ID CALM_ELEEL Reviewed; 149 AA.
AC P02594; Q90496;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=calm;
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electroplax;
RX PubMed=6185488; DOI=10.1016/s0021-9258(18)33040-0;
RA Lagace L., Chandra T., Woo S.L.C., Means A.R.;
RT "Identification of multiple species of calmodulin messenger RNA using a
RT full length complementary DNA.";
RL J. Biol. Chem. 258:1684-1688(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electroplax;
RA Iida Y.;
RT "cDNA sequences and molecular evolution of calmodulin genes of chicken and
RT eel.";
RL Bull. Chem. Soc. Jpn. 57:2667-2668(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 93-114.
RC TISSUE=Electroplax;
RX PubMed=6941292; DOI=10.1073/pnas.78.4.2330;
RA Munjaal R.P., Chandra T., Woo S.L.C., Dedman J.R., Means A.R.;
RT "A cloned calmodulin structural gene probe is complementary to DNA
RT sequences from diverse species.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2330-2334(1981).
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; J00931; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M36168; AAA49236.1; -; mRNA.
DR EMBL; M17495; AAA49237.1; -; mRNA.
DR EMBL; M25058; AAA62797.1; -; mRNA.
DR PIR; A03022; MCEE.
DR PIR; I50533; I50533.
DR PIR; I50535; I50535.
DR AlphaFoldDB; P02594; -.
DR BMRB; P02594; -.
DR SMR; P02594; -.
DR STRING; 8005.ENSEEEP00000028240; -.
DR Ensembl; ENSEEET00000043913.1; ENSEEEP00000043415.1; ENSEEEG00000020432.1.
DR Ensembl; ENSEEET00000043915.1; ENSEEEP00000043417.1; ENSEEEG00000020432.1.
DR GeneTree; ENSGT00950000182980; -.
DR OrthoDB; 3947998at2759; -.
DR Proteomes; UP000314983; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Calcium; Metal-binding; Methylation; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198233"
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 CONFLICT 93
FT /note="F -> V (in Ref. 3; AAA62797)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="D -> E (in Ref. 3; AAA49237)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="R -> G (in Ref. 3; AAA49237)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="M -> I (in Ref. 3; AAA49237)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="G -> A (in Ref. 3; AAA62797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 16810 MW; 6B4BDCDEE30F5046 CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMAKKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
//
