CALM_CAEEL
ID CALM_CAEEL Reviewed; 149 AA.
AC O16305;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=cmd-1; ORFNames=T21H3.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Kraev A., Gazzotti P.;
RT "Expression and functional characterization of calmodulin from
RT Caenorhabditis elegans.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH PDE1; MADF-3; RPL-7A; TAX-6; EFK-1; NPP-1; OBR-4; SOS-1;
RP AKT-1; UNC-13; TAG-196; UGT-48; NMY-2; F27D4.4; DDX-23; EFA-6 AND R11H6.4.
RX PubMed=17854888; DOI=10.1016/j.ceca.2007.07.008;
RA Shen X., Valencia C.A., Gao W., Cotten S.W., Dong B., Huang B.C., Liu R.;
RT "Ca(2+)/Calmodulin-binding proteins from the C. elegans proteome.";
RL Cell Calcium 43:444-456(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS).
RX PubMed=14635136; DOI=10.1002/prot.10517;
RA Symersky J., Lin G., Li S., Qiu S., Carson M., Schormann N., Luo M.;
RT "Structural genomics of Caenorhabditis elegans: crystal structure of
RT calmodulin.";
RL Proteins 53:947-949(2003).
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 -!- SUBUNIT: Interacts (in the presence of Ca(2+)) with pde-1, madf-3, rpl-
CC 7A, tax-6, efk-1, npp-1, obr-4, sos-1, akt-1, unc-13, tag-196, ugt-48,
CC nmy-2, F27D4.4, ddx-23, efa-6 and R11H6.4.
CC {ECO:0000269|PubMed:17854888}.
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; AJ132193; CAA10601.1; -; mRNA.
DR EMBL; FO081216; CCD69969.1; -; Genomic_DNA.
DR PIR; T31737; T31737.
DR RefSeq; NP_503386.1; NM_070985.5.
DR PDB; 1OOJ; X-ray; 2.11 A; A=1-149.
DR PDB; 5H7D; X-ray; 2.57 A; E/F/G/H/K/L/O/P=1-75.
DR PDBsum; 1OOJ; -.
DR PDBsum; 5H7D; -.
DR AlphaFoldDB; O16305; -.
DR BMRB; O16305; -.
DR SMR; O16305; -.
DR BioGRID; 43683; 66.
DR ComplexPortal; CPX-1128; Calcineurin-Calmodulin complex.
DR DIP; DIP-25019N; -.
DR IntAct; O16305; 1.
DR STRING; 6239.T21H3.3; -.
DR iPTMnet; O16305; -.
DR EPD; O16305; -.
DR PaxDb; O16305; -.
DR PeptideAtlas; O16305; -.
DR EnsemblMetazoa; T21H3.3a.1; T21H3.3a.1; WBGene00000552.
DR GeneID; 178614; -.
DR KEGG; cel:CELE_T21H3.3; -.
DR UCSC; T21H3.3.1; c. elegans.
DR CTD; 178614; -.
DR WormBase; T21H3.3a; CE13902; WBGene00000552; cmd-1.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000162930; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; O16305; -.
DR OMA; SCDRHPP; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; O16305; -.
DR Reactome; R-CEL-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-CEL-111933; Calmodulin induced events.
DR Reactome; R-CEL-111957; Cam-PDE 1 activation.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-CEL-163615; PKA activation.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-CEL-203615; eNOS activation.
DR Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR Reactome; R-CEL-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR Reactome; R-CEL-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-CEL-425561; Sodium/Calcium exchangers.
DR Reactome; R-CEL-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-CEL-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-CEL-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-5578775; Ion homeostasis.
DR Reactome; R-CEL-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-CEL-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-CEL-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR Reactome; R-CEL-9619229; Activation of RAC1 downstream of NMDARs.
DR Reactome; R-CEL-9648002; RAS processing.
DR EvolutionaryTrace; O16305; -.
DR PRO; PR:O16305; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000552; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; O16305; baseline and differential.
DR GO; GO:0005955; C:calcineurin complex; IC:ComplexPortal.
DR GO; GO:0071944; C:cell periphery; IDA:WormBase.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
DR GO; GO:0031965; C:nuclear membrane; IDA:WormBase.
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:0043277; P:apoptotic cell clearance; IMP:WormBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0051296; P:establishment of meiotic spindle orientation; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0050918; P:positive chemotaxis; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:WormBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
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; Metal-binding; Methylation;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198250"
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:0000250"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:1OOJ"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1OOJ"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1OOJ"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1OOJ"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1OOJ"
FT HELIX 66..93
FT /evidence="ECO:0007829|PDB:1OOJ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1OOJ"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1OOJ"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1OOJ"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1OOJ"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1OOJ"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:1OOJ"
SQ SEQUENCE 149 AA; 16825 MW; 6B40B8917FC7027B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGF ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVTMMTTK
