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DESCRIBE <http://purl.uniprot.org/SHA-384/6F715C067ED224AE0736C3DA53C14A4B4F989BB9449F253F4DEAE18F4F9DD041EAE8B8C93B1B04EDA9A45D1129D5C0C3>
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http://purl.uniprot.org/SHA-384/6F715C067ED224AE0736C3DA53C14A4B4F989BB9449F253F4DEAE18F4F9DD041EAE8B8C93B1B04EDA9A45D1129D5C0C3
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/6F715C067ED224AE0736C3DA53C14A4B4F989BB9449F253F4DEAE18F4F9DD041EAE8B8C93B1B04EDA9A45D1129D5C0C3
http://www.w3.org/2000/01/rdf-schema#comment
"Structure-function analysis of the Arabidopsis TPC1 channel in planta confirmed that helix S10 operates as the major voltage-sensing site with Glu450 and Glu478 identified as possible ion-pair partners for voltage-sensing Arg537."
xsd:string
http://purl.uniprot.org/uniprot/#_D5BA9942C0EDA6E236A3E2632D596A88C4EA21A3EB7BB31DE81CC5B18384ACCED129E5DA899F55A259FCBF42606565FE
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/6F715C067ED224AE0736C3DA53C14A4B4F989BB9449F253F4DEAE18F4F9DD041EAE8B8C93B1B04EDA9A45D1129D5C0C3
http://purl.uniprot.org/uniprot/Q94KI8
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/6F715C067ED224AE0736C3DA53C14A4B4F989BB9449F253F4DEAE18F4F9DD041EAE8B8C93B1B04EDA9A45D1129D5C0C3
http://purl.uniprot.org/uniprot/#_Q94KI8-mappedCitation-27270880
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/6F715C067ED224AE0736C3DA53C14A4B4F989BB9449F253F4DEAE18F4F9DD041EAE8B8C93B1B04EDA9A45D1129D5C0C3