LIPH lipase H [Homo sapiens (human)] - Gene

Summary

Official Symbol: LIPHprovided by HGNC
Official Full Name: lipase Hprovided by HGNC
Primary source: HGNC:HGNC:18483
See related: Ensembl:ENSG00000163898 MIM:607365; AllianceGenome:HGNC:18483
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: AH; LAH2; ARWH2; HYPT7; LPDLR; PLA1B; mPA-PLA1
Summary: This gene encodes a membrane-bound member of the mammalian triglyceride lipase family. It catalyzes the production of 2-acyl lysophosphatidic acid (LPA), which is a lipid mediator with diverse biological properties that include platelet aggregation, smooth muscle contraction, and stimulation of cell proliferation and motility. [provided by RefSeq, Jul 2008]
Expression: Biased expression in colon (RPKM 18.6), stomach (RPKM 18.4) and 12 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 3q27.2

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	3	NC_000003.12 (185506262..185552588, complement)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	3	NC_060927.1 (188322024..188368409, complement)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	3	NC_000003.11 (185224050..185270376, complement)

Chromosome 3 - NC_000003.12 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
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?

Circular RNA eukaryotic translation initiation factor 6 facilitates TPC-1 cell proliferation and invasion through the microRNA-138-5p/lipase H axis.
Title: Circular RNA eukaryotic translation initiation factor 6 facilitates TPC-1 cell proliferation and invasion through the microRNA-138-5p/lipase H axis.
Identification of LIPH as an unfavorable biomarkers correlated with immune suppression or evasion in pancreatic cancer based on RNA-seq.
Title: Identification of LIPH as an unfavorable biomarkers correlated with immune suppression or evasion in pancreatic cancer based on RNA-seq.
LIPH promotes metastasis by enriching stem-like cells in triple-negative breast cancer.
Title: LIPH promotes metastasis by enriching stem-like cells in triple-negative breast cancer.
High LIPH expression is associated with Coronary Artery Disease.
Title: Serum Triglyceride Lipase Concentrations are Independent Risk Factors for Coronary Artery Disease and In-Stent Restenosis.
Study analyzed a Japanese family with autosomal recessive woolly hair and identified a novel splice site mutation c.982+2T>A; +7_+21del in the LIPH gene, which caused skipping of exon 7 in cultured cells.
Title: Identification of a novel splice site mutation in the LIPH gene in a Japanese family with autosomal recessive woolly hair.
Two mutants of LIPH lead to secretion defects of LIPH, which are involved in the pathogenesis of Autosomal recessive woolly hair/hypotrichosis.
Title: Novel mutations in the lipase H gene lead to secretion defects of LIPH in Chinese patients with autosomal recessive woolly hair/hypotrichosis (ARWH/HT).
Novel sequence variants in the LIPH and LPAR6 genes underlies autosomal recessive woolly hair/hypotrichosis in three consanguineous Pakistani families.
Title: Novel sequence variants in the LIPH and LPAR6 genes underlies autosomal recessive woolly hair/hypotrichosis in consanguineous families.
The present study shows 93% of Japanese patients with ARWH had at least one of the two founder mutations in exon 6 of LIPH. Highly prevalent founder mutations in LIPH.
Title: Mutational analysis of 29 patients with autosomal-recessive woolly hair and hypotrichosis: LIPH mutations are extremely predominant in autosomal-recessive woolly hair and hypotrichosis in Japan.
The authors report no apparent decrease in total hair count but remarkable miniaturization and increased telogen/anagen hair ratio in patients homozygous mutations in LIPH.
Title: Identification of factors contributing to phenotypic divergence via quantitative image analyses of autosomal recessive woolly hair/hypotrichosis with homozygous c.736T>A LIPH mutation.
This meta-analysis demonstrates that the T allele in the LIPC rs493258 polymorphism was significantly associated with the risk of any and late age related macular degeneration
Title: The Association between LIPC rs493258 Polymorphism and the Susceptibility to Age-Related Macular Degeneration.

Submit: New GeneRIF Correction See all GeneRIFs (41)

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

Associated conditions

Description	Tests
Hypotrichosis 7 MedGen: C1836672 OMIM: 604379 GeneReviews: Not available	Compare labs

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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Markers

D3S1602 (e-PCR), detects polymorphism
- UniSTS:12095

D3S2314 (e-PCR), detects polymorphism
- UniSTS:15487

D3S3592 (e-PCR), detects polymorphism
- UniSTS:47786

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables carboxylic ester hydrolase activity	IEA Inferred from Electronic Annotation more info
enables heparin binding	IDA Inferred from Direct Assay more info	PubMed
enables phospholipase activity	IBA Inferred from Biological aspect of Ancestor more info
enables phospholipase activity	IDA Inferred from Direct Assay more info	PubMed
enables phospholipase activity	TAS Traceable Author Statement more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in lipid catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in lipid catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in phosphatidic acid biosynthetic process	TAS Traceable Author Statement more info

Component	Evidence Code	Pubs
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: lipase member H

Names: LPD lipase-related protein; lipase, member H; mPA-PLA1 alpha; membrane-associated phosphatidic acid-selective phospholipase A1-alpha; membrane-bound phosphatidic acid-selective phospholipase A1; phospholipase A(1); phospholipase A1 member B

NP_640341.1

EC 2.7.11.30

XP_006713592.1

EC 2.7.11.30

XP_011510832.1

EC 2.7.11.30

XP_016861341.1

EC 2.7.11.30

XP_054201593.1

EC 2.7.11.30

XP_054201594.1

EC 2.7.11.30

XP_054201595.1

EC 2.7.11.30

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.

Genomic

NG_012183.1 RefSeqGene

Range

4994..51320

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_139248.3 → NP_640341.1 lipase member H precursor

See identical proteins and their annotated locations for NP_640341.1

Status: REVIEWED

Source sequence(s)

AC099661, AK122651, BC064941, BI965988

Consensus CDS

CCDS3272.1

UniProtKB/Swiss-Prot

A2IBA7, Q8TEC7, Q8WWY8

UniProtKB/TrEMBL

B4DPK4

Related

ENSP00000296252.4, ENST00000296252.9

Conserved Domains (1) summary

cd00707
Location:39 → 303

Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2023_10

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

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000003.12 Reference GRCh38.p14 Primary Assembly

Range

185506262..185552588 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_017005852.3 → XP_016861341.1 lipase member H isoform X2

UniProtKB/TrEMBL

A2IBA6, B4DPK4

Related

ENSP00000396384.2, ENST00000424591.6

Conserved Domains (1) summary

cd00707
Location:39 → 269

Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...
XM_006713529.5 → XP_006713592.1 lipase member H isoform X1

UniProtKB/TrEMBL

B4DPK4

Conserved Domains (1) summary

cd00707
Location:39 → 273

Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...
XM_011512530.4 → XP_011510832.1 lipase member H isoform X3

See identical proteins and their annotated locations for XP_011510832.1

UniProtKB/TrEMBL

B4DPK4

Conserved Domains (1) summary

cd00707
Location:1 → 260

Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...