Homology of pendrin sodium-iodide symporter and apical iodide transporter

Autor: Fabrizio Guarneri, Salvatore Benvenga
Rok vydání: 2018
Předmět:
Monocarboxylic Acid Transporters
0301 basic medicine
Sodium-iodide symporter
pendrin
Hearing Loss
Sensorineural
030209 endocrinology & metabolism
Pendred’s syndrome
medicine.disease_cause
Homology (biology)
apical iodide transporter
03 medical and health sciences
Solute carriers
0302 clinical medicine
Hypothyroidism
sodium/ iodide symporter
otorhinolaryngologic diseases
medicine
Humans
Amino Acid Sequence
STAS domain
Peptide sequence
health care economics and organizations
Ion transporter
Monocarboxylate transporter
Mutation
Ion Transport
Sequence Homology
Amino Acid
Symporters
biology
iodine
Chemistry
Pendrin
Iodides
Molecular biology
amino acid sequence homology
030104 developmental biology
Solute carriers
pendrin
sodium/ iodide symporter
apical iodide transporter
Pendred’s syndrome
iodine
amino acid sequence homology
STAS domain
Sulfate Transporters
Symporter
biology.protein
Goiter
Nodular
Zdroj: Frontiers in Bioscience. 23:1864-1873
ISSN: 1093-4715
1093-9946
DOI: 10.2741/4677
Popis: We observed local homology between human pendrin and sodium/iodide symporter (NIS), that was absent in the NIS-homologous sodium/monocarboxylate transporter or apical iodide transporter (AIT) which, however, does not transport iodide. Thus, we analyzed the full proteins. They shared 63 identical and 66 similar residues (overall homology 14.4%, but 21% when omitting intervening sequences of 15 or more residues). Pendrin was more homologous to NIS (25%) than AIT (20%), particularly in the STAS domain (sulfate transporter and antisigma factor antagonist). Homology was concentrated in 11 segments, with 3/11 involving the STAS domain. In 9/11, homology was greater with NIS (45-58.3%) than with AIT (8.3-42.3%); in 4 of these 9 segments, homology was comparable to or greater than that between NIS and AIT (8.3-52.6%). Pendrin residues which are mutated in Pendred's syndrome are identical to those in the aligned position of NIS and AIT. Hypothyroidism-associated pendrin mutations almost always fall within 4/11 segments. These are the first data that show homology between pendrin and NIS, and topographic relationships between pendrin mutations and the hypothyroid phenotype of PDS.
Databáze: OpenAIRE
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