Gene Ontology annotation through association of InterPro records with GO terms
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Deep research report for SLC26A11 ortholog in Pan paniscus
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SLC26A11 functions primarily as the lysosomal sulfate exporter, using the proton gradient as driving force
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SLC26A11 localizes predominantly to lysosomes with significant Lamp1 overlap (Manders coefficient 0.45-0.50) and minimal ER overlap (0.09-0.12)
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SLC26A11 exhibits dual transporter-channel function: electroneutral proton:sulfate/chloride exchange and chloride-selective channel conductance
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Bicarbonate and phosphate show minimal or no competition for the SLC26A11 substrate binding site
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Glu-320 acts as a pH-sensitive switch, increasing sulfate binding affinity approximately 50-fold at acidic pH
SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport.
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Purified human SLC26A11 couples proton:sulfate symport to chloride antiport in an electroneutral cycle.
"In the most parsimonious model, SLC26A11 is an exchanger that couples the symport of one proton and one sulfate ion (net charge of −1) to the antiport of one chloride ion (net charge of −1)."
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SLC26A11 also has an uncoupled chloride conductance arising from the transport cycle.
"exhibits an uncoupled, channel-like chloride conductance gated by proton:sulfate"
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SLC26A11 is lysosomal in mammalian cell lines and proposed as the lysosomal sulfate exporter.
"our functional characterization suggests that SLC26A11 represents the elusive lysosomal transporter for sulfate"
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Bicarbonate does not affect SLC26A11 sulfate transport.
"whereas phosphate and bicarbonate had no effect on SLC26A11ΔC activity"
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SLC26A11 is a homodimer with domain-swapped STAS domains.
"Both structures of nanobody-bound SLC26A11ΔC show an SLC26A11 homodimer with cytoplasmic STAS domains swapped between the protomers"
Slc26a11, a chloride transporter, localizes with the vacuolar H(+)-ATPase of A-intercalated cells of the kidney.
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Mouse Slc26a11 is on apical and basolateral membranes of kidney intercalated cells with the V-ATPase.
"KBAT and H+-ATPase colocalize on the apical membrane of A-intercalated cells and on the basolateral membrane of B-intercalated cells in the cortical collecting duct"
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Cellular pHi assays were interpreted as Cl-/HCO3- exchange.
"Taken together, these results are consistent with KBAT functioning in the Cl−∕HCO3− exchange mode."
Slc26a11 is prominently expressed in the brain and functions as a chloride channel: expression in Purkinje cells and stimulation of V H⁺-ATPase.
Molecular and functional characterization of SLC26A11, a sodium-independent sulfate transporter from high endothelial venules.
SLC26A11 Inhibition Reduces Oncotic Neuronal Death and Attenuates Stroke Reperfusion Injury.
Bonobo vs human/mouse SLC26A11 sequence comparison (re-review)
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A0A2R9CAF4 is full length and 99.2% identical to human SLC26A11.
"Bonobo vs human: 601/606 identical aligned positions (99.2%), no gaps; full-length product, not a fragment."
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The pH-sensing Glu-320 is conserved.
"is conserved as E320 in A0A2R9CAF4"
UniProt record A0A2R9CAF4