UniProt functional annotation for P0DP26



	UniProt functional annotation for P0DP26

UniProt codes: P0DP26, P02593.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endomplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity). {ECO:0000250|UniProtKB:P0DP23}.

Subunit: Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD (By similarity). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2. Interacts with SCN5A (By similarity). Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A (PubMed:17151196). Interacts with IQCF1 (PubMed:25380116). Interacts with SYT7 (PubMed:24569478). 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). Interacts with PCP4; regulates calmodulin calcium- binding (By similarity). 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 (By similarity). Interacts with alpha-synuclein/SNCA (By similarity). Interacts with SLC9A1 in a calcium-dependent manner (By similarity). In the absence of Ca(+2), interacts with GIMAP4 (via IQ domain) (PubMed:16569770). Interacts with SCN8A; the interaction modulates the inactivation rate of SCN8A (PubMed:23942337). Interaction with KIF1A; the interaction is increased in presence of calcium and increases neuronal dense core vesicles motility (By similarity). Interacts with KCNN3 (By similarity). Interacts with KCNQ1 (via C- terminus); forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner (By similarity). Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P0DP23, ECO:0000250|UniProtKB:P62161, ECO:0000269|PubMed:16569770, ECO:0000269|PubMed:17151196, ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:23942337, ECO:0000269|PubMed:24569478, ECO:0000269|PubMed:25380116}.

Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DP23}. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250|UniProtKB:P0DP23}.

Domain: The N-terminal and C-terminal lobes of CALM bind to the C- terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C- terminus to KCNQ1 is calcium-independent but is essential for assembly of the structure. Binding of CALM N-terminus to KCNQ1 is calcium- dependent and regulates electrophysiological activity of the channel. {ECO:0000250|UniProtKB:P0DP23}.

Ptm: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.

Ptm: Phosphorylation results in a decreased activity. {ECO:0000250}.

Miscellaneous: This protein has four functional calcium-binding sites. {ECO:0000250|UniProtKB:P0DP23}.

Similarity: Belongs to the calmodulin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endomplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity). {ECO:0000250\|UniProtKB:P0DP23}.


Subunit:		Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD (By similarity). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2. Interacts with SCN5A (By similarity). Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A (PubMed:17151196). Interacts with IQCF1 (PubMed:25380116). Interacts with SYT7 (PubMed:24569478). 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). Interacts with PCP4; regulates calmodulin calcium- binding (By similarity). 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 (By similarity). Interacts with alpha-synuclein/SNCA (By similarity). Interacts with SLC9A1 in a calcium-dependent manner (By similarity). In the absence of Ca(+2), interacts with GIMAP4 (via IQ domain) (PubMed:16569770). Interacts with SCN8A; the interaction modulates the inactivation rate of SCN8A (PubMed:23942337). Interaction with KIF1A; the interaction is increased in presence of calcium and increases neuronal dense core vesicles motility (By similarity). Interacts with KCNN3 (By similarity). Interacts with KCNQ1 (via C- terminus); forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner (By similarity). Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity (By similarity). {ECO:0000250, ECO:0000250\|UniProtKB:P0DP23, ECO:0000250\|UniProtKB:P62161, ECO:0000269\|PubMed:16569770, ECO:0000269\|PubMed:17151196, ECO:0000269\|PubMed:18650434, ECO:0000269\|PubMed:23942337, ECO:0000269\|PubMed:24569478, ECO:0000269\|PubMed:25380116}.
Subcellular location:		Cytoplasm, cytoskeleton, spindle {ECO:0000250\|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250\|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250\|UniProtKB:P0DP23}. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250\|UniProtKB:P0DP23}.
Domain:		The N-terminal and C-terminal lobes of CALM bind to the C- terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C- terminus to KCNQ1 is calcium-independent but is essential for assembly of the structure. Binding of CALM N-terminus to KCNQ1 is calcium- dependent and regulates electrophysiological activity of the channel. {ECO:0000250\|UniProtKB:P0DP23}.
Ptm:		Ubiquitination results in a strongly decreased activity. {ECO:0000250}.
Ptm:		Phosphorylation results in a decreased activity. {ECO:0000250}.
Miscellaneous:		This protein has four functional calcium-binding sites. {ECO:0000250\|UniProtKB:P0DP23}.
Similarity:		Belongs to the calmodulin family. {ECO:0000305}.