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Calmodulin (CaM)

 CALM_CHICK              Reviewed;         149 AA.
P62149; P02593; P70667; P99014; Q5ZIQ6; Q61379; Q61380;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 138.
RecName: Full=Calmodulin;
Short=CaM;
Name=CALM; Synonyms=CAM; ORFNames=RCJMB04_24e7;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6137485;
Putkey J.A., Ts'Ui K.F., Tanaka T., Lagace L., Stein J.P., Lai E.C.,
Means A.R.;
"Chicken calmodulin genes. A species comparison of cDNA sequences and
isolation of a genomic clone.";
J. Biol. Chem. 258:11864-11870(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2981850;
Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J.,
Lai E.C., Means A.R.;
"The structural organization of the chicken calmodulin gene.";
J. Biol. Chem. 260:907-912(1985).
[3]
ERRATUM.
Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J.,
Lai E.C., Means A.R.;
J. Biol. Chem. 262:4928-4929(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Iida Y.;
"cDNA sequences and molecular evolution of calmodulin genes of chicken
and eel.";
Bull. Chem. Soc. Jpn. 57:2667-2668(1984).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CB; TISSUE=Bursa of Fabricius;
PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
function analysis.";
Genome Biol. 6:R6.1-R6.9(2005).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=9195880; DOI=10.1016/S0969-2126(97)00217-7;
Tabernero L., Taylor D.A., Chandross R.J., VanBerkum M.F.A.,
Means A.R., Quiocho F.A., Sack J.S.;
"The structure of a calmodulin mutant with a deletion in the central
helix: implications for molecular recognition and protein binding.";
Structure 5:613-622(1997).
-!- FUNCTION: Calmodulin mediates the control of a large number of
enzymes, ion channels and other proteins by Ca(2+). Among the
enzymes to be stimulated by the calmodulin-Ca(2+) complex are a
number of protein kinases and phosphatases.
-!- MISCELLANEOUS: This protein has four functional calcium-binding
sites.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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EMBL; L00101; AAA48653.1; -; Genomic_DNA.
EMBL; L00096; AAA48653.1; JOINED; Genomic_DNA.
EMBL; L00097; AAA48653.1; JOINED; Genomic_DNA.
EMBL; L00098; AAA48653.1; JOINED; Genomic_DNA.
EMBL; L00099; AAA48653.1; JOINED; Genomic_DNA.
EMBL; L00100; AAA48653.1; JOINED; Genomic_DNA.
EMBL; M36167; AAA48650.1; -; mRNA.
EMBL; AJ720728; CAG32387.1; -; mRNA.
PIR; A92394; MCCH.
UniGene; Gga.11685; -.
PDB; 1AHR; X-ray; 1.80 A; A=2-149.
PDB; 1UP5; X-ray; 1.90 A; A/B=2-149.
PDB; 2BCX; X-ray; 2.00 A; A=2-149.
PDB; 2BKI; X-ray; 2.90 A; B/D=2-149.
PDB; 2KZ2; NMR; -; A=77-149.
PDB; 2M3S; NMR; -; A=1-149.
PDB; 2O5G; X-ray; 1.08 A; A=2-149.
PDB; 2O60; X-ray; 1.55 A; A=2-149.
PDB; 2VB6; X-ray; 2.30 A; B=1-149.
PDB; 3GOF; X-ray; 1.45 A; A/B=2-149.
PDB; 3GP2; X-ray; 1.46 A; A=2-148.
PDB; 4BYA; NMR; -; A=77-149.
PDB; 5HIT; X-ray; 2.85 A; A=2-148.
PDB; 6BNV; EM; 4.60 A; O/P/Q/R/S/T=4-148.
PDBsum; 1AHR; -.
PDBsum; 1UP5; -.
PDBsum; 2BCX; -.
PDBsum; 2BKI; -.
PDBsum; 2KZ2; -.
PDBsum; 2M3S; -.
PDBsum; 2O5G; -.
PDBsum; 2O60; -.
PDBsum; 2VB6; -.
PDBsum; 3GOF; -.
PDBsum; 3GP2; -.
PDBsum; 4BYA; -.
PDBsum; 5HIT; -.
PDBsum; 6BNV; -.
ProteinModelPortal; P62149; -.
SMR; P62149; -.
DIP; DIP-29154N; -.
ELM; P62149; -.
IntAct; P62149; 1.
STRING; 9031.ENSGALP00000037503; -.
iPTMnet; P62149; -.
PaxDb; P62149; -.
PRIDE; P62149; -.
Ensembl; ENSGALT00000045488; ENSGALP00000042446; ENSGALG00000026445.
Ensembl; ENSGALT00000080380; ENSGALP00000044697; ENSGALG00000010023.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118901; -.
HOVERGEN; HBG012180; -.
InParanoid; P62149; -.
OrthoDB; EOG091G0V73; -.
TreeFam; TF300912; -.
Reactome; R-GGA-111932; CaMK IV-mediated phosphorylation of CREB.
Reactome; R-GGA-111933; Calmodulin induced events.
Reactome; R-GGA-111957; Cam-PDE 1 activation.
Reactome; R-GGA-114608; Platelet degranulation.
Reactome; R-GGA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-GGA-163615; PKA activation.
Reactome; R-GGA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-GGA-203615; eNOS activation.
Reactome; R-GGA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-GGA-2672351; Stimuli-sensing channels.
Reactome; R-GGA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-GGA-4086398; Ca2+ pathway.
Reactome; R-GGA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-GGA-425561; Sodium/Calcium exchangers.
Reactome; R-GGA-442717; CREB phosphorylation through the activation of CaMKK.
Reactome; R-GGA-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-GGA-442745; Activation of CaMK IV.
Reactome; R-GGA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-GGA-445355; Smooth Muscle Contraction.
Reactome; R-GGA-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-GGA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-GGA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-GGA-5578775; Ion homeostasis.
Reactome; R-GGA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
Reactome; R-GGA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-GGA-5627123; RHO GTPases activate PAKs.
Reactome; R-GGA-5673001; RAF/MAP kinase cascade.
Reactome; R-GGA-70221; Glycogen breakdown (glycogenolysis).
Reactome; R-GGA-8876725; Protein methylation.
Reactome; R-GGA-936837; Ion transport by P-type ATPases.
EvolutionaryTrace; P62149; -.
PRO; PR:P62149; -.
Proteomes; UP000000539; Chromosome 3.
Proteomes; UP000000539; Chromosome 5.
Bgee; ENSGALG00000010023; Expressed in 11 organ(s), highest expression level in testis.
ExpressionAtlas; P62149; baseline and differential.
GO; GO:0034704; C:calcium channel complex; IEA:Ensembl.
GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0030017; C:sarcomere; IEA:Ensembl.
GO; GO:0005876; C:spindle microtubule; IEA:Ensembl.
GO; GO:0000922; C:spindle pole; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0010856; F:adenylate cyclase activator activity; IEA:Ensembl.
GO; GO:0008179; F:adenylate cyclase binding; IEA:Ensembl.
GO; GO:0019855; F:calcium channel inhibitor activity; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
GO; GO:0051401; F:CH domain binding; IPI:CAFA.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
GO; GO:0031997; F:N-terminal myristoylation domain binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0072542; F:protein phosphatase activator activity; IEA:Ensembl.
GO; GO:0031432; F:titin binding; IEA:Ensembl.
GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
GO; GO:0005513; P:detection of calcium ion; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
GO; GO:0075206; P:positive regulation by host of symbiont cAMP-mediated signal transduction; IEA:Ensembl.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
CDD; cd00051; EFh; 2.
InterPro; IPR039030; Calmodulin.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
PANTHER; PTHR23050:SF311; PTHR23050:SF311; 1.
Pfam; PF13499; EF-hand_7; 2.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 4.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome; Metal-binding;
Methylation; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 149 Calmodulin.
/FTId=PRO_0000198230.
DOMAIN 8 43 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 44 79 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 81 116 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 117 149 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 21 32 1.
CA_BIND 57 68 2.
CA_BIND 94 105 3.
CA_BIND 130 141 4.
MOD_RES 2 2 N-acetylalanine. {ECO:0000250}.
MOD_RES 116 116 N6,N6,N6-trimethyllysine. {ECO:0000250}.
TURN 2 4 {ECO:0000244|PDB:2M3S}.
HELIX 7 20 {ECO:0000244|PDB:2O5G}.
STRAND 25 28 {ECO:0000244|PDB:2O5G}.
HELIX 30 39 {ECO:0000244|PDB:2O5G}.
HELIX 46 56 {ECO:0000244|PDB:2O5G}.
STRAND 61 65 {ECO:0000244|PDB:2O5G}.
HELIX 66 74 {ECO:0000244|PDB:2O5G}.
TURN 79 81 {ECO:0000244|PDB:2M3S}.
HELIX 82 93 {ECO:0000244|PDB:2O5G}.
STRAND 98 101 {ECO:0000244|PDB:2O5G}.
HELIX 103 112 {ECO:0000244|PDB:2O5G}.
HELIX 119 129 {ECO:0000244|PDB:2O5G}.
STRAND 134 138 {ECO:0000244|PDB:2O5G}.
HELIX 139 145 {ECO:0000244|PDB:2O5G}.
SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK


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