LYPLA1 lysophospholipase 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: LYPLA1provided by HGNC
Official Full Name: lysophospholipase 1provided by HGNC
Primary source: HGNC:HGNC:6737
See related: Ensembl:ENSG00000120992 MIM:605599; AllianceGenome:HGNC:6737
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: APT1; LPL1; APT-1; LPL-I; hAPT1
Summary: This gene encodes a member of the alpha/beta hydrolase superfamily. The encoded protein functions as a homodimer, exhibiting both depalmitoylating as well as lysophospholipase activity, and may be involved in Ras localization and signaling. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene have been defined on chromosomes 4, 6, and 7. [provided by RefSeq, Jul 2013]
Expression: Ubiquitous expression in urinary bladder (RPKM 38.7), testis (RPKM 35.4) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 8q11.23

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	8	NC_000008.11 (54042987..54101947, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	8	NC_060932.1 (54420379..54479027, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	8	NC_000008.10 (54955547..55014507, complement)

Chromosome 8 - NC_000008.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A conserved but structurally divergent loop in acyl protein thioesterase 1 regulates its catalytic activity, ligand binding, and folded stability.
Title: A conserved but structurally divergent loop in acyl protein thioesterase 1 regulates its catalytic activity, ligand binding, and folded stability.
Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals.
Title: Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals.
LncRNA LOXL1-AS1 Facilitates the Oncogenic Character in Cervical Cancer by the miR-526b-5p /LYPLA1 Axis.
Title: LncRNA LOXL1-AS1 Facilitates the Oncogenic Character in Cervical Cancer by the miR-526b-5p /LYPLA1 Axis.
LYPLA1 and LYPLA2 are each able to account for the loss of the other to maintain lipid homeostasis in cells
Title: Lysophospholipases cooperate to mediate lipid homeostasis and lysophospholipid signaling.
The depalmitoylating enzyme acyl-protein thioesterase 1 (APT1) directs the asymmetric localization of Numb and beta-catenin in MDA-MB-231 triple receptor-negative breast cancer cells.
Title: The depalmitoylase APT1 directs the asymmetric partitioning of Notch and Wnt signaling during cell division.
Study results suggest that the LYPLA1 gene plays a tumorpromotor role in nonsmall cell lung cancer cells in vitro.
Title: Inhibition of cell proliferation and migration in non‑small cell lung cancer cells through the suppression of LYPLA1.
Data show taht active S-depalmitoylation in mitochondria, in part mediated by acyl-protein thioesterase 1 (APT1)
Title: Active and dynamic mitochondrial S-depalmitoylation revealed by targeted fluorescent probes.
Here, we describe the conserved functions of APT1 and APT2 across organisms and discuss the possibility that these enzymes are members of a larger family of depalmitoylation enzymes.
Title: Enzymatic protein depalmitoylation by acyl protein thioesterases.
High expression of APT1 is associated with chronic lymphocytic leukemia.
Title: miRs-138 and -424 control palmitoylation-dependent CD95-mediated cell death by targeting acyl protein thioesterases 1 and 2 in CLL.
identifcation APT1 as one of the thioesterases in the acylation cycle and demonstration that this protein is a cellular target of the inhibitor.
Title: Small-molecule inhibition of APT1 affects Ras localization and signaling.

Submit: New GeneRIF Correction See all GeneRIFs (14)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

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)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
Knockdown of lysophospholipase I (LYPLA1) by siRNA inhibits HIV-1 replication in HeLa P4/R5 cells	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Readthrough LYPLA1-TCEA1

Readthrough gene: LYPLA1-TCEA1, Included gene: TCEA1

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables carboxylic ester hydrolase activity	IBA Inferred from Biological aspect of Ancestor more info
enables lipase activity	IDA Inferred from Direct Assay more info	PubMed
enables lysophospholipase activity	IDA Inferred from Direct Assay more info	PubMed
enables palmitoyl-(protein) hydrolase activity	IBA Inferred from Biological aspect of Ancestor more info
enables palmitoyl-(protein) hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables palmitoyl-(protein) hydrolase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables phospholipase 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 fatty acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in fatty acid transport	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of Golgi to plasma membrane protein transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of Golgi to plasma membrane protein transport	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of aggrephagy	IDA Inferred from Direct Assay more info	PubMed
involved_in protein depalmitoylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein depalmitoylation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular exosome	HDA more info	PubMed
located_in mitochondrion	HTP more info	PubMed
is_active_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear membrane	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	IDA Inferred from Direct Assay more info
is_active_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: acyl-protein thioesterase 1

Names: lysoPLA I; lysophospholipase I; lysophospholipid-specific lysophospholipase; palmitoyl-protein hydrolase

NP_001266285.1

EC 3.1.2.22

NP_001266286.1

EC 3.1.2.22

NP_001266287.1

EC 3.1.2.22

NP_001266288.1

EC 3.1.2.22

NP_001266289.1

EC 3.1.2.22

NP_001412766.1

EC 3.1.2.22

NP_006321.1

EC 3.1.2.22

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_001279356.2 → NP_001266285.1 acyl-protein thioesterase 1 isoform 2

See identical proteins and their annotated locations for NP_001266285.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks an in-frame exon in the central coding region, compared to variant 1. The encoded isoform (2) is shorter, compared to isoform 1.

Source sequence(s)

AA827237, AF035293, AF052112, AK298206

Consensus CDS

CCDS75739.1

UniProtKB/TrEMBL

B4DP64, E5RGR0

Related

ENSP00000482430.1, ENST00000618914.4

Conserved Domains (1) summary

pfam02230
Location:11 → 192

Abhydrolase_2; Phospholipase/Carboxylesterase
NM_001279357.2 → NP_001266286.1 acyl-protein thioesterase 1 isoform 3

See identical proteins and their annotated locations for NP_001266286.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an in-frame exon in the central coding region, compared to variant 1. The encoded isoform (3) is shorter, compared to isoform 1.

Source sequence(s)

AA827237, AF035293, AF052112, AF077199

Consensus CDS

CCDS64899.1

UniProtKB/TrEMBL

E5RGR0

Related

ENSP00000344477.6, ENST00000343231.10

Conserved Domains (1) summary

pfam02230
Location:11 → 210

Abhydrolase_2; Phospholipase/Carboxylesterase
NM_001279358.2 → NP_001266287.1 acyl-protein thioesterase 1 isoform 4

Status: REVIEWED

Description

Transcript Variant: This variant (4) uses an alternate in-frame splice site in the 3' coding region, compared to variant 1. The encoded isoform (4) is shorter, compared to isoform 1.

Source sequence(s)

AA827237, AF035293, AF052112, DA881616

UniProtKB/TrEMBL

B4DJV9

Conserved Domains (1) summary

pfam02230
Location:11 → 212

Abhydrolase_2; Phospholipase/Carboxylesterase
NM_001279359.2 → NP_001266288.1 acyl-protein thioesterase 1 isoform 5

See identical proteins and their annotated locations for NP_001266288.1

Status: REVIEWED

Description

Transcript Variant: This variant (5) uses an alternate splice site in its 5' coding region, and initiates translation at an alternate start codon, compared to variant 1. The encoded isoform (5) has a shorter and distinct N-terminus, compared to isoform 1.

Source sequence(s)

AA307642, AA827237, AF035293, AF052112

UniProtKB/Swiss-Prot

O75608

Conserved Domains (1) summary

pfam02230
Location:8 → 177

Abhydrolase_2; Phospholipase/Carboxylesterase
NM_001279360.2 → NP_001266289.1 acyl-protein thioesterase 1 isoform 6

Status: REVIEWED

Description

Transcript Variant: This variant (6) uses an alternate 5'-terminal exon, and initiates translation at a downstream start codon, compared to variant 1. The encoded isoform (6) has a shorter N-terminus, compared to isoform 1.

Source sequence(s)

AA827237, AF035293, DA817192, DA883059

Consensus CDS

CCDS75738.1

UniProtKB/TrEMBL

A0A087X1K9

Related

ENSP00000484280.1, ENST00000618741.1

Conserved Domains (1) summary

pfam02230
Location:1 → 162

Abhydrolase_2; Phospholipase/Carboxylesterase
NM_001425837.1 → NP_001412766.1 acyl-protein thioesterase 1 isoform 7

Status: REVIEWED

Source sequence(s)

AC100821

UniProtKB/TrEMBL

E5RGR0

Related

ENSP00000428729.1, ENST00000518546.5
NM_006330.4 → NP_006321.1 acyl-protein thioesterase 1 isoform 1

See identical proteins and their annotated locations for NP_006321.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (1).

Source sequence(s)

AA827237, AF035293, AF052112

Consensus CDS

CCDS6157.1

UniProtKB/Swiss-Prot

O43202, O75608, Q9UQF9

UniProtKB/TrEMBL

B4DJV9, Q6IAQ1

Related

ENSP00000320043.3, ENST00000316963.8

Conserved Domains (1) summary

pfam02230
Location:11 → 226

Abhydrolase_2; Phospholipase/Carboxylesterase