecular Weight ,Psychiatry and Mental health ,Open reading frame ,Neurology ,chemistry ,Biochemistry ,Raphe Nuclei ,Neurology (clinical) ,Carrier Proteins ,Rat Protein ,Protein Kinases ,Protein Processing, Post-Translational - Abstract
A cDNA encoding a serotonin transporter (5-HTT) in the human dorsal raphe nucleus was isolated and sequenced using cross-species amplification of human 5-HTT partial cDNA by the polymerase chain reaction (PCR) and the RACE-PCR procedure, designed for rapid amplification of 3' and 5' cDNA ends. The cDNA contains an open reading frame encoding a hydrophobic polypeptide of 630 amino acids with a calculated molecular weight of approximately 70 kDa. The human 5-HTT is approximately 92% homologous to the rat protein but contains an additional consensus phosphorylation site for cAMP-dependent protein kinase recognition located in the cytoplasmic N-terminal region, while a potential protein kinase C phosphorylation site identified in the rat homolog is not conserved in the human 5-HTT. Hydropathicity analysis revealed twelve membrane spanning segments, a topology proposed for other cloned sodium-dependent transporters.
- Published
- 1993
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