Protein: Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (Q9TXJ0)
Organism: Caenorhabditis elegans
Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade which results in transcriptional activation. Transcriptional activation occurs at least in part through phosphorylation of crh-1. Regulates gene expression, sensory morphology, and function of the AFD thermosensory neurons. Involved in long-term adaptation of AFD neurons to temperatures warmer than the initial acclimatized cultivation temperature. Acts in the FLP thermal nociceptors to moderate the responsiveness to noxious heat and controls neuropeptide release from FLP neurons in response to temperature elevations. Regulates the dauer decision, the decision of the larvae to enter into the alternative stress-resistant and long-lived dauer developmental stage, based on the feeding state, primarily in the AWC sensory neurons. Acts non cell-autonomously in the AWC neurons to regulate expression of the daf-28 insulin-like peptide and cell-autonomously in the ASI sensory neurons to regulate expression of the growth promoting daf-7 in a food-regulated manner. Plays a role in memory-based thermal response of an individual AFD neuron cell. Involved in chemotaxis response in AWC neurons to attractant 2-heptanone, a volatile organic compound emitted by the nematode pathogenic bacterium B.nematocida B16. Plays a role in a type of aversive gustatory associated learning called salt avoidance learning via regulation of crh-1 signaling and the promotion of long-term memory formation. Represses transcription of glutamate receptor glr-1 in the nucleus basally and in response to change in synaptic activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:10428833, ECO:0000269|PubMed:25467978, ECO:0000269|PubMed:25467982, ECO:0000269|PubMed:26335407, ECO:0000269|PubMed:27462879, ECO:0000269|PubMed:34766550, ECO:0000269|PubMed:37166173}. Cytoplasm {ECO:0000269|PubMed:25467978, ECO:0000269|PubMed:25467982, ECO:0000269|PubMed:26335407, ECO:0000269|PubMed:27462879, ECO:0000269|PubMed:29875264, ECO:0000269|PubMed:34766550, ECO:0000269|PubMed:37166173}. Note=Localization is regulated by temperature in thermosensory neurons (PubMed:25467978, PubMed:25467982). Localizes to the nucleus upon elevated temperature shift (PubMed:25467978). Translocates from cytoplasm to the nucleus of FLP thermal nociceptors during thermal adaptation (PubMed:25467982). Localizes to the nucleus when incubated at 15 degrees Celsius but is cytoplasmic in AFD neurons when conditioned at 25 degrees Celsius; in FLP neurons, it localizes to the cytoplasm at 20 degrees Celsius and translocates to the nucleus when incubated at 28 degrees Celsius (PubMed:34766550). Localizes to the cytoplasm of ASE neurons before salt conditioning but the subcellular location does not influence salt-avoidance learning (PubMed:29875264). Nuclear accumulation is induced by elevated Ca(2+) and calmodulin in both FLP and AFD neurons (PubMed:34766550). Translocates transiently from cytoplasm to the nucleus, in AWC sensory neurons in response to food withdrawal, and in FLP neurons as a result of phosphorylation by ckk-1 or binding of Ca(2+) and calmodulin upon prolonged heat activation (PubMed:26335407, PubMed:37166173). Prolonged starvation results in cytoplasmic enrichment (PubMed:26335407). The distribution between cytoplasm and nucleus is regulated by synaptic glutamate receptor glr-1 levels in PVC neurons, accumulating in the nucleus with increasing glr-1 (PubMed:27462879). {ECO:0000269|PubMed:25467978, ECO:0000269|PubMed:25467982, ECO:0000269|PubMed:26335407, ECO:0000269|PubMed:27462879, ECO:0000269|PubMed:29875264, ECO:0000269|PubMed:34766550, ECO:0000269|PubMed:37166173}.
InterPro domains:
- IPR011009: Protein kinase-like domain superfamily (homologous_superfamily) [19-304]
- IPR017441: Protein kinase, ATP binding site (binding_site) [28-52]
- IPR008271: Serine/threonine-protein kinase, active site (active_site) [140-152]
- IPR000719: Protein kinase domain (domain) [22-278]
Sequence:
MPLFKRRDGSGPAPNATIREKYDFRDVLGTGAFSKVFLAESKSDAGQMYAVKCIDKKALKGKEESLENEIKVLRKLRHNNIVQLFDTYDEKQFVYLVMELVTGGELFDRIVAKGSYTEQDASNLIRQVLEAVGFMHDNGVVHRDLKPENLLYYNQDEDSKIMISDFGLSKTEDSGVMATACGTPGYVAPEVLQQKPYGKAVDVWSIGVIAYILLCGYPPFYDESDANLFAQIIKGEYEFDAPYWDQISDSAKDFITHLMCCDPEARFTCQDALSHPWISGNTAYTHDIHGTVAVHLKKSLAKRNWKKAYNAAAAIRQLQMLRLSSNSNRLQKQASQQQPEPPTPAFHA
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding), GO:0005516 (calmodulin binding)
Biological Process (BP): GO:0008150 (biological process), GO:0065007 (biological regulation), GO:0051179 (localization), GO:0048518 (positive regulation of biological process), GO:0050789 (regulation of biological process), GO:0009987 (cellular process), GO:0023052 (signaling), GO:0050793 (regulation of developmental process), GO:0051641 (cellular localization), GO:0044237 (cellular metabolic process), GO:0032879 (regulation of localization), GO:0050794 (regulation of cellular process), GO:0051234 (establishment of localization), GO:0071840 (cellular component organization or biogenesis), GO:0051094 (positive regulation of developmental process), GO:0051050 (positive regulation of transport), GO:0007154 (cell communication), GO:0007165 (signal transduction), GO:0033036 (macromolecule localization), GO:0048522 (positive regulation of cellular process), GO:0099536 (synaptic signaling), GO:0051049 (regulation of transport), GO:0046907 (intracellular transport), GO:0032388 (positive regulation of intracellular transport), GO:0060341 (regulation of cellular localization), GO:0006810 (transport), GO:0070727 (cellular macromolecule localization), GO:0051649 (establishment of localization in cell), GO:0016043 (cellular component organization), GO:0060627 (regulation of vesicle-mediated transport), GO:0051130 (positive regulation of cellular component organization), GO:0045807 (positive regulation of endocytosis), GO:0051128 (regulation of cellular component organization), GO:0030100 (regulation of endocytosis), GO:0099504 (synaptic vesicle cycle), GO:0090316 (positive regulation of intracellular protein transport), GO:0071705 (nitrogen compound transport), GO:0032386 (regulation of intracellular transport), GO:1904951 (positive regulation of establishment of protein localization), GO:1905153 (regulation of membrane invagination), GO:0072594 (establishment of protein localization to organelle), GO:0070201 (regulation of establishment of protein localization), GO:0071702 (organic substance transport), GO:0016192 (vesicle-mediated transport), GO:0032880 (regulation of protein localization), GO:0008104 (protein localization), GO:0006996 (organelle organization), GO:0032386 (regulation of intracellular transport), GO:0070925 (organelle assembly), GO:0033365 (protein localization to organelle), GO:0006897 (endocytosis), GO:0007033 (vacuole organization), GO:0099003 (vesicle-mediated transport in synapse), GO:0090322 (regulation of superoxide metabolic process), GO:0051028 (mRNA transport), GO:0033157 (regulation of intracellular protein transport), GO:0080171 (lytic vacuole organization), GO:0030001 (metal ion transport), GO:0080171 (lytic vacuole organization), GO:0007040 (lysosome organization)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0032991 (protein-containing complex), GO:0005829 (cytosol), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus)