ID CALM_BOVIN Reviewed; 149 AA. AC P62157; P02593; P70667; P99014; Q08D84; Q2KJE6; Q61379; Q61380; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 196. DE RecName: Full=Calmodulin; DE Short=CaM; GN Name=CALM; Synonyms=CAM; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12658628; DOI=10.1002/mrd.10292; RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., RA Izaike Y., Todoroki J., Hashizume K.; RT "Characterization of gene expression profiles in early bovine pregnancy RT using a custom cDNA microarray."; RL Mol. Reprod. Dev. 65:9-18(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus, and Hereford; RC TISSUE=Fetal pons, Ileum, and Uterus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-149. RC TISSUE=Uterus; RA Grand R.J.A., Perry S.V.; RT "The amino acid sequence of the troponin C-like protein (modulator protein) RT from bovine uterus."; RL FEBS Lett. 92:137-142(1978). RN [4] RP PROTEIN SEQUENCE OF 2-149. RC TISSUE=Brain; RA Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T.; RT "Determination of the complete amino acid sequence of calmodulin RT (phenylalanine-rich acidic protein II) from bovine brain."; RL Biomed. Res. 1:248-264(1980). RN [5] RP PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT RP LYS-116. RC TISSUE=Brain; RX PubMed=7356670; DOI=10.1016/s0021-9258(19)86127-6; RA Watterson D.M., Sharief F., Vanaman T.C.; RT "The complete amino acid sequence of the Ca2+-dependent modulator protein RT (calmodulin) of bovine brain."; RL J. Biol. Chem. 255:962-975(1980). RN [6] RP PROTEIN SEQUENCE OF 2-28, AND UBIQUITINATION AT LYS-22. RX PubMed=9716384; DOI=10.1046/j.1432-1327.1998.2550422.x; RA Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E., Jennissen H.P.; RT "Modulation of calmodulin function by ubiquitin-calmodulin ligase and RT identification of the responsible ubiquitylation site in vertebrate RT calmodulin."; RL Eur. J. Biochem. 255:422-431(1998). RN [7] RP RETRACTED PAPER. RX PubMed=3058479; DOI=10.1111/j.1432-1033.1988.tb14420.x; RA Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W., Tripier D., RA Hucho F.; RT "Heat-resistant inhibitors of protein kinase C from bovine brain."; RL Eur. J. Biochem. 177:657-664(1988). RN [8] RP RETRACTION NOTICE OF PUBMED:3058479. RX PubMed=2180696; DOI=10.1111/j.1432-1033.1990.tb15390.x; RA Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W., Tripier D., RA Hucho F.; RL Eur. J. Biochem. 188:204-204(1990). RN [9] RP METHYLATION AT LYS-116. RA Weise C.; RL Unpublished observations (OCT-2002). RN [10] RP INTERACTION WITH MYO1C. RX PubMed=8022785; DOI=10.1073/pnas.91.14.6349; RA Reizes O., Barylko B., Li C., Suedhof T.C., Albenisi J.P.; RT "Domain Structure of a mammalian myosin I-beta."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6349-6353(1994). RN [11] RP INTERACTION WITH MYO10. RX PubMed=11457842; DOI=10.1074/jbc.m104785200; RA Homma K., Saito J., Ikebe R., Ikebe M.; RT "Motor function and regulation of myosin X."; RL J. Biol. Chem. 276:34348-34354(2001). RN [12] RP 3D-STRUCTURE MODELING OF TRIMETHYLATED CALMODULIN. RX PubMed=3375233; DOI=10.1002/prot.340030102; RA Strynadka N.C.J., James M.N.G.; RT "Two trifluoperazine-binding sites on calmodulin predicted from comparative RT molecular modeling with troponin-C."; RL Proteins 3:1-17(1988). RN [13] RP STRUCTURE BY NMR OF 1-75. RX PubMed=9305950; DOI=10.1021/bi971022+; RA Bentrop D., Bertini I., Cremonini M.A., Forsen S., Luchinat C., RA Malmendal A.; RT "Solution structure of the paramagnetic complex of the N-terminal domain of RT calmodulin with two Ce3+ ions by 1H NMR."; RL Biochemistry 36:11605-11618(1997). RN [14] RP STRUCTURE BY NMR OF 77-149. RX PubMed=8262263; DOI=10.1016/0014-5793(93)80839-m; RA Finn B.E., Drakenberg T., Forsen S.; RT "The structure of apo-calmodulin. A 1H NMR examination of the carboxy- RT terminal domain."; RL FEBS Lett. 336:368-374(1993). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=1519061; DOI=10.1126/science.1519061; RA Meador W.E., Means A.R., Quiocho F.A.; RT "Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin- RT peptide complex."; RL Science 257:1251-1255(1992). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-148. RX PubMed=8259515; DOI=10.1126/science.8259515; RA Meador W.E., Means A.R., Quiocho F.A.; RT "Modulation of calmodulin plasticity in molecular recognition on the basis RT of X-ray structures."; RL Science 262:1718-1721(1993). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 6-148 GLU-85 DEL. RX PubMed=8341712; DOI=10.1073/pnas.90.14.6869; RA Raghunathan S., Chandross R.J., Cheng B.P., Persechini A., Sobottka S.E., RA Kretsinger R.H.; RT "The linker of des-Glu84-calmodulin is bent."; RL Proc. Natl. Acad. Sci. U.S.A. 90:6869-6873(1993). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). RX PubMed=7803388; DOI=10.1021/bi00255a006; RA Cook W.J., Walter L.J., Walter M.R.; RT "Drug binding by calmodulin: crystal structure of a calmodulin- RT trifluoperazine complex."; RL Biochemistry 33:15259-15265(1994). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-149. RX PubMed=7634090; DOI=10.1038/nsb1194-795; RA Vandonselaar M., Hickie R.A., Quail J.W., Delbaere L.T.; RT "Trifluoperazine-induced conformational change in Ca(2+)-calmodulin."; RL Nat. Struct. Biol. 1:795-801(1994). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-147. RX PubMed=9438860; DOI=10.1016/s0969-2126(97)00308-0; RA Wall M.E., Clarage J.B., Phillips G.N.; RT "Motions of calmodulin characterized using both Bragg and diffuse X-ray RT scattering."; RL Structure 5:1599-1612(1997). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 79-149. RX PubMed=11320306; DOI=10.1107/s090744490100347x; RA Olsson L.L., Sjolin L.; RT "Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A RT resolution."; RL Acta Crystallogr. D 57:664-669(2001). CC -!- FUNCTION: Calmodulin acts as part of a calcium signal transduction CC pathway by mediating the control of a large number of enzymes, ion CC channels, aquaporins and other proteins through calcium-binding. CC Calcium-binding is required for the activation of calmodulin. Among the CC enzymes to be stimulated by the calmodulin-calcium complex are a number CC of protein kinases, such as myosin light-chain kinases and calmodulin- CC dependent protein kinase type II (CaMK2), and phosphatases. Together CC with CCP110 and centrin, is involved in a genetic pathway that CC regulates the centrosome cycle and progression through cytokinesis. Is CC a regulator of voltage-dependent L-type calcium channels. Mediates CC calcium-dependent inactivation of CACNA1C. Positively regulates CC calcium-activated potassium channel activity of KCNN2. Forms a CC potassium channel complex with KCNQ1 and regulates electrophysiological CC activity of the channel via calcium-binding. Acts as a sensor to CC modulate the endoplasmic reticulum contacts with other organelles CC mediated by VMP1:ATP2A2. {ECO:0000250|UniProtKB:P0DP23}. CC -!- SUBUNIT: Interacts with CEP97, CCP110, TTN/titin and SRY. Interacts CC with MYO5A and RRAD (By similarity). Interacts with USP6; the CC interaction is calcium dependent (By similarity). Interacts with CC CDK5RAP2. Interacts with SCN5A. Interacts with RYR1 and RYR2 (By CC similarity). Interacts with FCHO1. Interacts with MIP in a 1:2 CC stoichiometry; the interaction with the cytoplasmic domains from two CC MIP subunits promotes MIP water channel closure. Interacts with ORAI1; CC this may play a role in the regulation of ORAI1-mediated calcium CC transport. Interacts with SYT7 (By similarity). Interacts with MYO10 CC and MYO1C (PubMed:11457842, PubMed:8022785). Interacts with SLC9A1 in a CC calcium-dependent manner (By similarity). Interacts with HINT1; CC interaction increases in the presence of calcium ions (By similarity). CC Interacts with HINT3 (By similarity). Interacts with SLC26A5 (via STAS CC domain); this interaction is calcium-dependent and the STAS domain CC interacts with only one lobe of CALM which is an elongated conformation CC (By similarity). {ECO:0000250|UniProtKB:P0DP23, CC ECO:0000250|UniProtKB:P0DP26, ECO:0000250|UniProtKB:P62158, CC ECO:0000250|UniProtKB:P62204, ECO:0000269|PubMed:11457842, CC ECO:0000269|PubMed:8022785}. CC -!- INTERACTION: CC P62157; Q9LF79: ACA8; Xeno; NbExp=14; IntAct=EBI-397403, EBI-980643; CC P62157; Q8L517: At4g30490; Xeno; NbExp=4; IntAct=EBI-397403, EBI-4439046; CC P62157; Q14451: GRB7; Xeno; NbExp=2; IntAct=EBI-397403, EBI-970191; CC P62157; P23711: Hmox2; Xeno; NbExp=3; IntAct=EBI-397403, EBI-2910092; CC P62157; P02788: LTF; Xeno; NbExp=2; IntAct=EBI-397403, EBI-1058602; CC P62157; P29476: Nos1; Xeno; NbExp=2; IntAct=EBI-397403, EBI-349460; CC P62157; Q62600: Nos3; Xeno; NbExp=2; IntAct=EBI-397403, EBI-7052018; CC P62157; Q96PH1-4: NOX5; Xeno; NbExp=3; IntAct=EBI-397403, EBI-7305642; CC P62157; P48436: SOX9; Xeno; NbExp=7; IntAct=EBI-397403, EBI-3920028; CC P62157; Q13586: STIM1; Xeno; NbExp=2; IntAct=EBI-397403, EBI-448878; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle. CC Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the CC cell during interphase, but during mitosis becomes dramatically CC localized to the spindle poles and the spindle microtubules. CC {ECO:0000250}. CC -!- PTM: Ubiquitination results in a strongly decreased activity. CC {ECO:0000269|PubMed:9716384}. CC -!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites. CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB099053; BAC56543.1; -; mRNA. DR EMBL; BC105380; AAI05381.1; -; mRNA. DR EMBL; BC120080; AAI20081.1; -; mRNA. DR EMBL; BC123890; AAI23891.1; -; mRNA. DR PIR; A90719; MCBO. DR RefSeq; NP_001039714.1; NM_001046249.2. DR RefSeq; NP_001229501.1; NM_001242572.1. DR RefSeq; NP_001229516.1; NM_001242587.1. DR PDB; 1A29; X-ray; 2.74 A; A=2-149. DR PDB; 1AK8; NMR; -; A=1-76. DR PDB; 1CDM; X-ray; 2.00 A; A=5-148. DR PDB; 1CM1; X-ray; 2.00 A; A=2-149. DR PDB; 1CM4; X-ray; 2.00 A; A=2-149. DR PDB; 1CMF; NMR; -; A=77-149. DR PDB; 1CMG; NMR; -; A=77-149. DR PDB; 1DEG; X-ray; 2.90 A; A=6-148. DR PDB; 1FW4; X-ray; 1.70 A; A=79-149. DR PDB; 1LIN; X-ray; 2.00 A; A=2-149. DR PDB; 1PRW; X-ray; 1.70 A; A=2-149. DR PDB; 1QIV; X-ray; 2.64 A; A=2-149. DR PDB; 1QIW; X-ray; 2.30 A; A/B=2-149. DR PDB; 1XA5; X-ray; 2.12 A; A=2-149. DR PDB; 2F2O; X-ray; 2.17 A; A/B=1-149. DR PDB; 2F2P; X-ray; 2.60 A; A/B=1-149. DR PDB; 2FOT; X-ray; 2.45 A; A=2-149. DR PDB; 3IF7; X-ray; 1.60 A; A=2-149. DR PDB; 6O20; EM; 3.30 A; F=1-149. DR PDBsum; 1A29; -. DR PDBsum; 1AK8; -. DR PDBsum; 1CDM; -. DR PDBsum; 1CM1; -. DR PDBsum; 1CM4; -. DR PDBsum; 1CMF; -. DR PDBsum; 1CMG; -. DR PDBsum; 1DEG; -. DR PDBsum; 1FW4; -. DR PDBsum; 1LIN; -. DR PDBsum; 1PRW; -. DR PDBsum; 1QIV; -. DR PDBsum; 1QIW; -. DR PDBsum; 1XA5; -. DR PDBsum; 2F2O; -. DR PDBsum; 2F2P; -. DR PDBsum; 2FOT; -. DR PDBsum; 3IF7; -. DR PDBsum; 6O20; -. DR AlphaFoldDB; P62157; -. DR EMDB; EMD-0607; -. DR EMDB; EMD-16311; -. DR PCDDB; P62157; -. DR SMR; P62157; -. DR BioGRID; 176895; 1. DR BioGRID; 544691; 9. DR DIP; DIP-36674N; -. DR ELM; P62157; -. DR IntAct; P62157; 107. DR MINT; P62157; -. DR STRING; 9913.ENSBTAP00000074130; -. DR BindingDB; P62157; -. DR ChEMBL; CHEMBL6092; -. DR iPTMnet; P62157; -. DR MetOSite; P62157; -. DR PaxDb; 9913-ENSBTAP00000019411; -. DR PeptideAtlas; P62157; -. DR Ensembl; ENSBTAT00000002055.6; ENSBTAP00000002055.6; ENSBTAG00000001575.6. DR Ensembl; ENSBTAT00000082279.1; ENSBTAP00000057928.1; ENSBTAG00000014583.4. DR Ensembl; ENSBTAT00000083507.1; ENSBTAP00000058610.1; ENSBTAG00000025644.5. DR GeneID; 100297344; -. DR GeneID; 520277; -. DR GeneID; 617095; -. DR KEGG; bta:100297344; -. DR KEGG; bta:520277; -. DR KEGG; bta:617095; -. DR CTD; 801; -. DR CTD; 805; -. DR CTD; 808; -. DR VEuPathDB; HostDB:ENSBTAG00000001575; -. DR VEuPathDB; HostDB:ENSBTAG00000014583; -. DR VEuPathDB; HostDB:ENSBTAG00000025644; -. DR eggNOG; KOG0027; Eukaryota. DR GeneTree; ENSGT00950000182980; -. DR HOGENOM; CLU_061288_2_0_1; -. DR InParanoid; P62157; -. DR OMA; SCDRHPP; -. DR OrthoDB; 22601at2759; -. DR TreeFam; TF300912; -. DR EvolutionaryTrace; P62157; -. DR PRO; PR:P62157; -. DR Proteomes; UP000009136; Chromosome 10. DR Proteomes; UP000009136; Chromosome 11. DR Proteomes; UP000009136; Chromosome 18. DR Bgee; ENSBTAG00000001575; Expressed in oocyte and 105 other cell types or tissues. DR ExpressionAtlas; P62157; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL. DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL. DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL. DR CDD; cd00051; EFh; 2. DR Gene3D; 1.10.238.10; EF-hand; 3. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR23050:SF552; AT10229P-RELATED; 1. DR PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1. DR Pfam; PF13499; EF-hand_7; 2. DR PRINTS; PR00450; RECOVERIN. DR SMART; SM00054; EFh; 4. DR SUPFAM; SSF47473; EF-hand; 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; Isopeptide bond; Metal-binding; Methylation; KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7356670, FT ECO:0000269|PubMed:9716384, ECO:0000269|Ref.3, FT ECO:0000269|Ref.4" FT CHAIN 2..149 FT /note="Calmodulin" FT /id="PRO_0000198222" 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 BINDING 21 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 25 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 32 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 59 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 105 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 132 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 136 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:7356670" FT MOD_RES 22 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT MOD_RES 45 FT /note="Phosphothreonine; by CaMK4" FT /evidence="ECO:0000250|UniProtKB:P0DP29" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT MOD_RES 95 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT MOD_RES 100 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT MOD_RES 111 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT MOD_RES 116 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:7356670, ECO:0000269|Ref.9" FT MOD_RES 116 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT MOD_RES 139 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P0DP23" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:9716384" FT HELIX 7..20 FT /evidence="ECO:0007829|PDB:3IF7" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:1CM4" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:3IF7" FT HELIX 30..39 FT /evidence="ECO:0007829|PDB:3IF7" FT HELIX 46..56 FT /evidence="ECO:0007829|PDB:3IF7" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:3IF7" FT HELIX 66..75 FT /evidence="ECO:0007829|PDB:3IF7" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:1QIW" FT HELIX 83..93 FT /evidence="ECO:0007829|PDB:3IF7" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:3IF7" FT HELIX 103..112 FT /evidence="ECO:0007829|PDB:3IF7" FT HELIX 119..129 FT /evidence="ECO:0007829|PDB:3IF7" FT STRAND 131..138 FT /evidence="ECO:0007829|PDB:3IF7" FT HELIX 139..146 FT /evidence="ECO:0007829|PDB:3IF7" SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64; MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK //