The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Phospholipase C beta, distal C-terminal domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 2: 1-phosphatidylinositol 4,5-bisphosphate phosphodie...

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 4 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
3 A2AT93 (/IPI) Q15147 (/IPI) Q91UZ1 (/IPI)
Mitogen-activated protein kinase binding GO:0051019
Interacting selectively and non-covalently with a mitogen-activated protein kinase.
2 A2AT93 (/ISO) Q91UZ1 (/ISO)
Phospholipase C activity GO:0004629
Catalysis of the reaction: a phospholipid + H2O = 1,2-diacylglycerol + a phosphatidate.
1 Q15147 (/TAS)
Mitogen-activated protein kinase binding GO:0051019
Interacting selectively and non-covalently with a mitogen-activated protein kinase.
1 Q9QW07 (/IPI)

There are 7 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Negative regulation of potassium ion transport GO:0043267
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
2 A2AT93 (/ISO) Q91UZ1 (/ISO)
Modulation of chemical synaptic transmission GO:0050804
Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Modulation of chemical synaptic transmission GO:0050804
Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission.
2 A2AT93 (/IMP) Q91UZ1 (/IMP)
G protein-coupled receptor signaling pathway GO:0007186
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription. The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
1 Q15147 (/TAS)
Phototransduction GO:0007602
The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
1 Q9QW07 (/NAS)
Negative regulation of potassium ion transport GO:0043267
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
1 Q9QW07 (/IMP)
Inositol phosphate metabolic process GO:0043647
The chemical reactions and pathways involving inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
1 Q15147 (/TAS)

There are 12 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 A2AT93 (/ISO) Q91UZ1 (/ISO)
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Postsynaptic density GO:0014069
An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Dendrite GO:0030425
A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Parallel fiber to Purkinje cell synapse GO:0098688
An excitatory synapse formed by the parallel fibers of granule cells synapsing onto the dendrites of Purkinje cells.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Parallel fiber to Purkinje cell synapse GO:0098688
An excitatory synapse formed by the parallel fibers of granule cells synapsing onto the dendrites of Purkinje cells.
2 A2AT93 (/IMP) Q91UZ1 (/IMP)
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
2 A2AT93 (/IDA) Q91UZ1 (/IDA)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
2 A2AT93 (/IMP) Q91UZ1 (/IMP)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 Q9QW07 (/IDA)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 Q15147 (/TAS)