CALM3_HUMAN
ID CALM3_HUMAN Reviewed; 149 AA.
AC P0DP25; P02593; P62158; P70667; P99014; Q13942; Q53S29; Q61379; Q61380;
AC Q96HK3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Calmodulin-3 {ECO:0000312|HGNC:HGNC:1449};
GN Name=CALM3 {ECO:0000312|HGNC:HGNC:1449};
GN Synonyms=CALML2, CAM3, CAMC, CAMIII;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3182832; DOI=10.1016/s0021-9258(18)37497-0;
RA Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A., Krebs J.,
RA Penniston J.T., Carafoli E., Strehler E.E.;
RT "Multiple divergent mRNAs code for a single human calmodulin.";
RL J. Biol. Chem. 263:17055-17062(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=2223880; DOI=10.1016/0167-4781(90)90203-e;
RA Koller M., Schnyder B., Strehler E.E.;
RT "Structural organization of the human CaMIII calmodulin gene.";
RL Biochim. Biophys. Acta 1087:180-189(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT
RP LYS-116.
RC TISSUE=Brain;
RX PubMed=7093203; DOI=10.1021/bi00539a041;
RA Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,
RA Titani K.;
RT "Complete amino acid sequence of human brain calmodulin.";
RL Biochemistry 21:2565-2569(1982).
RN [7]
RP PROTEIN SEQUENCE OF 2-31 AND 92-107, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Bensaad K., Vousden K.H.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 15-31; 77-107 AND 128-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP CALCIUM-BINDING SITES.
RX PubMed=1474585; DOI=10.1016/0022-2836(92)90324-d;
RA Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.;
RT "Calmodulin structure refined at 1.7 A resolution.";
RL J. Mol. Biol. 228:1177-1192(1992).
RN [10]
RP INTERACTION WITH TTN.
RX PubMed=9804419; DOI=10.1038/27603;
RA Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O.,
RA Wilmanns M., Gautel M.;
RT "Structural basis for activation of the titin kinase domain during
RT myofibrillogenesis.";
RL Nature 395:863-869(1998).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP INTERACTION WITH SRY.
RX PubMed=12871148; DOI=10.2174/0929866033479004;
RA Kelly S., Yotis J., Macris M., Harley V.;
RT "Recombinant expression, purification and characterisation of the HMG
RT domain of human SRY.";
RL Protein Pept. Lett. 10:281-286(2003).
RN [13]
RP INTERACTION WITH USP6.
RX PubMed=16127172; DOI=10.1074/jbc.m505220200;
RA Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.;
RT "Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific
RT protease TRE17/USP6.";
RL J. Biol. Chem. 280:35967-35973(2005).
RN [14]
RP INTERACTION WITH SRY.
RX PubMed=15746192; DOI=10.1210/me.2004-0334;
RA Sim H., Rimmer K., Kelly S., Ludbrook L.M., Clayton A.H., Harley V.R.;
RT "Defective calmodulin-mediated nuclear transport of the sex-determining
RT region of the Y chromosome (SRY) in XY sex reversal.";
RL Mol. Endocrinol. 19:1884-1892(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP FUNCTION, INTERACTION WITH CCP110, AND SUBCELLULAR LOCATION.
RX PubMed=16760425; DOI=10.1091/mbc.e06-04-0371;
RA Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z.,
RA Salisbury J.L., Sanchez I., Dynlacht B.D.;
RT "CP110 cooperates with two calcium-binding proteins to regulate cytokinesis
RT and genome stability.";
RL Mol. Biol. Cell 17:3423-3434(2006).
RN [17]
RP INTERACTION WITH CEP97 AND CCP110.
RX PubMed=17719545; DOI=10.1016/j.cell.2007.06.027;
RA Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.;
RT "Cep97 and CP110 suppress a cilia assembly program.";
RL Cell 130:678-690(2007).
RN [18]
RP INTERACTION WITH RYR1 AND RYR2.
RX PubMed=18650434; DOI=10.1074/jbc.m804432200;
RA Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
RA Weber D.J.;
RT "S100A1 and calmodulin compete for the same binding site on ryanodine
RT receptor.";
RL J. Biol. Chem. 283:26676-26683(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND TYR-139, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-95, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP INTERACTION WITH CDK5RAP2.
RX PubMed=20466722; DOI=10.1074/jbc.m110.105965;
RA Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.;
RT "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and
RT the Golgi complex.";
RL J. Biol. Chem. 285:22658-22665(2010).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP INTERACTION WITH ORAI1.
RX PubMed=23109337; DOI=10.1074/jbc.m112.380964;
RA Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y.,
RA London R.E., Birnbaumer L.;
RT "Crystal structure of calmodulin binding domain of orai1 in complex with
RT Ca2+ calmodulin displays a unique binding mode.";
RL J. Biol. Chem. 287:43030-43041(2012).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [28]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [32]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [34]
RP INTERACTION KCNQ2 AND KCNQ3.
RX PubMed=27564677; DOI=10.1021/acs.biochem.6b00477;
RA Strulovich R., Tobelaim W.S., Attali B., Hirsch J.A.;
RT "Structural insights into the M-channel proximal C-terminus/calmodulin
RT complex.";
RL Biochemistry 55:5353-5365(2016).
RN [35]
RP INTERACTION WITH PCP4, AND REGION.
RX PubMed=27876793; DOI=10.1038/ncomms13583;
RA Wang X., Putkey J.A.;
RT "PEP-19 modulates calcium binding to calmodulin by electrostatic
RT steering.";
RL Nat. Commun. 7:13583-13583(2016).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [37]
RP INVOLVEMENT IN LQT16, AND VARIANT LQT16 GLY-130.
RX PubMed=25460178; DOI=10.1016/j.hrthm.2014.10.035;
RA Reed G.J., Boczek N.J., Etheridge S.P., Ackerman M.J.;
RT "CALM3 mutation associated with long QT syndrome.";
RL Heart Rhythm 12:419-422(2015).
RN [38]
RP INVOLVEMENT IN CPVT6, VARIANT CPVT6 VAL-103, CHARACTERIZATION OF VARIANT
RP CPVT6 VAL-103, AND INTERACTION WITH RYR2.
RX PubMed=27516456; DOI=10.1161/circep.116.004161;
RA Gomez-Hurtado N., Boczek N.J., Kryshtal D.O., Johnson C.N., Sun J.,
RA Nitu F.R., Cornea R.L., Chazin W.J., Calvert M.L., Tester D.J.,
RA Ackerman M.J., Knollmann B.C.;
RT "Novel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A103V) Activates
RT Arrhythmogenic Ca Waves and Sparks.";
RL Circ. Arrhythm. Electrophysiol. 9:0-0(2016).
RN [39]
RP INVOLVEMENT IN LQT16, VARIANTS LQT16 GLY-130 AND LYS-141, CHARACTERIZATION
RP OF VARIANT LQT16 LYS-141, AND FUNCTION.
RX PubMed=31454269; DOI=10.1161/circgen.119.002581;
RA Wren L.M., Jimenez-Jaimez J., Al-Ghamdi S., Al-Aama J.Y., Bdeir A.,
RA Al-Hassnan Z.N., Kuan J.L., Foo R.Y., Potet F., Johnson C.N., Aziz M.C.,
RA Carvill G.L., Kaski J.P., Crotti L., Perin F., Monserrat L., Burridge P.W.,
RA Schwartz P.J., Chazin W.J., Bhuiyan Z.A., George A.L. Jr.;
RT "Genetic mosaicism in calmodulinopathy.";
RL Circ. Genom. Precis. Med. 12:375-385(2019).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels, aquaporins and other proteins through calcium-binding. Is
CC a regulator of voltage-dependent L-type calcium channels
CC (PubMed:31454269). Among the enzymes to be stimulated by the
CC calmodulin-calcium complex are a number of protein kinases and
CC phosphatases. Together with CCP110 and centrin, is involved in a
CC genetic pathway that regulates the centrosome cycle and progression
CC through cytokinesis. {ECO:0000250|UniProtKB:P0DP23,
CC ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:31454269}.
CC -!- SUBUNIT: Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By
CC similarity). Interacts with CEP97, CCP110, TTN/titin and SRY
CC (PubMed:9804419, PubMed:12871148, PubMed:15746192, PubMed:16760425,
CC PubMed:17719545). Interacts with USP6; the interaction is calcium
CC dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722).
CC Interacts with SCN5A (By similarity). Interacts with RYR1
CC (PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts
CC with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic
CC domains from two MIP subunits promotes MIP water channel closure (By
CC similarity). Interacts with ORAI1; this may play a role in the
CC regulation of ORAI1-mediated calcium transport (By similarity).
CC Interacts with IQCF1 (By similarity). Interacts with SYT7 (By
CC similarity). Interacts with CEACAM1 (via cytoplasmic domain); this
CC interaction is in a calcium dependent manner and reduces homophilic
CC cell adhesion through dissociation of dimer (By similarity). Interacts
CC with RYR2; regulates RYR2 calcium-release channel activity
CC (PubMed:27516456, PubMed:18650434). Interacts with PCP4; regulates
CC calmodulin calcium-binding (PubMed:27876793). Interacts with the
CC heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-
CC independent, constitutive and participates in the proper assembly of a
CC functional heterotetrameric M channel (PubMed:27564677).
CC {ECO:0000250|UniProtKB:P0DP23, ECO:0000250|UniProtKB:P62157,
CC ECO:0000250|UniProtKB:P62161, ECO:0000250|UniProtKB:P62204,
CC ECO:0000269|PubMed:12871148, ECO:0000269|PubMed:15746192,
CC ECO:0000269|PubMed:16127172, ECO:0000269|PubMed:16760425,
CC ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:18650434,
CC ECO:0000269|PubMed:20466722, ECO:0000269|PubMed:22484487,
CC ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:27516456,
CC ECO:0000269|PubMed:27564677, ECO:0000269|PubMed:27876793,
CC ECO:0000269|PubMed:9804419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:14654843}.
CC Note=Distributed throughout the cell during interphase, but during
CC mitosis becomes dramatically localized to the spindle poles and the
CC spindle microtubules.
CC -!- PTM: Ubiquitination results in a strongly decreased activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
CC -!- DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 6
CC (CPVT6) [MIM:618782]: An arrhythmogenic disorder characterized by
CC stress-induced, bidirectional ventricular tachycardia that may
CC degenerate into cardiac arrest and cause sudden death. Patients present
CC with recurrent syncope, seizures, or sudden death after physical
CC activity or emotional stress. CPVT6 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:27516456}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Long QT syndrome 16 (LQT16) [MIM:618782]: An autosomal
CC dominant form of long QT syndrome, a heart disorder characterized by a
CC prolonged QT interval on the ECG and polymorphic ventricular
CC arrhythmias. They cause syncope and sudden death in response to
CC exercise or emotional stress, and can present with a sentinel event of
CC sudden cardiac death in infancy. {ECO:0000269|PubMed:25460178,
CC ECO:0000269|PubMed:31454269}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000269|PubMed:1474585}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J04046; AAA51918.1; -; mRNA.
DR EMBL; X52606; CAA36839.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X52607; CAA36839.1; JOINED; Genomic_DNA.
DR EMBL; X52608; CAA36839.1; JOINED; Genomic_DNA.
DR EMBL; BT006855; AAP35501.1; -; mRNA.
DR EMBL; AC093503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005137; AAH05137.1; -; mRNA.
DR CCDS; CCDS33061.1; -.
DR CCDS; CCDS86782.1; -.
DR RefSeq; NP_001316851.1; NM_001329922.1.
DR RefSeq; NP_001316852.1; NM_001329923.1.
DR RefSeq; NP_001316853.1; NM_001329924.1.
DR RefSeq; NP_001316854.1; NM_001329925.1.
DR RefSeq; NP_001316855.1; NM_001329926.1.
DR RefSeq; NP_001734.1; NM_001743.5.
DR RefSeq; NP_005175.2; NM_005184.3.
DR RefSeq; NP_008819.1; NM_006888.4.
DR PDB; 5COC; X-ray; 2.67 A; A=7-78.
DR PDB; 5J03; X-ray; 2.00 A; B=1-149.
DR PDB; 6K67; X-ray; 1.95 A; B/D=9-81.
DR PDB; 7BYL; EM; 2.50 A; B/D/F/H=1-149.
DR PDB; 7BYM; EM; 3.10 A; B/D/F/H=1-149.
DR PDB; 7BYN; EM; 3.30 A; B/D/F/H=1-149.
DR PDB; 7CR3; EM; 3.60 A; C/E/F/H=1-149.
DR PDB; 7CR4; EM; 3.90 A; C/E/G/H=1-149.
DR PDB; 7CR7; EM; 3.70 A; C/E/F/H=1-149.
DR PDB; 7VNP; EM; 2.79 A; B/D/F/H=1-149.
DR PDB; 7VNQ; EM; 2.96 A; B/D/F/H=1-149.
DR PDB; 7VNR; EM; 2.80 A; B/D/F/H=1-149.
DR PDBsum; 5COC; -.
DR PDBsum; 5J03; -.
DR PDBsum; 6K67; -.
DR PDBsum; 7BYL; -.
DR PDBsum; 7BYM; -.
DR PDBsum; 7BYN; -.
DR PDBsum; 7CR3; -.
DR PDBsum; 7CR4; -.
DR PDBsum; 7CR7; -.
DR PDBsum; 7VNP; -.
DR PDBsum; 7VNQ; -.
DR PDBsum; 7VNR; -.
DR AlphaFoldDB; P0DP25; -.
DR SMR; P0DP25; -.
DR BindingDB; P0DP25; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugCentral; P0DP25; -.
DR GlyGen; P0DP25; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0DP25; -.
DR MetOSite; P0DP25; -.
DR BioMuta; CALM3; -.
DR EPD; P0DP25; -.
DR jPOST; P0DP25; -.
DR MassIVE; P0DP25; -.
DR PRIDE; P0DP25; -.
DR Antibodypedia; 39411; 188 antibodies from 17 providers.
DR DNASU; 801; -.
DR Ensembl; ENST00000291295.14; ENSP00000291295.8; ENSG00000160014.17.
DR Ensembl; ENST00000596362.1; ENSP00000472141.1; ENSG00000160014.17.
DR GeneID; 801; -.
DR GeneID; 805; -.
DR GeneID; 808; -.
DR KEGG; hsa:801; -.
DR KEGG; hsa:805; -.
DR KEGG; hsa:808; -.
DR MANE-Select; ENST00000272298.12; ENSP00000272298.7; NM_001743.6; NP_001734.1.
DR MANE-Select; ENST00000291295.14; ENSP00000291295.8; NM_005184.4; NP_005175.2.
DR MANE-Select; ENST00000356978.9; ENSP00000349467.4; NM_006888.6; NP_008819.1.
DR CTD; 801; -.
DR CTD; 805; -.
DR CTD; 808; -.
DR DisGeNET; 801; -.
DR DisGeNET; 805; -.
DR DisGeNET; 808; -.
DR GeneCards; CALM3; -.
DR HGNC; HGNC:1449; CALM3.
DR HPA; ENSG00000160014; Tissue enhanced (brain).
DR MalaCards; CALM3; -.
DR MIM; 114183; gene.
DR MIM; 618782; phenotype.
DR neXtProt; NX_P0DP25; -.
DR OpenTargets; ENSG00000143933; -.
DR OpenTargets; ENSG00000160014; -.
DR OpenTargets; ENSG00000198668; -.
DR Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia.
DR Orphanet; 101016; Romano-Ward syndrome.
DR VEuPathDB; HostDB:ENSG00000160014; -.
DR GeneTree; ENSGT00950000182980; -.
DR OMA; HQIEFDE; -.
DR OrthoDB; 1386217at2759; -.
DR PathwayCommons; P0DP25; -.
DR SignaLink; P0DP25; -.
DR SIGNOR; P0DP25; -.
DR BioGRID-ORCS; 801; 10 hits in 1080 CRISPR screens.
DR BioGRID-ORCS; 805; 35 hits in 960 CRISPR screens.
DR BioGRID-ORCS; 808; 45 hits in 1080 CRISPR screens.
DR ChiTaRS; CALM3; human.
DR Pharos; P0DP25; Tclin.
DR PRO; PR:P0DP25; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P0DP25; protein.
DR Bgee; ENSG00000160014; Expressed in prefrontal cortex and 209 other tissues.
DR ExpressionAtlas; P0DP25; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
DR GO; GO:1902494; C:catalytic complex; IDA:CAFA.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0030017; C:sarcomere; IDA:BHF-UCL.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0010856; F:adenylate cyclase activator activity; IDA:UniProtKB.
DR GO; GO:0008179; F:adenylate cyclase binding; IPI:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0031997; F:N-terminal myristoylation domain binding; IPI:UniProtKB.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0072542; F:protein phosphatase activator activity; IDA:BHF-UCL.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; TAS:BHF-UCL.
DR GO; GO:0031432; F:titin binding; IPI:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0005513; P:detection of calcium ion; IMP:BHF-UCL.
DR GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; IEA:Ensembl.
DR GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IDA:BHF-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; TAS:BHF-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; TAS:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IMP:UniProtKB.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Isopeptide bond;
KW Long QT syndrome; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..149
FT /note="Calmodulin-3"
FT /id="PRO_0000439934"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 77..149
FT /note="Necessary and sufficient for interaction with PCP4"
FT /evidence="ECO:0000269|PubMed:27876793"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:1474585"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 22
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 45
FT /note="Phosphothreonine; by CaMK4"
FT /evidence="ECO:0000250|UniProtKB:P0DP31"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 100
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:7093203,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 116
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62157"
FT VARIANT 103
FT /note="A -> V (in CPVT6; decreased calcium-binding
FT affinity; not changed binding to RYR2; increased RYR2
FT calcium-release channel activity; decreased calcium-
FT dependent inactivation of L-type calcium channel; not
FT changed action potential duration)"
FT /evidence="ECO:0000269|PubMed:27516456"
FT /id="VAR_078261"
FT VARIANT 130
FT /note="D -> G (in LQT16)"
FT /evidence="ECO:0000269|PubMed:25460178,
FT ECO:0000269|PubMed:31454269"
FT /id="VAR_083815"
FT VARIANT 141
FT /note="E -> K (in LQT16; loss-of-function variant causing
FT impaired negative regulation of high voltage-gated calcium
FT channel activity; impaired regulation of cardiac muscle
FT cell action potential; decreased calcium ion binding)"
FT /evidence="ECO:0000269|PubMed:31454269"
FT /id="VAR_083816"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:6K67"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7BYL"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:6K67"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:6K67"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6K67"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:6K67"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:7BYL"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:7BYL"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:7BYL"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:7BYL"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:7BYL"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:7BYL"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:7BYL"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
