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. Author manuscript; available in PMC: 2014 Feb 7.
Published in final edited form as: Curr Cancer Drug Targets. 2010 Mar;10(2):242–267. doi: 10.2174/156800910791054194

Fig. 2.

Fig. 2

Secondary structure model of functional NIS protein. NIS is predicted to have 13 transmembrane domains with the NH2 terminus facing extracellularly and the COOH terminus facing intracellularly. There are three potential glycosylation sites at positions 225, 485, and 497 of the amino acid sequence. The length of the 13 transmembrane segments ranges from 20–28 amino acids, except for transmembrane segment V which contains 18 residues. (Modified from Spitzweg et al J. Clin. Endocrinol. Metab 2001 86, 3327–35).