Q15111 · PLCL1_HUMAN
- ProteinInactive phospholipase C-like protein 1
- GenePLCL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1095 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor (By similarity).
Regulates the turnover of receptors and thus contributes to the maintenance of GABA-mediated synaptic inhibition. Its aberrant expression could contribute to the genesis and progression of lung carcinoma. Acts as an inhibitor of PPP1C
Regulates the turnover of receptors and thus contributes to the maintenance of GABA-mediated synaptic inhibition. Its aberrant expression could contribute to the genesis and progression of lung carcinoma. Acts as an inhibitor of PPP1C
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | phosphatidylinositol phospholipase C activity | |
Molecular Function | phospholipase C activity | |
Biological Process | gamma-aminobutyric acid signaling pathway | |
Biological Process | intracellular signal transduction | |
Biological Process | lipid metabolic process | |
Biological Process | negative regulation of cold-induced thermogenesis | |
Biological Process | regulation of synaptic transmission, GABAergic |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInactive phospholipase C-like protein 1
- Short namesPLC-L1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15111
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_038993 | 445 | in dbSNP:rs45506698 | |||
Sequence: D → N | ||||||
Natural variant | VAR_038994 | 454 | in dbSNP:rs45506696 | |||
Sequence: P → S | ||||||
Natural variant | VAR_038995 | 546 | in dbSNP:rs45596936 | |||
Sequence: S → F | ||||||
Natural variant | VAR_038996 | 667 | in dbSNP:rs1064213 | |||
Sequence: V → I | ||||||
Natural variant | VAR_038997 | 684 | in dbSNP:rs6741084 | |||
Sequence: W → C | ||||||
Natural variant | VAR_038998 | 937 | in dbSNP:rs45452996 | |||
Sequence: S → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,193 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000319414 | 1-1095 | UniProt | Inactive phospholipase C-like protein 1 | |||
Sequence: MAEGAAGREDPAPPDAAGGEDDPRVGPDAAGDCVTAASGGRMRDRRSGVALPGAAGTPADSEAGLLEAARATPRRSSIIKDPSNQKCGGRKKTVSFSSMPSEKKISSANDCISFMQAGCELKKVRPNSRIYNRFFTLDTDLQALRWEPSKKDLEKAKLDISAIKEIRLGKNTETFRNNGLADQICEDCAFSILHGENYESLDLVANSADVANIWVSGLRYLVSRSKQPLDFMEGNQNTPRFMWLKTVFEAADVDGNGIMLEDTSVELIKQLNPTLKEAKIRLKFKEIQKSKEKLTTRVTEEEFCEAFCELCTRPEVYFLLVQISKNKEYLDANDLMLFLEAEQGVTHITEDICLDIIRRYELSEEGRQKGFLAIDGFTQYLLSSECDIFDPEQKKVAQDMTQPLSHYYINASHNTYLIEDQFRGPADINGYIRALKMGCRSVELDVSDGSDNEPILCNRNNMTTHVSFRSVIEVINKFAFVASEYPLILCLGNHCSLPQQKVMAQQMKKVFGNKLYTEAPLPSESYLPSPEKLKRMIIVKGKKLPSDPDVLEGEVTDEDEEAEMSRRMSVDYNGEQKQIRLCRELSDLVSICKSVQYRDFELSMKSQNYWEMCSFSETEASRIANEYPEDFVNYNKKFLSRIYPSAMRIDSSNLNPQDFWNCGCQIVAMNFQTPGPMMDLHTGWFLQNGGCGYVLRPSIMRDEVSYFSANTKGILPGVSPLALHIKIISGQNFPKPKGACAKGDVIDPYVCIEIHGIPADCSEQRTKTVQQNSDNPIFDETFEFQVNLPELAMIRFVVLDDDYIGDEFIGQYTIPFECLQPGYRHVPLRSFVGDIMEHVTLFVHIAITNRSGGGKAQKRSLSVRMGKKVREYTMLRNIGLKTIDDIFKIAVHPLREAIDMRENMQNAIVSIKELCGLPPIASLKQCLLTLSSRLITSDNTPSVSLVMKDSFPYLEPLGAIPDVQKKMLTAYDLMIQESRFLIEMADTVQEKIVQCQKAGMEFHEELHNLGAKEGLKGRKLNKATESFAWNITVLKGQGDLLKNAKNEAIENMKQIQLACLSCGLSKAPSSSAEAKSKRSLEAIEEKESSEENGKL | |||||||
Modified residue | 47 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 77 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 93 | UniProt | Phosphothreonine; by PKA | ||||
Sequence: T | |||||||
Modified residue | 95 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 556 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 556 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 569 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 569 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1079 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by the catalytic subunit of PKA. Phosphorylation of Thr-93 resulted in dissociation of PPP1C from PRIP1 (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in a variety of fetal and adult organs including brain, lung and kidney. Its expression was greatly reduced in small and non-small cell lung carcinoma. Isoform 1 is predominantly expressed in brain.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PPP2CA (By similarity).
Interacts with Ins(1,4,5)P3, Ins(1,4,5,6)P4, GABARAP, GABA receptor beta subunits, GABA receptor gamma-2 subunits and PPP1C. May form a ternary complex with GABA receptor beta subunit and GABARAP. The formation of a ternary complex with GABA receptor beta subunit and GABARAP could be the key step for facilitating the association of GABARAP with the GABA receptor gamma-2 subunit and to allow it to be transported at the right destination
Interacts with Ins(1,4,5)P3, Ins(1,4,5,6)P4, GABARAP, GABA receptor beta subunits, GABA receptor gamma-2 subunits and PPP1C. May form a ternary complex with GABA receptor beta subunit and GABARAP. The formation of a ternary complex with GABA receptor beta subunit and GABARAP could be the key step for facilitating the association of GABARAP with the GABA receptor gamma-2 subunit and to allow it to be transported at the right destination
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-61 | Disordered | ||||
Sequence: MAEGAAGREDPAPPDAAGGEDDPRVGPDAAGDCVTAASGGRMRDRRSGVALPGAAGTPADS | ||||||
Region | 83-222 | Interaction with PPP1C | ||||
Sequence: SNQKCGGRKKTVSFSSMPSEKKISSANDCISFMQAGCELKKVRPNSRIYNRFFTLDTDLQALRWEPSKKDLEKAKLDISAIKEIRLGKNTETFRNNGLADQICEDCAFSILHGENYESLDLVANSADVANIWVSGLRYLV | ||||||
Domain | 113-223 | PH | ||||
Sequence: SFMQAGCELKKVRPNSRIYNRFFTLDTDLQALRWEPSKKDLEKAKLDISAIKEIRLGKNTETFRNNGLADQICEDCAFSILHGENYESLDLVANSADVANIWVSGLRYLVS | ||||||
Domain | 398-542 | PI-PLC X-box | ||||
Sequence: QDMTQPLSHYYINASHNTYLIEDQFRGPADINGYIRALKMGCRSVELDVSDGSDNEPILCNRNNMTTHVSFRSVIEVINKFAFVASEYPLILCLGNHCSLPQQKVMAQQMKKVFGNKLYTEAPLPSESYLPSPEKLKRMIIVKGK | ||||||
Region | 543-567 | Interaction with GABA A beta subunit | ||||
Sequence: KLPSDPDVLEGEVTDEDEEAEMSRR | ||||||
Domain | 585-701 | PI-PLC Y-box | ||||
Sequence: LSDLVSICKSVQYRDFELSMKSQNYWEMCSFSETEASRIANEYPEDFVNYNKKFLSRIYPSAMRIDSSNLNPQDFWNCGCQIVAMNFQTPGPMMDLHTGWFLQNGGCGYVLRPSIMR | ||||||
Domain | 701-830 | C2 | ||||
Sequence: RDEVSYFSANTKGILPGVSPLALHIKIISGQNFPKPKGACAKGDVIDPYVCIEIHGIPADCSEQRTKTVQQNSDNPIFDETFEFQVNLPELAMIRFVVLDDDYIGDEFIGQYTIPFECLQPGYRHVPLRS | ||||||
Coiled coil | 894-914 | |||||
Sequence: LREAIDMRENMQNAIVSIKEL | ||||||
Coiled coil | 1034-1059 | |||||
Sequence: LKGQGDLLKNAKNEAIENMKQIQLAC | ||||||
Region | 1066-1095 | Disordered | ||||
Sequence: KAPSSSAEAKSKRSLEAIEEKESSEENGKL | ||||||
Compositional bias | 1077-1095 | Basic and acidic residues | ||||
Sequence: KRSLEAIEEKESSEENGKL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q15111-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,095
- Mass (Da)122,728
- Last updated2009-04-14 v3
- ChecksumC7B34D38C654E2D3
Q15111-2
- Name2
- Differences from canonical
- 1-98: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_031475 | 1-98 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 176 | in Ref. 1; BAA07688 | ||||
Sequence: R → T | ||||||
Sequence conflict | 563 | in Ref. 1; BAA07688 | ||||
Sequence: E → Q | ||||||
Compositional bias | 1077-1095 | Basic and acidic residues | ||||
Sequence: KRSLEAIEEKESSEENGKL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D42108 EMBL· GenBank· DDBJ | BAA07688.1 EMBL· GenBank· DDBJ | mRNA | ||
AC011997 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC013478 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC020719 EMBL· GenBank· DDBJ | AAY14733.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC101531 EMBL· GenBank· DDBJ | AAI01532.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111985 EMBL· GenBank· DDBJ | AAI11986.1 EMBL· GenBank· DDBJ | mRNA | ||
BX537442 EMBL· GenBank· DDBJ | CAD97684.1 EMBL· GenBank· DDBJ | mRNA |