CALM_BOVIN
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 03-AUG-2022, entry version 187.
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 mediates the control of a large number of enzymes,
CC ion channels, aquaporins and other proteins by Ca(2+). Among the
CC enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number
CC of protein kinases and phosphatases. Together with CCP110 and centrin,
CC is involved in a genetic pathway that regulates the centrosome cycle
CC and progression through cytokinesis (By similarity). {ECO:0000250}.
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). {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}.
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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 PCDDB; P62157; -.
DR SMR; P62157; -.
DR BioGRID; 176895; 1.
DR BioGRID; 544691; 8.
DR DIP; DIP-36674N; -.
DR ELM; P62157; -.
DR IntAct; P62157; 107.
DR MINT; P62157; -.
DR BindingDB; P62157; -.
DR ChEMBL; CHEMBL6092; -.
DR iPTMnet; P62157; -.
DR MetOSite; P62157; -.
DR PaxDb; P62157; -.
DR PeptideAtlas; P62157; -.
DR PRIDE; P62157; -.
DR Ensembl; ENSBTAT00000002055; ENSBTAP00000002055; ENSBTAG00000001575.
DR Ensembl; ENSBTAT00000082279; ENSBTAP00000057928; ENSBTAG00000014583.
DR Ensembl; ENSBTAT00000083507; ENSBTAP00000058610; ENSBTAG00000025644.
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; 1386217at2759; -.
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 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:0030234; F:enzyme regulator activity; IBA:GO_Central.
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 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; 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
