CALM_PARTE
ID CALM_PARTE Reviewed; 149 AA.
AC P07463; A0DD49;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=CAM; ORFNames=GSPATT00015825001;
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2163766; DOI=10.1016/0092-8674(90)90250-i;
RA Kink J.A., Maley M.E., Preston R.R., Ling K.Y., Wallen-Friedman M.A.,
RA Saimi Y., Kung C.;
RT "Mutations in paramecium calmodulin indicate functional differences between
RT the C-terminal and N-terminal lobes in vivo.";
RL Cell 62:165-174(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2;
RX PubMed=17086204; DOI=10.1038/nature05230;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [3]
RP PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-14
RP AND LYS-116.
RX PubMed=3100523; DOI=10.1016/s0021-9258(19)75744-5;
RA Schaefer W.H., Lukas T.J., Blair I.A., Schultz J.E., Watterson D.M.;
RT "Amino acid sequence of a novel calmodulin from Paramecium tetraurelia that
RT contains dimethyllysine in the first domain.";
RL J. Biol. Chem. 262:1025-1029(1987).
RN [4]
RP MUTAGENESIS OF SER-102.
RX PubMed=2438688; DOI=10.1073/pnas.84.11.3931;
RA Schaefer W.H., Hinrichsen R.D., Burgess-Cassler A., Kung C., Blair I.A.,
RA Watterson D.M.;
RT "A mutant Paramecium with a defective calcium-dependent potassium
RT conductance has an altered calmodulin: a nonlethal selective alteration in
RT calmodulin regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3931-3935(1987).
RN [5]
RP MUTAGENESIS OF ILE-137.
RX PubMed=2477839; DOI=10.1073/pnas.86.19.7331;
RA Lukas T.J., Wallen-Friedman M., Kung C., Watterson D.M.;
RT "In vivo mutations of calmodulin: a mutant Paramecium with altered ion
RT current regulation has an isoleucine-to-threonine change at residue 136 and
RT an altered methylation state at lysine residue 115.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7331-7335(1989).
RN [6]
RP MUTAGENESIS OF ASP-51.
RX PubMed=1315966; DOI=10.1002/prot.340120408;
RA Ling K.-Y., Preston R.R., Burns R., Kink J.A., Saimi Y., Kung C.;
RT "Primary mutations in calmodulin prevent activation of the Ca(2+)-dependent
RT Na+ channel in Paramecium.";
RL Proteins 12:365-371(1992).
RN [7]
RP MUTAGENESIS OF VAL-36; GLY-41; ASP-51; GLU-55; GLY-60; ASP-96; ALA-103;
RP GLU-105; HIS-136 AND MET-146.
RX PubMed=8020480; DOI=10.1111/j.1432-1033.1994.tb18882.x;
RA Ling K.-Y., Maley M.E., Preston R.R., Saimi Y., Kung C.;
RT "New non-lethal calmodulin mutations in Paramecium. A structural and
RT functional bipartition hypothesis.";
RL Eur. J. Biochem. 222:433-439(1994).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8453381; DOI=10.1002/pro.5560020316;
RA Rao S.T., Wu S., Satyshur K.A., Ling K.-Y., Kung C., Sundaralingam M.;
RT "Structure of Paramecium tetraurelia calmodulin at 1.8-A resolution.";
RL Protein Sci. 2:436-447(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
RX PubMed=15299476; DOI=10.1107/s0907444993007991;
RA Ban C., Ramakrishnan B., Ling K.-Y., Kung C., Sundaralingam M.;
RT "Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68-A
RT resolution.";
RL Acta Crystallogr. D 50:50-63(1994).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+). Among the enzymes to be
CC stimulated by the calmodulin-Ca(2+) complex are a number of protein
CC kinases and phosphatases.
CC -!- INTERACTION:
CC P07463; P04775: Scn2a; Xeno; NbExp=2; IntAct=EBI-15916571, EBI-2619448;
CC -!- PTM: The pantophobiac mutant CAM2 is undermethylated on Lys-116.
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; M34540; AAA29443.1; -; Genomic_DNA.
DR EMBL; S68025; AAB20487.1; -; Genomic_DNA.
DR EMBL; CT868385; CAK80966.1; -; Genomic_DNA.
DR PIR; A35603; MCPP.
DR RefSeq; XP_001448363.1; XM_001448326.1.
DR PDB; 1CLM; X-ray; 1.80 A; A=2-149.
DR PDB; 1EXR; X-ray; 1.00 A; A=2-149.
DR PDB; 1N0Y; X-ray; 1.75 A; A/B=2-149.
DR PDB; 1OSA; X-ray; 1.68 A; A=2-149.
DR PDB; 2KXW; NMR; -; A=77-149.
DR PDB; 2M5E; NMR; -; A=77-149.
DR PDB; 5E1K; X-ray; 1.00 A; A=2-149.
DR PDB; 5E1N; X-ray; 1.00 A; A=2-149.
DR PDB; 5E1P; X-ray; 1.01 A; A=2-149.
DR PDBsum; 1CLM; -.
DR PDBsum; 1EXR; -.
DR PDBsum; 1N0Y; -.
DR PDBsum; 1OSA; -.
DR PDBsum; 2KXW; -.
DR PDBsum; 2M5E; -.
DR PDBsum; 5E1K; -.
DR PDBsum; 5E1N; -.
DR PDBsum; 5E1P; -.
DR AlphaFoldDB; P07463; -.
DR BMRB; P07463; -.
DR SMR; P07463; -.
DR DIP; DIP-59128N; -.
DR ELM; P07463; -.
DR IntAct; P07463; 1.
DR STRING; 5888.CAK80966; -.
DR iPTMnet; P07463; -.
DR EnsemblProtists; CAK80966; CAK80966; GSPATT00015825001.
DR GeneID; 5034148; -.
DR KEGG; ptm:GSPATT00015825001; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P07463; -.
DR OMA; SCDRHPP; -.
DR EvolutionaryTrace; P07463; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR039030; Calmodulin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050:SF401; PTHR23050:SF401; 1.
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; Direct protein sequencing;
KW Metal-binding; Methylation; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3100523"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198261"
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 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:3100523"
FT MOD_RES 14
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:3100523"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:3100523"
FT MUTAGEN 36
FT /note="V->I: In CAM13."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 41
FT /note="G->E: In CAM12."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 51
FT /note="D->G: In CAM15."
FT /evidence="ECO:0000269|PubMed:1315966,
FT ECO:0000269|PubMed:8020480"
FT MUTAGEN 51
FT /note="D->N: In CAM12; lacks the Ca(2+)-dependent K(+)
FT current."
FT /evidence="ECO:0000269|PubMed:1315966,
FT ECO:0000269|PubMed:8020480"
FT MUTAGEN 55
FT /note="E->K: In CAM11."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 60
FT /note="G->S: In CAM14."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 96
FT /note="D->G: In CAM5."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 102
FT /note="S->F: In CAM1 (also named PNTA1); lacks the Ca(2+)-
FT dependent K(+) current."
FT /evidence="ECO:0000269|PubMed:2438688"
FT MUTAGEN 103
FT /note="A->V: In CAM6."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 105
FT /note="E->K: In CAM4."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 136
FT /note="H->R: In CAM7."
FT /evidence="ECO:0000269|PubMed:8020480"
FT MUTAGEN 137
FT /note="I->T: In CAM2 (also named PNTA2)."
FT /evidence="ECO:0000269|PubMed:2477839"
FT MUTAGEN 146
FT /note="M->V: In CAM3."
FT /evidence="ECO:0000269|PubMed:8020480"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:1EXR"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1EXR"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1EXR"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1EXR"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1EXR"
FT HELIX 66..93
FT /evidence="ECO:0007829|PDB:1EXR"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5E1K"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1EXR"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2KXW"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1EXR"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1EXR"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:1EXR"
SQ SEQUENCE 149 AA; 16803 MW; CDE9230226C3BAB0 CRC64;
MAEQLTEEQI AEFKEAFALF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL SLMARKMKEQ DSEEELIEAF KVFDRDGNGL ISAAELRHVM TNLGEKLTDD
EVDEMIREAD IDGDGHINYE EFVRMMVSK
