CALL_CAEEL
ID CALL_CAEEL Reviewed; 161 AA.
AC P04630;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Calmodulin-like protein;
GN Name=cal-1; Synonyms=cmd-1; ORFNames=C13C12.1;
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 [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=3783700; DOI=10.1016/0022-2836(86)90002-1;
RA Salvato M., Sulston J., Albertson D., Brenner S.;
RT "A novel calmodulin-like gene from the nematode Caenorhabditis elegans.";
RL J. Mol. Biol. 190:281-290(1986).
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).
CC -!- FUNCTION: This protein resembles calmodulin in sequence but possibly
CC resembles troponin C in function.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; X04259; CAA27814.1; -; Genomic_DNA.
DR EMBL; Z77653; CAB01124.2; -; Genomic_DNA.
DR PIR; A24921; A24921.
DR PIR; T19229; T19229.
DR RefSeq; NP_001256429.1; NM_001269500.1.
DR AlphaFoldDB; P04630; -.
DR SMR; P04630; -.
DR STRING; 6239.C13C12.1b; -.
DR PaxDb; P04630; -.
DR EnsemblMetazoa; C13C12.1a.1; C13C12.1a.1; WBGene00000285.
DR GeneID; 179715; -.
DR UCSC; T21H3.3.1; c. elegans.
DR CTD; 179715; -.
DR WormBase; C13C12.1a; CE42931; WBGene00000285; cal-1.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00970000196720; -.
DR HOGENOM; CLU_061288_2_1_1; -.
DR InParanoid; P04630; -.
DR PhylomeDB; P04630; -.
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 PRO; PR:P04630; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000285; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; P04630; baseline and differential.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Calmodulin-like protein"
FT /id="PRO_0000073545"
FT DOMAIN 21..56
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 57..92
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 93..128
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 129..161
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
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 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
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 BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 161 AA; 18707 MW; EBE39E5CCD1722BA CRC64;
MAIPSNLMQF SEDIIKQLTP EEIDEFREAF MMFDKDGNGT ISTKELGIAM RSLGQNPTEQ
EILEMINEVD IDGNGQIEFP EFCVMMKRMM KETDSEMIRE AFRVFDKDGN GVITAQEFRY
FMVHMGMQFS EEEVDEMIKE VDVDGDGEID YEEFVKMMSN Q
