https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Elisa+Pasqualetto 2026-10-03T10:53:03Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=STAS_domain_of_the_SLC26_anion_transporter_prestin&diff=1404194 2012-06-08T12:56:17Z

<p>Elisa Pasqualetto: </p> <hr /> <div>== The SulP family ==<br /> <br /> The Sulphate permease SulP is a large and diverse family of integral membrane proteins, with members found in eubacteria, plants, fungi and mammals (SLC26). These anion transporters show a similar structural organization: a highly conserved transmembrane central core and a less conserved cytoplasmic C-terminal portion, comprising a STAS domain. <br /> <br /> [[Image:Table_slc.jpg|300px]]<br /> <br /> == The STAS domain ==<br /> <br /> The STAS domain (Sulphate Transporter and Anti-Sigma factor antagonist) was identified by omology between the SulP gene family and the bacterial anti-sigma factor antagonist (ASA) SpoIIAA of Bacillus subtilis.<br /> The STAS domain is involved in the function/regulation of SulP transporters.<br /> Most probably the 3D structures of the anion transporters STAS domains significantly deviate from those of the bacterial ASAs, whose structures are known.</div>

Elisa Pasqualetto https://proteopedia.org/index.php?title=STAS_domain_of_the_SLC26_anion_transporter_prestin&diff=1404193 2012-06-08T12:55:41Z

<p>Elisa Pasqualetto: </p> <hr /> <div>== The SulP family ==<br /> <br /> The Sulphate permease SulP is a large and diverse family of integral membrane proteins, with members found in eubacteria, plants, fungi and mammals (SLC26). These anion transporters show a similar structural organization: a highly conserved transmembrane central core and a less conserved cytoplasmic C-terminal portion, comprising a STAS domain. <br /> <br /> [[Image:Table_slc.jpg]]<br /> <br /> == The STAS domain ==<br /> <br /> The STAS domain (Sulphate Transporter and Anti-Sigma factor antagonist) was identified by omology between the SulP gene family and the bacterial anti-sigma factor antagonist (ASA) SpoIIAA of Bacillus subtilis.<br /> The STAS domain is involved in the function/regulation of SulP transporters.<br /> Most probably the 3D structures of the anion transporters STAS domains significantly deviate from those of the bacterial ASAs, whose structures are known.</div>

Elisa Pasqualetto https://proteopedia.org/index.php?title=File:Table_slc.jpg&diff=1404187 2012-06-08T12:50:28Z

<p>Elisa Pasqualetto: uploaded a new version of &quot;Image:Table slc.jpg&quot;</p> <hr /> <div>The 11 human SLC26 anion transporters.</div>

Elisa Pasqualetto https://proteopedia.org/index.php?title=File:Table_slc.jpg&diff=1404178 2012-06-08T12:43:18Z

<p>Elisa Pasqualetto: The 11 human SLC26 anion transporters.</p> <hr /> <div>The 11 human SLC26 anion transporters.</div>

Elisa Pasqualetto https://proteopedia.org/index.php?title=STAS_domain_of_the_SLC26_anion_transporter_prestin&diff=1404175 2012-06-08T12:37:46Z

<p>Elisa Pasqualetto: New page: == The SulP family == The Sulphate permease SulP is a large and diverse family of integral membrane proteins, with members found in eubacteria, plants, fungi and mammals (SLC26). These a...</p> <hr /> <div><br /> == The SulP family ==<br /> <br /> The Sulphate permease SulP is a large and diverse family of integral membrane proteins, with members found in eubacteria, plants, fungi and mammals (SLC26). These anion transporters show a similar structural organization: a highly conserved transmembrane central core and a less conserved cytoplasmic C-terminal portion, comprising a STAS domain. <br /> <br /> == The STAS domain ==<br /> <br /> The STAS domain (Sulphate Transporter and Anti-Sigma factor antagonist) was identified by omology between the SulP gene family and the bacterial anti-sigma factor antagonist (ASA) SpoIIAA of Bacillus subtilis.<br /> The STAS domain is involved in the function/regulation of SulP transporters.<br /> Most probably the 3D structures of the anion transporters STAS domains significantly deviate from those of the bacterial ASAs, whose structures are known.</div>

Elisa Pasqualetto