CALM_CHICK
ID CALM_CHICK Reviewed; 149 AA.
AC P62149; P02593; P70667; P99014; Q5ZIQ6; Q61379; Q61380;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=CALM; Synonyms=CAM; ORFNames=RCJMB04_24e7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6137485; DOI=10.1016/s0021-9258(17)44312-2;
RA Putkey J.A., Ts'Ui K.F., Tanaka T., Lagace L., Stein J.P., Lai E.C.,
RA Means A.R.;
RT "Chicken calmodulin genes. A species comparison of cDNA sequences and
RT isolation of a genomic clone.";
RL J. Biol. Chem. 258:11864-11870(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2981850; DOI=10.1016/s0021-9258(20)71185-3;
RA Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J., Lai E.C.,
RA Means A.R.;
RT "The structural organization of the chicken calmodulin gene.";
RL J. Biol. Chem. 260:907-912(1985).
RN [3]
RP ERRATUM OF PUBMED:2981850.
RA Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J., Lai E.C.,
RA Means A.R.;
RL J. Biol. Chem. 262:4928-4929(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9195880; DOI=10.1016/s0969-2126(97)00217-7;
RA Tabernero L., Taylor D.A., Chandross R.J., VanBerkum M.F.A., Means A.R.,
RA Quiocho F.A., Sack J.S.;
RT "The structure of a calmodulin mutant with a deletion in the central helix:
RT implications for molecular recognition and protein binding.";
RL Structure 5:613-622(1997).
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 -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; L00101; AAA48653.1; -; Genomic_DNA.
DR EMBL; L00096; AAA48653.1; JOINED; Genomic_DNA.
DR EMBL; L00097; AAA48653.1; JOINED; Genomic_DNA.
DR EMBL; L00098; AAA48653.1; JOINED; Genomic_DNA.
DR EMBL; L00099; AAA48653.1; JOINED; Genomic_DNA.
DR EMBL; L00100; AAA48653.1; JOINED; Genomic_DNA.
DR EMBL; M36167; AAA48650.1; -; mRNA.
DR EMBL; AJ720728; CAG32387.1; -; mRNA.
DR PIR; A92394; MCCH.
DR PDB; 1AHR; X-ray; 1.80 A; A=2-149.
DR PDB; 1UP5; X-ray; 1.90 A; A/B=2-149.
DR PDB; 2BCX; X-ray; 2.00 A; A=2-149.
DR PDB; 2BKI; X-ray; 2.90 A; B/D=2-149.
DR PDB; 2KZ2; NMR; -; A=77-149.
DR PDB; 2M3S; NMR; -; A=1-149.
DR PDB; 2O5G; X-ray; 1.08 A; A=2-149.
DR PDB; 2O60; X-ray; 1.55 A; A=2-149.
DR PDB; 2VB6; X-ray; 2.30 A; B=1-149.
DR PDB; 3GOF; X-ray; 1.45 A; A/B=2-149.
DR PDB; 3GP2; X-ray; 1.46 A; A=2-148.
DR PDB; 4BYA; NMR; -; A=77-149.
DR PDB; 5HIT; X-ray; 2.85 A; A=2-148.
DR PDB; 6BNV; EM; 4.60 A; O/P/Q/R/S/T=4-148.
DR PDBsum; 1AHR; -.
DR PDBsum; 1UP5; -.
DR PDBsum; 2BCX; -.
DR PDBsum; 2BKI; -.
DR PDBsum; 2KZ2; -.
DR PDBsum; 2M3S; -.
DR PDBsum; 2O5G; -.
DR PDBsum; 2O60; -.
DR PDBsum; 2VB6; -.
DR PDBsum; 3GOF; -.
DR PDBsum; 3GP2; -.
DR PDBsum; 4BYA; -.
DR PDBsum; 5HIT; -.
DR PDBsum; 6BNV; -.
DR AlphaFoldDB; P62149; -.
DR BMRB; P62149; -.
DR SMR; P62149; -.
DR DIP; DIP-29154N; -.
DR ELM; P62149; -.
DR IntAct; P62149; 1.
DR STRING; 9031.ENSGALP00000016260; -.
DR iPTMnet; P62149; -.
DR MetOSite; P62149; -.
DR PaxDb; P62149; -.
DR Ensembl; ENSGALT00000016279; ENSGALP00000016260; ENSGALG00000010023.
DR Ensembl; ENSGALT00000045488; ENSGALP00000042446; ENSGALG00000026445.
DR VEuPathDB; HostDB:geneid_396523; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000182980; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P62149; -.
DR OMA; SCDRHPP; -.
DR TreeFam; TF300912; -.
DR EvolutionaryTrace; P62149; -.
DR PRO; PR:P62149; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000010023; Expressed in spermatid and 14 other tissues.
DR ExpressionAtlas; P62149; baseline and differential.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0051401; F:CH domain binding; IPI:CAFA.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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_0000198230"
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"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:2M3S"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:2O5G"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2O5G"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:2O5G"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:2O5G"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2O5G"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:2O5G"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2M3S"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2O5G"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2O5G"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:2O5G"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:2O5G"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2O5G"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:2O5G"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK