{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q3UMR5","secondaryAccessions":["B2RTD1","Q3TTK3"],"uniProtkbId":"MCU_MOUSE","entryAudit":{"firstPublicDate":"2007-04-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-04-03","entryVersion":139,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Calcium uniporter protein, mitochondrial"}},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:3026965"}],"value":"Mcu"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21685886"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23900286"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24212091"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25251370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25603276"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25732818"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26119731"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26119742"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26644474"}],"value":"Channel-forming and calcium-conducting subunit of the mitochondrial inner membrane calcium uniporter complex (uniplex), which mediates calcium uptake into the mitochondrial matrix (PubMed:21685886, PubMed:23900286, PubMed:24212091). MCU channel activity is regulated by the calcium-sensor subunits of the uniplex MICU1 and MICU2 (or MICU3) (By similarity). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates ATP production, cytoplasmic calcium signals and activation of cell death pathways (By similarity). Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes (By similarity). While dispensable for baseline homeostatic cardiac function, acts as a key regulator of short-term mitochondrial calcium loading underlying a 'fight-or-flight' response during acute stress: acts by mediating a rapid increase of mitochondrial calcium in pacemaker cells (PubMed:25603276, PubMed:26119731, PubMed:26119742). Participates in mitochondrial permeability transition during ischemia-reperfusion injury (PubMed:26119731). Mitochondrial calcium uptake in skeletal muscle cells is involved in muscle size in adults (PubMed:25732818). Regulates synaptic vesicle endocytosis kinetics in central nerve terminal (PubMed:26644474). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (By similarity). Involved in antigen processing and presentation (PubMed:25251370)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Ca(2+)(in) = Ca(2+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29671"},{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"}],"value":"MCU channel activity is regulated by the heterodimer composed of MICU1 and either MICU2 or MICU3, which act as calcium-sensors (By similarity). At low calcium levels, MICU1 occludes the pore of the MCU channel, preventing mitochondrial calcium uptake (By similarity). At higher calcium levels, calcium-binding to MICU1 and MICU2 (or MICU3) induces a conformational change that weakens MCU-MICU1 interactions and moves the MICU1-MICU2 heterodimer away from the pore, allowing calcium permeation through the channel (By similarity). MCU channel activity is gated by EMRE/SMDT1 via the juxtamembrane helix loop (By similarity). Inhibited by ruthenium red or its derivative Ru360 (By similarity)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23409044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23900286"}],"value":"Homotetramer (PubMed:23900286). Component of the uniplex complex, composed of MCU, EMRE/SMDT1, MICU1 and MICU2 (or MICU3) in a 4:4:1:1 stoichiometry (PubMed:23409044). Interacts with CCDC109B/MCUB; this inhibits channel activity (By similarity). Interacts with MCUR1 (By similarity). Interactions with MICU1 and MCUR1 are mutually exclusive (By similarity). Interacts with SLC25A23 (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q3UMR5","intActId":"EBI-776370"},"interactantTwo":{"uniProtKBAccession":"Q810S1","geneName":"Mcub","intActId":"EBI-8847756"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23900286"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"26057074"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23900286"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q3UMR5-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q3UMR5-2"],"sequenceIds":["VSP_024264","VSP_024265"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21685888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23409044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23900286"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26057074"}],"value":"Detected in heart muscle (at protein level) (PubMed:26057074). Expressed in skeletal muscle, heart, kidney, liver, brain, lung, white fat and spleen"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"}],"value":"The selectivity filter, in which calcium ions are arranged in single file, is composed of two acidic rings separated by one helical turn along the central axis of the channel pore"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"}],"value":"The N-terminal domain is required for efficient Ca(2+) uptake and for interaction with MCUR1. It is not required for targeting to the mitochondria, oligomerization, interaction with MICU1 and MICU2, or assembly of the uniplex complex"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"}],"value":"Phosphorylation by CaMK2 in heart leads to increased MCU current. The regulation of MCU by CaMK2 is however subject to discussion: another group was unable to reproduce these results. Phosphorylated on tyrosines by PTK2B/PYK2, promoting oligomerization"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"}],"value":"Glutathionylation at Cys-96 in response to reactive oxygen species (ROS) promotes MCU higher-order assembly, leading to constitutive activation of the MCU channel and mitochondrial calcium overload"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8NE86"}],"value":"Undergoes proteolytic degradation by SPG7"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24212091"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26057074"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26119731"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26119742"}],"value":"No visible phenotype (PubMed:24212091, PubMed:26057074). Although slightly smaller, mice are grossly normal (PubMed:24212091). Only minor alterations in basal energetics are observed (PubMed:24212091). Cells show a strong reduction, but not a complete absence, of mitochondrial matrix calcium (PubMed:24212091). The skeletal muscles exhibit alterations in the phosphorylation and activity of pyruvate dehydrogenase and mice show defects in ability to perform strenuous work (PubMed:24212091). Mitochondria lack evidence for calcium-induced permeability transition pore (PTP) opening (PubMed:24212091). Mitochondria from mutant mouse heart muscle have impaired Ca(2+) uptake and reduced Ca(2+) levels in the mitochondrial matrix; still, mutant mice have apparently normal heart function and display no cardiac defects (PubMed:26057074). Conditional mutant mice with cardiomyocyte-specific deletion of Mcu in adults display no overt baseline phenotype and are protected against mitochondrial calcium overload by preventing the activation of the mitochondrial permeability transition pore (PubMed:26119731, PubMed:26119742). Mice however lack contractile responsiveness to acute stress and 'fight-or-flight' response: they produce mitochondria refractory to acute calcium uptake, with impaired ATP production and inhibited mitochondrial permeability transition pore opening upon acute calcium challenge (PubMed:26119731, PubMed:26119742)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the MCU (TC 1.A.77) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"Calcium uniporter protein, mitochondrial","featureId":"PRO_0000282977"},{"type":"Topological 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