{"id":"3fc8a0ad-3e98-5b53-8261-f8e19f90853d","stable_key":"911fb3c7-8cc3-5667-b677-5682fab67648:histidine-lat1-exchange","predicate":"transports","statement":"Reconstituted human LAT1 supported histidine antiport, including exchange with internal cysteine, tyrosine or glutamine; external histidine affinity exceeded internal affinity.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"5f13eec0-aadb-52f5-9878-9396db26054c","mechanism_event_label":"The transporter exchanges substrates, so both sides of the membrane matter.","subject":{"id":"16d078ff-692c-50eb-a34b-c61ef43821e1","slug":"slc7a5","display_name":"Human L-type amino acid transporter 1 / LAT1 / SLC7A5","entity_type_key":"protein"},"object":{"id":"44374451-3436-5136-a8ae-5dcc6d8c353b","slug":"histidine","display_name":"L-Histidine","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"5f13eec0-aadb-52f5-9878-9396db26054c","stable_key":"911fb3c7-8cc3-5667-b677-5682fab67648:histidine-lat1-exchange-event","event_type":"observed_relationship","label":"The transporter exchanges substrates, so both sides of the membrane matter.","description":"Reconstituted human LAT1 supported histidine antiport, including exchange with internal cysteine, tyrosine or glutamine; external histidine affinity exceeded internal affinity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"16d078ff-692c-50eb-a34b-c61ef43821e1","slug":"slc7a5","display_name":"Human L-type amino acid transporter 1 / LAT1 / SLC7A5","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"44374451-3436-5136-a8ae-5dcc6d8c353b","slug":"histidine","display_name":"L-Histidine","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"ca899f13-50ad-55e5-ab99-329ae0038c74","slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"bcfef85f-831d-5439-ba51-1aef4b090441","slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"8637bb39-2c30-5168-baaf-3e613d831db0","slug":"glutamine","display_name":"L-Glutamine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human SiHa extracts and purified recombinant human LAT1 in proteoliposomes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"In-vitro exchange does not establish whole-body competition or supplement ratios.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"histidine","display_name":"L-Histidine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"The transporter exchanges substrates, so both sides of the membrane matter.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"LAT1 is the transport competent unit of the LAT1/CD98 heterodimeric amino acid transporter. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26256001/ · DOI 10.1016/j.biocel.2015.08.004","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"transport_effect","value_text":"depends","comparator":null,"unit":null,"notes":"Recorded as antiport, including exchange with internal cysteine, tyrosine or glutamine.","entity":null},{"dimension":"transport_pool","value_text":"the cytosol across the plasma membrane","comparator":null,"unit":null,"notes":"Recorded as antiport, including exchange with internal cysteine, tyrosine or glutamine.","entity":null}],"evidence":[{"id":"849bdaae-0c3e-58e7-a9c2-787b1b990442","evidence_kind":"source_excerpt","locator":"Lines 58-64","start_line":58,"end_line":64,"excerpt":"## histidine-lat1-exchange\nThe transporter exchanges substrates, so both sides of the membrane matter.\nReconstituted human LAT1 supported histidine antiport, including exchange with internal cysteine, tyrosine or glutamine; external histidine affinity exceeded internal affinity.\nModel: Human SiHa extracts and purified recombinant human LAT1 in proteoliposomes.\nLimitations: In-vitro exchange does not establish whole-body competition or supplement ratios.\nEvidence access: Primary abstract\nLAT1 is the transport competent unit of the LAT1/CD98 heterodimeric amino acid transporter. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26256001/ · DOI 10.1016/j.biocel.2015.08.004","model_system":"Human SiHa extracts and purified recombinant human LAT1 in proteoliposomes.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"ce59e6c9-1213-523b-9d0b-400b7a81cd1c","stable_key":"import-911fb3c7-8cc3-5667-b677-5682fab67648","title":"L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text.","file_path":"","sha256":"cb672530ec8b4a4542d0f3957e80ca76bb0449e9f988845b0f7681f623c4ec9b","revision_id":"19a7f26c-d9a1-5411-a81d-025f3d98a452","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}