CALM_CHLRE
ID CALM_CHLRE Reviewed; 163 AA.
AC P04352;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Calmodulin;
DE Short=CaM;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3198631; DOI=10.1016/s0021-9258(19)77643-1;
RA Zimmer W.E., Schloss J.A., Silflow C.D., Youngblom J., Watterson D.M.;
RT "Structural organization, DNA sequence, and expression of the calmodulin
RT gene.";
RL J. Biol. Chem. 263:19370-19383(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-163, AND ACETYLATION AT ALA-2.
RX PubMed=16664269; DOI=10.1104/pp.78.3.477;
RA Lukas T.J., Wiggins M.E., Watterson D.M.;
RT "Amino acid sequence of a novel calmodulin from the unicellular alga
RT Chlamydomonas.";
RL Plant Physiol. 78:477-483(1985).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATED WITH THE COMPLEX CONTAINING
RP CFAP61; CFAP91 AND CFAP251.
RX PubMed=17967944; DOI=10.1083/jcb.200703107;
RA Dymek E.E., Smith E.F.;
RT "A conserved CaM- and radial spoke associated complex mediates regulation
RT of flagellar dynein activity.";
RL J. Cell Biol. 179:515-526(2007).
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. {ECO:0000269|PubMed:17967944}.
CC -!- SUBUNIT: Associates with the spoke-associated complex containing
CC CFAP61, CFAP91 and CFAP251; the association is calcium sensitive.
CC {ECO:0000269|PubMed:17967944}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000269|PubMed:17967944}.
CC -!- PTM: Trimethylation of Lys-119 observed in other calmodulins is absent
CC here.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- MISCELLANEOUS: This protein is unusual among eukaryotic calmodulins in
CC having an 11-residue extension of its carboxyl end.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; M20729; AAA33083.1; -; Genomic_DNA.
DR PIR; A32005; MCKM.
DR RefSeq; XP_001703420.1; XM_001703368.1.
DR PDB; 7JTS; EM; 6.10 A; t=1-163.
DR PDBsum; 7JTS; -.
DR AlphaFoldDB; P04352; -.
DR SMR; P04352; -.
DR STRING; 3055.EDP06102; -.
DR iPTMnet; P04352; -.
DR ProMEX; P04352; -.
DR EnsemblPlants; PNW85257; PNW85257; CHLRE_03g178150v5.
DR GeneID; 5728821; -.
DR Gramene; PNW85257; PNW85257; CHLRE_03g178150v5.
DR KEGG; cre:CHLRE_03g178150v5; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR OMA; FPEFLML; -.
DR OrthoDB; 1386217at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
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; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Flagellum; Metal-binding; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16664269"
FT CHAIN 2..163
FT /note="Calmodulin"
FT /id="PRO_0000198286"
FT DOMAIN 11..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 47..82
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 84..119
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 120..155
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
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:0000269|PubMed:16664269"
SQ SEQUENCE 163 AA; 18296 MW; 87C87F0AFB8AAE22 CRC64;
MAANTEQLTE EQIAEFKEAF ALFDKDGDGT ITTKELGTVM RSLGQNPTEA ELQDMISEVD
ADGNGTIDFP EFLMLMARKM KETDHEDELR EAFKVFDKDG NGFISAAELR HVMTNLGEKL
SEEEVDEMIR EADVDGDGQV NYEEFVRMMT SGATDDKDKK GHK
