PLAAT2 phospholipase A and acyltransferase 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PLAAT2provided by HGNC
Official Full Name: phospholipase A and acyltransferase 2provided by HGNC
Primary source: HGNC:HGNC:17824
See related: Ensembl:ENSG00000133328 MIM:613866; AllianceGenome:HGNC:17824
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: HRASLS2; PLAAT-2; PLA1/2-2
Summary: The protein encoded by this gene has both phospholipase and acyltransferase activities and acts as a tumor suppressor. The encoded protein can hydrolyze dipalmitoylated phosphatidylcholine (PC) to palmitic acid and lyso-PC. In addition, this protein can catalyze the N-acylation of phosphatidylethanolamine and can catalyze the O-acylation of lyso-PC to form PC. [provided by RefSeq, Jul 2016]
Expression: Biased expression in duodenum (RPKM 16.4), small intestine (RPKM 9.9) and 3 other tissues See more
Orthologs: all
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Genomic context

Location:: 11q12.3

Exon count:: 6

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	11	NC_000011.10 (63552770..63565070, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	11	NC_060935.1 (63542032..63554332, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	11	NC_000011.9 (63320242..63330851, complement)

Chromosome 11 - NC_000011.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Data show that acyl-modified forms of HRAS-like tumor suppressors HRASLS2 and HRASLS3 mimicking lipolytic activity of lecithin retinol acyltransferase LRAT.
Title: Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins.
Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)
Title: Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
Observational study of gene-disease association. (HuGE Navigator)
Title: Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
The tumor suppressors TIG3, HRASLS2 and H-rev107 are involved in the phospholipid metabolism with different physiological roles.
Title: Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes.
HRASLS2 protein suppressed growth and RAS activities of cancer cells, and the C-terminal hydrophobic domain appeared to be indispensable for both activities.
Title: Cloning and functional characterization of the HRASLS2 gene.

Submit: New GeneRIF Correction

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables N-acyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables N-acyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables acyltransferase activity	TAS Traceable Author Statement more info
enables calcium-dependent phospholipase A2 activity	IEA Inferred from Electronic Annotation more info
enables calcium-independent phospholipase A2 activity	IEA Inferred from Electronic Annotation more info
enables phosphatidylserine 1-acylhydrolase activity	IEA Inferred from Electronic Annotation more info
enables phospholipase A1 activity	IBA Inferred from Biological aspect of Ancestor more info
enables phospholipase A1 activity	IDA Inferred from Direct Assay more info	PubMed
enables phospholipase A2 activity	IBA Inferred from Biological aspect of Ancestor more info
enables phospholipase A2 activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in N-acylphosphatidylethanolamine metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in N-acylphosphatidylethanolamine metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in lipid catabolic process	IEA Inferred from Electronic Annotation more info
involved_in phosphatidylethanolamine acyl-chain remodeling	TAS Traceable Author Statement more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	TAS Traceable Author Statement more info
located_in membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: phospholipase A and acyltransferase 2

Names: HRAS like suppressor 2; phospholipase A/acyltransferase-2

NP_060348.1

EC 3.1.1.32

EC 3.1.1.4

XP_011543422.1

EC 3.1.1.32

EC 3.1.1.4

XP_054225195.1

EC 3.1.1.32

EC 3.1.1.4

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.