Plcl1 phospholipase C-like 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Plcl1provided by MGI
Official Full Name: phospholipase C-like 1provided by MGI
Primary source: MGI:MGI:3036262
See related: Ensembl:ENSMUSG00000038349 AllianceGenome:MGI:3036262
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: PLCE; PLCL; PRIP; PLC-L; PLDL1; PLC-L1; PRIP-1; C230017K02Rik
Summary: Predicted to enable GABA receptor binding activity and phosphatidylinositol phospholipase C activity. Involved in negative regulation of cold-induced thermogenesis. Acts upstream of or within gamma-aminobutyric acid signaling pathway and regulation of GABAergic synaptic transmission. Predicted to be located in cytoplasm. Is expressed in nervous system and vibrissa. Orthologous to human PLCL1 (phospholipase C like 1 (inactive)). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Broad expression in bladder adult (RPKM 3.1), cerebellum adult (RPKM 3.0) and 24 other tissues See more
Orthologs: human all
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Genomic context

Location:: 1 C1.2; 1 28.15 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	1	NC_000067.7 (55442722..55793444)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	1	NC_000067.6 (55405946..55754285)

Chromosome 1 - NC_000067.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

DOT1L protects against podocyte injury in diabetic kidney disease through phospholipase C-like 1.
Title: DOT1L protects against podocyte injury in diabetic kidney disease through phospholipase C-like 1.
PLCL1 regulates fibroblast-like synoviocytes inflammation via NLRP3 inflammasomes in rheumatoid arthritis.
Title: PLCL1 regulates fibroblast-like synoviocytes inflammation via NLRP3 inflammasomes in rheumatoid arthritis.
Expression of PRIP, a phosphatidylinositol 4,5-bisphosphate binding protein, attenuates PI3K/AKT signaling and suppresses tumor growth in a xenograft mouse model.
Title: Expression of PRIP, a phosphatidylinositol 4,5-bisphosphate binding protein, attenuates PI3K/AKT signaling and suppresses tumor growth in a xenograft mouse model.
Phospholipase C-related catalytically inactive protein regulates lipopolysaccharide-induced hypothalamic inflammation-mediated anorexia in mice.
Title: Phospholipase C-related catalytically inactive protein regulates lipopolysaccharide-induced hypothalamic inflammation-mediated anorexia in mice.
PRIP, a protein phosphatase-binding protein, can modulate fat metabolism via phosphoregulation of adipose lipolysis-related molecules, and regulates non-shivering heat generation in brown adipocytes
Title: Phospholipase C-related catalytically inactive protein: A novel signaling molecule for modulating fat metabolism and energy expenditure.
Phospholipase C-related catalytically inactive protein (PRIP)-deficient mouse embryonic fibroblasts exhibited increased cell migration, and was significantly attenuated upon transfection with a siRNA targeting p110alpha, a catalytic subunit of class I phosphoinositide 3-kinases (PIK3CA).
Title: Suppression of cell migration by phospholipase C-related catalytically inactive protein-dependent modulation of PI3K signalling.
These results suggest that PRIPs are positively involved in the development of follicles via their regulation of LH-LHR signaling and estradiol secretion.
Title: Phospholipase C-related but catalytically inactive proteins regulate ovarian follicle development.
Data show that PRIP is required for the fusion of Staphylococcus aureus-containing autophagosome-like vacuoles with lysosomes, indicating that PRIP is a novel modulator in the regulation of the innate immune system in non-phagocytic host cells.
Title: Phospholipase C-related catalytically inactive protein participates in the autophagic elimination of Staphylococcus aureus infecting mouse embryonic fibroblasts.
PRIP promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of HSL and perilipin A, thus reducing PKA-mediated lipolysis.
Title: Phospholipase C-related catalytically inactive protein (PRIP) regulates lipolysis in adipose tissue by modulating the phosphorylation of hormone-sensitive lipase.
Suppressed expression of PRIP-1 induces an elevated expression of KCC2 in the spinal cord, resulting in inhibition of nociception and amelioration of neuropathic pain in DKO mice.
Title: Phospholipase C-related but catalytically inactive protein modulates pain behavior in a neuropathic pain model in mice.

Submit: New GeneRIF Correction See all GeneRIFs (16)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (1)
Targeted (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:224943

NoName (e-PCR)
- UniSTS:224188

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables GABA receptor binding	ISO Inferred from Sequence Orthology more info	PubMed
enables GABA receptor binding	TAS Traceable Author Statement more info	PubMed
enables phosphatidylinositol phospholipase C activity	IBA Inferred from Biological aspect of Ancestor more info
enables phosphatidylinositol phospholipase C activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in gamma-aminobutyric acid signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within gamma-aminobutyric acid signaling pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in intracellular signal transduction	IEA Inferred from Electronic Annotation more info
involved_in lipid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of cold-induced thermogenesis	IGI Inferred from Genetic Interaction more info	PubMed
involved_in phosphatidylinositol metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in phosphatidylinositol-mediated signaling	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within positive regulation of receptor binding	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of synaptic transmission, GABAergic	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within regulation of synaptic transmission, GABAergic	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within regulation of synaptic transmission, GABAergic	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in release of sequestered calcium ion into cytosol	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: inactive phospholipase C-like protein 1

Names: phospholipase C, eta 2 pseudogene; phospholipase C-related but catalytically inactive protein

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001114663.1 → NP_001108135.1 inactive phospholipase C-like protein 1

See identical proteins and their annotated locations for NP_001108135.1

Status: PROVISIONAL

Source sequence(s)

AC145691, AI644888, AK083136, AK140530, BE981359

Consensus CDS

CCDS48263.1

UniProtKB/Swiss-Prot

D3Z0W5, Q3TSM9, Q3USB7

Related

ENSMUSP00000037854.9, ENSMUST00000042986.10

Conserved Domains (5) summary

cd00275
Location:721 → 849

C2_PLC_like; C2 domain present in Phosphoinositide-specific phospholipases C (PLC)

cd08597
Location:399 → 689

PI-PLCc_PRIP_metazoa; Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein

cd13364
Location:116 → 224

PH_PLC_eta; Phospholipase C-eta (PLC-eta) pleckstrin homology (PH) domain

cd15898
Location:244 → 273

EFh_PI-PLC; EF-hand motif [structural motif]

cl28895
Location:244 → 386

EFh_PI-PLC; EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000067.7 Reference GRCm39 C57BL/6J

Range

55442722..55793444

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_036164399.1 → XP_036020292.1 inactive phospholipase C-like protein 1 isoform X1

Conserved Domains (4) summary

cd00275
Location:721 → 849

C2_PLC_like; C2 domain present in Phosphoinositide-specific phospholipases C (PLC)

cd08597
Location:399 → 689

PI-PLCc_PRIP_metazoa; Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein

cd13364
Location:116 → 224

PH_PLC_eta; Phospholipase C-eta (PLC-eta) pleckstrin homology (PH) domain

cd16222
Location:244 → 386

EFh_PRIP1; EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1)

RNA

XR_004941953.1 RNA Sequence

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NG_018587.1: Suppressed sequence

Description

NG_018587.1: This RefSeq was permanently suppressed because it is now thought that this gene does not encode a protein.