<http://purl.uniprot.org/SHA-384/544657039C8E613B2B1974DA8C0090E782081F3A085B496F185600BC2D35F1A528F27EB7127B70CB0497986D0E799B2D> <http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://purl.uniprot.org/core/Domain_Annotation> .
<http://purl.uniprot.org/SHA-384/544657039C8E613B2B1974DA8C0090E782081F3A085B496F185600BC2D35F1A528F27EB7127B70CB0497986D0E799B2D> <http://www.w3.org/2000/01/rdf-schema#comment> "The transmembrane domain (TM) is the major site of interaction with SLC51A. The extracellular-membrane interface is absolutely required for transport activity. The intracellular-membrane interface is necessary for establishing the correct membrane orientation that is essential for the heterodimer Ost-alpha/Ost-beta complex formation and transport activity at the cell membrane surface." .
<http://purl.uniprot.org/uniprot/Q80WK2> <http://purl.uniprot.org/core/annotation> <http://purl.uniprot.org/SHA-384/544657039C8E613B2B1974DA8C0090E782081F3A085B496F185600BC2D35F1A528F27EB7127B70CB0497986D0E799B2D> .