LIPC
Hepatic triacylglycerol lipase
Also known as: HL, HTGL, LIPC_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P11150
- Gene
- LIPC
- Ensembl
- ENSG00000166035
- Chromosome
- 15
- Canonical length
- 499 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted secreted proteins
- Secretome location
- Secreted to blood
- Quaternary structure
- Homodimer
OverviewNCBI Gene
Enables phospholipase A1 activity and triacylglycerol lipase activity. Involved in several processes, including cholesterol homeostasis; plasma lipoprotein particle remodeling; and triglyceride catabolic process. Located in extracellular space. Implicated in several diseases, including Alzheimer's disease; coronary artery disease; familial combined hyperlipidemia; peripheral vascular disease; and type 2 diabetes mellitus. Biomarker of hyperinsulinism; obesity; and type 1 diabetes mellitus. [provided by Alliance of Genome Resources, Jul 2025]
Canonical amino-acid sequenceUniProt
499 residues, UniProt reviewed canonical sequence.
>P11150|LIPC
1 MDTSPLCFSI LLVLCIFIQS SALGQSLKPE PFGRRAQAVE TNKTLHEMKT RFLLFGETNQ
61 GCQIRINHPD TLQECGFNSS LPLVMIIHGW SVDGVLENWI WQMVAALKSQ PAQPVNVGLV
121 DWITLAHDHY TIAVRNTRLV GKEVAALLRW LEESVQLSRS HVHLIGYSLG AHVSGFAGSS
181 IGGTHKIGRI TGLDAAGPLF EGSAPSNRLS PDDANFVDAI HTFTREHMGL SVGIKQPIGH
241 YDFYPNGGSF QPGCHFLELY RHIAQHGFNA ITQTIKCSHE RSVHLFIDSL LHAGTQSMAY
301 PCGDMNSFSQ GLCLSCKKGR CNTLGYHVRQ EPRSKSKRLF LVTRAQSPFK VYHYQFKIQF
361 INQTETPIQT TFTMSLLGTK EKMQKIPITL GKGIASNKTY SFLITLDVDI GELIMIKFKW
421 ENSAVWANVW DTVQTIIPWS TGPRHSGLVL KTIRVKAGET QQRMTFCSEN TDDLLLRPTQ
481 EKIFVKCEIK SKTSKRKIRLocalizationUniProt · AlphaFold · HPA
Whether an antibody against LIPC can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.29
- Highest tissue expression
- 160 nTPM
Expression across tissuesHPA
Tissue
- liver: 160 nTPM
- kidney: 5.6 nTPM
- pancreas: 2.3 nTPM
- thymus: 2 nTPM
- spinal cord: 1.9 nTPM
- duodenum: 1.7 nTPM
Single-cell type
- hepatocytes: 303 nCPM
- papillary tip epithelial cells: 89 nCPM
- renal collecting duct principal cells: 77 nCPM
- microglia: 70 nCPM
- loop of henle epithelial cells: 48 nCPM
- renal connecting tubule cells: 43 nCPM
Immune cell
- MAIT T-cell: 1.8 nTPM
- basophil: 1.7 nTPM
- NK-cell: 1.5 nTPM
- gdT-cell: 1.3 nTPM
- naive CD8 T-cell: 1.3 nTPM
- total PBMC: 1.1 nTPM
Brain region
- white matter: 3.6 nTPM
- pons: 3.4 nTPM
- cerebral cortex: 3.1 nTPM
- cerebellum: 2.9 nTPM
- medulla oblongata: 2.9 nTPM
- midbrain: 2.8 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about LIPC.
Disease | AllUniProt
Conditions LIPC is implicated in, by any mechanism.
- Hepatic lipase deficiency (HL deficiency) MIM:614025
Disease | GeneticClinVar
4 pathogenic / likely-pathogenic of 349 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Hyperlipidemia due to hepatic triglyceride lipase deficiency
- Abnormal circulating lipid concentration
- Cervical cancer
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.93
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.92
- DepMap mean gene effect
- 0.1
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cholesterol homeostasis
- cholesterol metabolic process
- chylomicron remnant clearance
- fatty acid biosynthetic process
- high-density lipoprotein particle remodeling
- low-density lipoprotein particle remodeling
- phosphatidylcholine catabolic process
- reverse cholesterol transport
- triglyceride catabolic process
- triglyceride homeostasis
- very-low-density lipoprotein particle remodeling
- intermediate-density lipoprotein particle remodeling
Molecular functions
- apolipoprotein binding
- heparin binding
- lipoprotein lipase activity
- low-density lipoprotein particle binding
- phosphatidylcholine lysophospholipase activity
- phospholipase A1 activity
- phospholipase activity
- triacylglycerol lipase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads LIPC as an antibody target. Whether an autoantibody or antibody against LIPC could matter depends on whether native LIPC is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
LIPC is annotated as secreted, so native LIPC circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label LIPC as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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