ID CALM1_XENLA Reviewed; 149 AA.
AC P0DP33; P02593; P0DP40; P62155; P70667; P99014; Q61379; Q61380; Q6INP3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Calmodulin-1 {ECO:0000250|UniProtKB:P0DP23};
GN Name=calm1 {ECO:0000250|UniProtKB:P0DP23};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=7552748; DOI=10.1038/nsb0995-768;
RA Kuboniwa H., Tjandra N., Grzesiek S., Ren H., Klee C.B., Bax A.;
RT "Solution structure of calcium-free calmodulin.";
RL Nat. Struct. Biol. 2:768-776(1995).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=7552747; DOI=10.1038/nsb0995-758;
RA Zhang M., Tanaka T., Ikura M.;
RT "Calcium-induced conformational transition revealed by the solution
RT structure of apo calmodulin.";
RL Nat. Struct. Biol. 2:758-767(1995).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=9514729; DOI=10.1006/jmbi.1997.1524;
RA Osawa M., Swindells M.B., Tanikawa J., Tanaka T., Mase T., Furuya T.,
RA Ikura M.;
RT "Solution structure of calmodulin-W-7 complex: the basis of diversity in
RT molecular recognition.";
RL J. Mol. Biol. 276:165-176(1998).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=10493800; DOI=10.1021/bi9908235;
RA Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M., Schulte P.,
RA Schwalbe H., Griesinger C., Krebs J., Schmid H., Vorherr T.E., Carafoli E.;
RT "NMR solution structure of a complex of calmodulin with a binding peptide
RT of the Ca(2+) pump.";
RL Biochemistry 38:12320-12332(1999).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=10467092; DOI=10.1038/12271;
RA Osawa M., Tokumitsu H., Swindells M.B., Kurihara H., Orita M.,
RA Shibanuma T., Furuya T., Ikura M.;
RT "A novel target recognition revealed by calmodulin in complex with Ca2+-
RT calmodulin-dependent kinase kinase.";
RL Nat. Struct. Biol. 6:819-824(1999).
RN [7]
RP STRUCTURE BY NMR OF 1-77 AND 83-149.
RX PubMed=11142512; DOI=10.1023/a:1026563923774;
RA Chou J.J., Li S., Bax A.;
RT "Study of conformational rearrangement and refinement of structural
RT homology models by the use of heteronuclear dipolar couplings.";
RL J. Biomol. NMR 18:217-227(2000).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=12684008; DOI=10.1016/s0022-2836(03)00271-7;
RA Yap K.L., Yuan T., Mal T.K., Vogel H.J., Ikura M.;
RT "Structural basis for simultaneous binding of two carboxy-terminal peptides
RT of plant glutamate decarboxylase to calmodulin.";
RL J. Mol. Biol. 328:193-204(2003).
RN [9]
RP STRUCTURE BY NMR OF 79-149.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of magnesium-bound form of calmodulin C-domain
RT E104D/E140D Mutant.";
RL Submitted (APR-2008) to the PDB data bank.
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.
CC {ECO:0000250|UniProtKB:P0DP23}.
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; BC094079; AAH94079.1; -; mRNA.
DR PIR; I51402; I51402.
DR RefSeq; NP_001080864.1; NM_001087395.1.
DR RefSeq; NP_001084025.1; NM_001090556.1.
DR RefSeq; NP_001089059.1; NM_001095590.1.
DR RefSeq; XP_018085904.1; XM_018230415.1.
DR PDB; 1CFC; NMR; -; A=2-149.
DR PDB; 1CFD; NMR; -; A=2-149.
DR PDB; 1CFF; NMR; -; A=2-149.
DR PDB; 1CKK; NMR; -; A=2-149.
DR PDB; 1DMO; NMR; -; A=2-149.
DR PDB; 1F70; NMR; -; A=2-77.
DR PDB; 1F71; NMR; -; A=83-149.
DR PDB; 1IQ5; X-ray; 1.80 A; A=1-149.
DR PDB; 1MUX; NMR; -; A=2-149.
DR PDB; 1NWD; NMR; -; A=2-149.
DR PDB; 1SY9; NMR; -; A=2-149.
DR PDB; 1X02; NMR; -; A=2-149.
DR PDB; 1Y0V; X-ray; 3.60 A; H/I/J/K/L/M=6-149.
DR PDB; 2COL; X-ray; 2.20 A; B=80-146.
DR PDB; 2K3S; NMR; -; B=83-149.
DR PDB; 2KDU; NMR; -; A=2-149.
DR PDB; 2LLO; NMR; -; A=2-81.
DR PDB; 2LLQ; NMR; -; A=83-149.
DR PDB; 2MES; NMR; -; A=2-149.
DR PDB; 2RRT; NMR; -; A=79-149.
DR PDB; 4R8G; X-ray; 3.50 A; A/B/H=2-149.
DR PDB; 5J7J; NMR; -; A=2-149.
DR PDB; 5T0X; NMR; -; A=2-149.
DR PDB; 6CTB; NMR; -; A=3-149.
DR PDBsum; 1CFC; -.
DR PDBsum; 1CFD; -.
DR PDBsum; 1CFF; -.
DR PDBsum; 1CKK; -.
DR PDBsum; 1DMO; -.
DR PDBsum; 1F70; -.
DR PDBsum; 1F71; -.
DR PDBsum; 1IQ5; -.
DR PDBsum; 1MUX; -.
DR PDBsum; 1NWD; -.
DR PDBsum; 1SY9; -.
DR PDBsum; 1X02; -.
DR PDBsum; 1Y0V; -.
DR PDBsum; 2COL; -.
DR PDBsum; 2K3S; -.
DR PDBsum; 2KDU; -.
DR PDBsum; 2LLO; -.
DR PDBsum; 2LLQ; -.
DR PDBsum; 2MES; -.
DR PDBsum; 2RRT; -.
DR PDBsum; 4R8G; -.
DR PDBsum; 5J7J; -.
DR PDBsum; 5T0X; -.
DR PDBsum; 6CTB; -.
DR AlphaFoldDB; P0DP33; -.
DR SASBDB; P0DP33; -.
DR SMR; P0DP33; -.
DR DNASU; 108698710; -.
DR DNASU; 380558; -.
DR DNASU; 399259; -.
DR DNASU; 606721; -.
DR GeneID; 108698710; -.
DR GeneID; 380558; -.
DR GeneID; 399259; -.
DR GeneID; 606721; -.
DR KEGG; xla:108698710; -.
DR KEGG; xla:380558; -.
DR KEGG; xla:399259; -.
DR KEGG; xla:606721; -.
DR AGR; Xenbase:XB-GENE-1014645; -.
DR AGR; Xenbase:XB-GENE-17331898; -.
DR AGR; Xenbase:XB-GENE-976648; -.
DR CTD; 108698710; -.
DR CTD; 380558; -.
DR CTD; 399259; -.
DR CTD; 606721; -.
DR OrthoDB; 22601at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Proteomes; UP000186698; Chromosome 5S.
DR Proteomes; UP000186698; Chromosome 8L.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 108698710; Expressed in brain and 19 other cell types or tissues.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR IDEAL; IID50309; -.
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; Metal-binding; Methylation;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CHAIN 2..149
FT /note="Calmodulin-1"
FT /id="PRO_0000439944"
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:0000250|UniProtKB:P0DP23"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:1IQ5"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2LLO"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1IQ5"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1IQ5"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1IQ5"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1F70"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1IQ5"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1IQ5"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1NWD"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1IQ5"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1CFF"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1IQ5"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1IQ5"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5T0X"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1IQ5"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1IQ5"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:1IQ5"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
//
