{"id":"6131952d-585d-52c2-a058-7e4cd492f9f1","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-coa6-sco1-reduction","predicate":"reduces_disulfides_in","statement":"COA6 acted as a thiol reductase for critical cysteine disulfides in SCO1.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"50cab790-0840-5830-a5cb-29240e2cc94f","mechanism_event_label":"An assembly factor prepares copper-binding sites for use.","subject":{"id":"7ff2c8cb-50e2-5ac1-82d2-50a914b38a14","slug":"coa6","display_name":"Human cytochrome c oxidase assembly factor COA6","entity_type_key":"protein"},"object":{"id":"6c18f07d-6a6e-5dcd-8294-2a3b3ee9c27c","slug":"sco1","display_name":"Human cytochrome c oxidase assembly protein SCO1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"50cab790-0840-5830-a5cb-29240e2cc94f","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-coa6-sco1-reduction-event","event_type":"biochemical_relationship","label":"An assembly factor prepares copper-binding sites for use.","description":"COA6 acted as a thiol reductase for critical cysteine disulfides in SCO1.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"f2fd6214-9693-51a4-b4f4-54b5153745f4","slug":"cox-cua-assembly","display_name":"Assembly of the cytochrome c oxidase binuclear CuA center","entity_type_key":"cellular_process"},"role":"downstream assembly process","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"7ff2c8cb-50e2-5ac1-82d2-50a914b38a14","slug":"coa6","display_name":"Human cytochrome c oxidase assembly factor COA6","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"6c18f07d-6a6e-5dcd-8294-2a3b3ee9c27c","slug":"sco1","display_name":"Human cytochrome c oxidase assembly protein SCO1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/copper-research/32061935.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a\", \"start_char\": 0, \"end_char\": 1043, \"text_sha256\": \"7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"COA6 knockout HEK293T cells and biochemical protein interaction experiments","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"COA6 loss; SCO1/SCO2 disulfide reduction assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"COA6 machinery failure is not dietary copper depletion. Protein import effects were selective rather than universal loss of all mitochondrial import.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Copper research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Human cells and proteins","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"An assembly factor prepares copper-binding sites for use.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[copper-p32061935] COA6 Facilitates Cytochrome c Oxidase Biogenesis as Thiol-reductase for Copper Metallochaperones in Mitochondria. (2020). https://pubmed.ncbi.nlm.nih.gov/32061935/ DOI: 10.1016/j.jmb.2020.01.036","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Mitochondrial intermembrane space","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"3eaa4589-68a3-5357-b3a6-f8af7bdd3d18","evidence_kind":"source_excerpt","locator":"Lines 650-661","start_line":650,"end_line":661,"excerpt":"### copper-coa6-sco1-reduction\nCOA6 acted as a thiol reductase for critical cysteine disulfides in SCO1.\nCondition category: normal\nnutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: An assembly factor prepares copper-binding sites for use.\norganism: Human cells and proteins\ntissue_or_cell_type: Mitochondrial intermembrane space\nexperimental_model: COA6 knockout HEK293T cells and biochemical protein interaction experiments\nlimitations: COA6 machinery failure is not dietary copper depletion. Protein import effects were selective rather than universal loss of all mitochondrial import.\nexposure: COA6 loss; SCO1/SCO2 disulfide reduction assays\nevidence_span: {\"source_cache\": \"artifacts/copper-research/32061935.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a\", \"start_char\": 0, \"end_char\": 1043, \"text_sha256\": \"7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a\"}\n[copper-p32061935] COA6 Facilitates Cytochrome c Oxidase Biogenesis as Thiol-reductase for Copper Metallochaperones in Mitochondria. 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