CMK1_CAEBR
ID CMK1_CAEBR Reviewed; 356 AA.
AC A8X6H4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 4.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1 {ECO:0000250|UniProtKB:Q9TXJ0};
DE EC=2.7.11.17 {ECO:0000250|UniProtKB:Q9TXJ0};
DE AltName: Full=CaM kinase I {ECO:0000250|UniProtKB:Q9TXJ0};
DE Short=CaM-KI {ECO:0000250|UniProtKB:Q9TXJ0};
GN Name=cmk-1; ORFNames=CBG08406;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in
CC the calcium-triggered CaMKK-CaMK1 signaling cascade which results in
CC transcriptional activation. Transcriptional activation occurs at least
CC in part through phosphorylation of crh-1. Regulates gene expression,
CC sensory morphology, and function of the AFD thermosensory neurons.
CC Involved in long-term adaptation of AFD neurons to temperatures warmer
CC than the initial acclimatized cultivation temperature. Acts in the FLP
CC thermal nociceptors to moderate the responsiveness to noxious heat and
CC controls neuropeptide release from FLP neurons in response to
CC temperature elevations. Regulates the dauer decision, the decision of
CC the larvae to enter into the alternative stress-resistant and long-
CC lived dauer developmental stage, based on the feeding state, primarily
CC in the AWC sensory neurons. Acts non cell-autonomously in the AWC
CC neurons to regulate expression of the daf-28 insulin-like peptide and
CC cell-autonomously in the ASI sensory neurons to regulate expression of
CC the growth promoting daf-7 in a food-regulated manner. Plays a role in
CC memory-based thermal response of an individual AFD neuron cell.
CC Involved in chemotaxis response in AWC neurons to attractant 2-
CC heptanone, a volatile organic compound emitted by the nematode
CC pathogenic bacterium B.nematocida B16. Represses transcription of
CC glutamate receptor glr-1 in the nucleus basally and in response to
CC change in synaptic activity. {ECO:0000250|UniProtKB:Q63450}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17;
CC Evidence={ECO:0000250|UniProtKB:Q9TXJ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.17; Evidence={ECO:0000250|UniProtKB:Q9TXJ0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9TXJ0};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC calmodulin results in a conformational change that generates functional
CC binding sites for both substrate and ATP, and thus relieves
CC autoinhibition and lowers the Km of substrate binding. Must be
CC phosphorylated by ckk-1 to be maximally active but this does not appear
CC to be required for activity in AFD neurons.
CC {ECO:0000250|UniProtKB:Q9TXJ0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9TXJ0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9TXJ0}. Note=Localization is regulated by
CC temperature in thermosensory neurons. Localizes to the nucleus upon
CC elevated temperature shift. Translocates from cytoplasm to the nucleus
CC of FLP thermal nociceptors during thermal adaptation. Translocates
CC transiently from cytoplasm to the nucleus of AWC sensory neurons in
CC response to food withdrawal. Prolonged starvation results in
CC cytoplasmic enrichment. The distribution between cytoplasm and nucleus
CC is regulated by synaptic glutamate receptor glr-1 levels in PVC
CC neurons, accumulating in the nucleus with increasing glr-1.
CC {ECO:0000250|UniProtKB:Q9TXJ0}.
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and interacts in the inactive folded state with the catalytic
CC domain as a pseudosubstrate. {ECO:0000250|UniProtKB:Q9TXJ0}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000255}.
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DR EMBL; HE601100; CAP28235.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X6H4; -.
DR SMR; A8X6H4; -.
DR STRING; 6238.CBG08406; -.
DR WormBase; CBG08406; CBP46723; WBGene00030202; Cbr-cmk-1.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; A8X6H4; -.
DR OMA; ADCPEGK; -.
DR OrthoDB; 330091at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Calmodulin-binding; Cytoplasm;
KW Developmental protein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..356
FT /note="Calcium/calmodulin-dependent protein kinase type 1"
FT /id="PRO_0000395334"
FT DOMAIN 22..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 278..318
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT REGION 298..319
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT MOTIF 2..7
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9TXJ0"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 179
FT /note="Phosphothreonine; by ckk-1"
FT /evidence="ECO:0000250|UniProtKB:Q9TXJ0"
SQ SEQUENCE 356 AA; 40532 MW; C57BE221D474F0A4 CRC64;
MPLFKRRDVN TPAPTSSIRE KYDFRDVLGT GAFSKVFLAE SKTDVGQLYA VKCIDKKALK
GKEESLENEI KVLRKLRHNN IVQLFETYDE KQFVYLVMEL VTGGELFDRI VAKGSYTEQD
ASNLIRQVLE AVSFMHDNGV VHRDLKPENL LYYNQDEDSK IMISDFGLSK TEDSGVMATA
CGTPGYVAPE VLQQKPYGKA VDVWSIGVIA YILLCGYPPF YDESDANLFA QIIKGEYEFD
APYWDQISDS AKDFISHLMC CDPEMRFTCQ SALEHPWISG NTAYTHDIHR TVAVHLKKSL
AKRNWKKAFN AAAAIRQLQL LRLSPIATAF RNKRPNSNQR LQLPNVLVFQ YFCKIP
