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LIPI lipase I [ Homo sapiens (human) ]

Gene ID: 149998, updated on 8-Dec-2018

Summary

Official Symbol
LIPIprovided by HGNC
Official Full Name
lipase Iprovided by HGNC
Primary source
HGNC:HGNC:18821
See related
Ensembl:ENSG00000188992 MIM:609252
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
CT17; LPDL; PLA1C; PRED5; mPA-PLA1 beta
Summary
The protein encoded by this gene is a phospholipase that hydrolyzes phosphatidic acid to produce lysophosphatidic acid. Defects in this gene are a cause of susceptibility to familial hypertrigliceridemia. This gene is also expressed at high levels in Ewing family tumor cells. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]
Expression
Biased expression in thyroid (RPKM 1.4), endometrium (RPKM 0.3) and 2 other tissues See more
Orthologs

Genomic context

See LIPI in Genome Data Viewer
Location:
21q11.2
Exon count:
12
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 21 NC_000021.9 (14108813..14210953, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 21 NC_000021.8 (15480784..15583361, complement)

Chromosome 21 - NC_000021.9Genomic Context describing neighboring genes Neighboring gene ankyrin repeat domain 20 family member A18, pseudogene Neighboring gene RNA, 5S ribosomal pseudogene 488 Neighboring gene endoplasmic reticulum lectin 1 pseudogene 1 Neighboring gene RNA binding motif protein 11 Neighboring gene ATP binding cassette subfamily C member 13 (pseudogene)

Genomic regions, transcripts, and products

Expression

  • 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 Jun 15 11:32:44 2016

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Pathways from BioSystems

  • Digestion of dietary lipid, organism-specific biosystem (from REACTOME)
    Digestion of dietary lipid, organism-specific biosystemDietary lipids such as long-chain triacylglycerols and cholesterol esters are digested in the stomach and small intestine to yield long-chain fatty acids, monoacylglycerols, glycerol and cholesterol ...
  • Lipid digestion, mobilization, and transport, organism-specific biosystem (from REACTOME)
    Lipid digestion, mobilization, and transport, organism-specific biosystemProcesses annotated here include the digestion of dietary lipids, sterol uptake, the formation and turnover of lipoproteins (chylomicrons, VLDL, LDL, and HDL), and the mobilization of fatty acids thr...
  • Metabolism, organism-specific biosystem (from REACTOME)
    Metabolism, organism-specific biosystemMetabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as th...
  • Metabolism of lipids and lipoproteins, organism-specific biosystem (from REACTOME)
    Metabolism of lipids and lipoproteins, organism-specific biosystemLipids are hydrophobic but otherwise chemically diverse molecules that play a wide variety of roles in human biology. They include ketone bodies, fatty acids, triacylglycerols, phospholipids and sphi...

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
carboxylic ester hydrolase activity IEA
Inferred from Electronic Annotation
more info
 
heparin binding IDA
Inferred from Direct Assay
more info
PubMed 
phospholipase activity IDA
Inferred from Direct Assay
more info
PubMed 
phospholipase activity TAS
Traceable Author Statement
more info
 
Process Evidence Code Pubs
lipid catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
phosphatidic acid biosynthetic process TAS
Traceable Author Statement
more info
 
Component Evidence Code Pubs
extracellular region IEA
Inferred from Electronic Annotation
more info
 
plasma membrane TAS
Traceable Author Statement
more info
 

General protein information

Preferred Names
lipase member I
Names
LPD lipase
cancer/testis antigen 17
lipase, member I
membrane-associated phosphatidic acid-selective phospholipase A1-beta
NP_001289927.1
NP_001289928.1
NP_001289929.1
NP_001289930.1
NP_945347.2
XP_006724028.1

NCBI Reference Sequences (RefSeq)

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

  1. NG_021434.2 RefSeqGene

    Range
    4985..103121
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001302998.1NP_001289927.1  lipase member I isoform 1 precursor

    Status: REVIEWED

    Description
    Transcript Variant: This variant (fl) encodes isoform 1.
    Source sequence(s)
    AY197607, AY918476, JN387910
    UniProtKB/Swiss-Prot
    Q6XZB0
    UniProtKB/TrEMBL
    Q5D1Q2
    Related
    ENSP00000440381.2, ENST00000536861.5
    Conserved Domains (1) summary
    cd00707
    Location:41309
    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 ...
  2. NM_001302999.1NP_001289928.1  lipase member I isoform 2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (deltaE5) lacks an alternate in-frame exon, compared to variant fl. The encoded isoform (2) is shorter than isoform 1.
    Source sequence(s)
    AY197607, AY918476, JN387913
    UniProtKB/Swiss-Prot
    Q6XZB0
    UniProtKB/TrEMBL
    Q5D1Q2
    Related
    ENSP00000482652.1, ENST00000614229.4
    Conserved Domains (2) summary
    cd00707
    Location:41279
    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 ...
    pfam00151
    Location:14304
    Lipase; Lipase
  3. NM_001303000.1NP_001289929.1  lipase member I isoform 3 precursor

    Status: REVIEWED

    Description
    Transcript Variant: This variant (deltaE7.2) uses an alternate in-frame splice site, compared to variant fl. The encoded isoform (3) is shorter than isoform 1.
    Source sequence(s)
    AY197607, AY918476, JN387915
    UniProtKB/Swiss-Prot
    Q6XZB0
    UniProtKB/TrEMBL
    Q5D1Q2
    Conserved Domains (2) summary
    cd00707
    Location:41330
    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 ...
    pfam00151
    Location:14330
    Lipase; Lipase
  4. NM_001303001.1NP_001289930.1  lipase member I isoform 4

    Status: REVIEWED

    Description
    Transcript Variant: This variant (deltaE8-9) lacks two alternate in-frame exons, compared to variant fl. The encoded isoform (4) is shorter than isoform 1.
    Source sequence(s)
    AY197607, AY918476, JN387916
    UniProtKB/Swiss-Prot
    Q6XZB0
    UniProtKB/TrEMBL
    Q5D1Q2
    Conserved Domains (2) summary
    cd00707
    Location:41309
    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 ...
    pfam00151
    Location:14334
    Lipase; Lipase
  5. NM_198996.3NP_945347.2  lipase member I isoform 5

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) differs in the 5' UTR, lacks a portion of the 5' coding region, and initiates translation at an alternate start codon, compared to variant fl. The encoded isoform (5) has a distinct N-terminus and is longer than isoform 1.
    Source sequence(s)
    AI017218, AY197607, AY918476, BI460152
    Consensus CDS
    CCDS13564.1
    UniProtKB/Swiss-Prot
    Q6XZB0
    UniProtKB/TrEMBL
    Q5D1Q2
    Related
    ENSP00000343331.2, ENST00000344577.6
    Conserved Domains (2) summary
    cd00707
    Location:62330
    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 ...
    pfam00151
    Location:26355
    Lipase; Lipase

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109 details...Open this link in a new tab

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

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000021.9 Reference GRCh38.p12 Primary Assembly

    Range
    14108813..14210953 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_006723965.3XP_006724028.1  lipase member I isoform X1

    Conserved Domains (2) summary
    cd00707
    Location:70338
    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 ...
    pfam00151
    Location:43363
    Lipase; Lipase

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_145317.1: Suppressed sequence

    Description
    NM_145317.1: This RefSeq was permanently suppressed because it was created in error.
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