{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DP25","secondaryAccessions":["P02593","P62158","P70667","P99014","Q13942","Q53S29","Q61379","Q61380","Q96HK3"],"uniProtkbId":"CALM3_HUMAN","entryAudit":{"firstPublicDate":"2017-05-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-05-10","entryVersion":61,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:1449"}],"value":"Calmodulin-3"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:1449"}],"value":"CALM3"},"synonyms":[{"value":"CALML2"},{"value":"CAM3"},{"value":"CAMC"},{"value":"CAMIII"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16760425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31454269"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35568036"}],"value":"Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding (PubMed:16760425, PubMed:31454269). Calcium-binding is required for the activation of calmodulin (PubMed:16760425, PubMed:31454269, PubMed:35568036). Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases (PubMed:16760425, PubMed:35568036). Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35338844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35446120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36423631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36624349"}],"value":"(Microbial infection) Required for C.violaceum CopC and S.flexneri OspC3 arginine ADP-riboxanase activity"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35568036"}],"value":"(Microbial infection) Inactivated by S.flexneri OspC1 and OspC3 proteins, which specifically bind the apo-form of calmodulin, thereby preventing calcium-binding and activity"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DP23"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P62157"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P62161"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P62204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12871148"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15746192"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16127172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16760425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17719545"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18650434"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466722"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22484487"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23109337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25582440"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27516456"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27564677"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27876793"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38297121"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9804419"}],"value":"Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By similarity). Interacts with CEP97, CCP110, TTN/titin and SRY (PubMed:12871148, PubMed:15746192, PubMed:16760425, PubMed:17719545, PubMed:9804419). Interacts with USP6; the interaction is calcium dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722). Interacts with SCN5A (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure (By similarity). Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with IQCF1 (By similarity). Interacts with SYT7 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:18650434, PubMed:27516456). Interacts with PCP4; regulates calmodulin calcium-binding (PubMed:27876793). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates in the proper assembly of a functional heterotetrameric M channel (PubMed:27564677). Component of the SIFI complex (PubMed:25582440, PubMed:38297121)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35338844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35446120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36423631"}],"value":"(Microbial infection) Interacts with C.violaceum CopC (PubMed:35338844, PubMed:35446120, PubMed:36423631). C.violaceum CopC interacts specifically with the apo form of calmodulin (PubMed:35446120, PubMed:36423631)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35568036"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36624349"}],"value":"(Microbial infection) Interacts with S.flexneri OspC1 and OspC3 (PubMed:35568036, PubMed:36624349). S.flexneri OspC1 and OspC3 interact specifically with the apo form of calmodulin and prevents calcium-binding (PubMed:35568036)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0DP25","intActId":"EBI-52319544"},"interactantTwo":{"uniProtKBAccession":"O00159","geneName":"MYO1C","intActId":"EBI-350423"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"value":"Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16760425"}],"value":"Cytoplasm, cytoskeleton, spindle","id":"SL-0251"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16760425"}],"value":"Cytoplasm, cytoskeleton, spindle pole","id":"SL-0448"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14654843"}],"value":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","id":"SL-0048"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Ubiquitination results in a strongly decreased activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Phosphorylation results in a decreased activity"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Ventricular tachycardia, catecholaminergic polymorphic, 6","diseaseAccession":"DI-05767","acronym":"CPVT6","description":"An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress. CPVT6 inheritance is autosomal dominant.","diseaseCrossReference":{"database":"MIM","id":"618782"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27516456"}]},"note":{"texts":[{"value":"The disease may be caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Long QT syndrome 16","diseaseAccession":"DI-05766","acronym":"LQT16","description":"An autosomal dominant form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. 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