CALM_ANAPL
ID CALM_ANAPL Reviewed; 149 AA.
AC P62144; P02593; P70667; P99014; Q61379; Q61380;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=CALM; Synonyms=CAM;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8389959; DOI=10.1016/0169-328x(93)90022-h;
RA Kimura N., Kurosawa N., Kondo K., Tsukada Y.;
RT "Molecular cloning of the kainate-binding protein and calmodulin genes
RT which are induced by an imprinting stimulus in ducklings.";
RL Brain Res. Mol. Brain Res. 17:351-355(1993).
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; D83350; BAA11896.1; -; mRNA.
DR PIR; I51202; I51202.
DR PDB; 1UP5; X-ray; 1.90 A; A/B=2-149.
DR PDBsum; 1UP5; -.
DR AlphaFoldDB; P62144; -.
DR BMRB; P62144; -.
DR SMR; P62144; -.
DR Ensembl; ENSAPLT00020007544; ENSAPLP00020007025; ENSAPLG00020005121.
DR Ensembl; ENSAPLT00020007678; ENSAPLP00020007147; ENSAPLG00020005235.
DR OMA; SCDRHPP; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198229"
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 HELIX 7..20
FT /evidence="ECO:0007829|PDB:1UP5"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1UP5"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1UP5"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1UP5"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1UP5"
FT HELIX 66..93
FT /evidence="ECO:0007829|PDB:1UP5"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1UP5"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1UP5"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1UP5"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:1UP5"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
