PNLIP
Pancreatic triacylglycerol lipase
Also known as: LIPP_HUMAN, PL
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P16233
- Gene
- PNLIP
- Ensembl
- ENSG00000175535
- Chromosome
- 10
- Canonical length
- 465 aa
- Protein class
- Disease related genes, Enzymes, FDA approved drug targets, Human disease related genes, Metabolic proteins, Plasma proteins, Predicted secreted proteins
- Secretome location
- Secreted to digestive system
OverviewNCBI Gene
This gene encodes a member of the lipase family of proteins. The encoded enzyme is secreted by the pancreas and hydrolyzes triglycerides in the small intestine, and is essential for the efficient digestion of dietary fats. Inhibition of the encoded enzyme may prevent high-fat diet-induced obesity in mice and result in weight loss in human patients with obesity. Mutations in this gene cause congenital pancreatic lipase deficiency, a rare disorder characterized by steatorrhea. [provided by RefSeq, Jul 2016]
Canonical amino-acid sequenceUniProt
465 residues, UniProt reviewed canonical sequence.
>P16233|PNLIP
1 MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD VNTRFLLYTN
61 ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLANVCKNL FKVESVNCIC
121 VDWKGGSRTG YTQASQNIRI VGAEVAYFVE FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR
181 RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH
241 LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF
301 PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS
361 VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQMVKFIWY
421 NNVINPTLPR VGASKIIVET NVGKQFNFCS PETVREEVLL TLTPCLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PNLIP 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)
- 0.23
- Highest tissue expression
- 419,356 nTPM
Expression across tissuesHPA
Tissue
- pancreas: 419,356 nTPM
- ovary: 87 nTPM
- heart muscle: 73 nTPM
- salivary gland: 68 nTPM
- duodenum: 61 nTPM
- small intestine: 32 nTPM
Single-cell type
- pancreatic acinar cells: 41,200 nCPM
- pancreatic duct cells: 210 nCPM
- monocytes: 37 nCPM
- pancreatic islet cells: 18 nCPM
- mast cells: 11 nCPM
- macrophages: 7 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- amygdala: 0 nTPM
- basal ganglia: 0 nTPM
- cerebellum: 0 nTPM
- cerebral cortex: 0 nTPM
- choroid plexus: 0 nTPM
- hippocampal formation: 0 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about PNLIP.
Disease | AllUniProt
Conditions PNLIP is implicated in, by any mechanism.
- Pancreatic lipase deficiency (PNLIPD) MIM:614338
Disease | GeneticClinVar
18 pathogenic / likely-pathogenic of 277 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Pancreatic triacylglycerol lipase deficiency
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)
- 0.99
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.44
- DepMap mean gene effect
- 0.08
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 1% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cholesterol homeostasis
- fatty acid biosynthetic process
- high-density lipoprotein particle remodeling
- intestinal cholesterol absorption
- lipid metabolic process
- triglyceride catabolic process
- positive regulation of triglyceride lipase activity
Molecular functions
- all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity
- lipase activity
- lipoprotein lipase activity
- metal ion binding
- phospholipase A1 activity
- triacylglycerol lipase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PNLIP as an antibody target. Whether an autoantibody or antibody against PNLIP could matter depends on whether native PNLIP is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PNLIP is annotated as secreted, so native PNLIP 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 PNLIP as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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