LIPF
Gastric triacylglycerol lipase
Also known as: HGL, HLAL, LIPF_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P07098
- Gene
- LIPF
- Ensembl
- ENSG00000182333
- Chromosome
- 10
- Canonical length
- 398 aa
- Protein class
- Enzymes, FDA approved drug targets, Metabolic proteins, Predicted secreted proteins
- Secretome location
- Secreted to digestive system
OverviewNCBI Gene
This gene encodes gastric lipase, an enzyme involved in the digestion of dietary triglycerides in the gastrointestinal tract, and responsible for 30% of fat digestion processes occurring in human. It is secreted by gastric chief cells in the fundic mucosa of the stomach, and it hydrolyzes the ester bonds of triglycerides under acidic pH conditions. The gene is a member of a conserved gene family of lipases that play distinct roles in neutral lipid metabolism. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]
Canonical amino-acid sequenceUniProt
398 residues, UniProt reviewed canonical sequence.
>P07098|LIPF
1 MWLLLTMASL ISVLGTTHGL FGKLHPGSPE VTMNISQMIT YWGYPNEEYE VVTEDGYILE
61 VNRIPYGKKN SGNTGQRPVV FLQHGLLASA TNWISNLPNN SLAFILADAG YDVWLGNSRG
121 NTWARRNLYY SPDSVEFWAF SFDEMAKYDL PATIDFIVKK TGQKQLHYVG HSQGTTIGFI
181 AFSTNPSLAK RIKTFYALAP VATVKYTKSL INKLRFVPQS LFKFIFGDKI FYPHNFFDQF
241 LATEVCSREM LNLLCSNALF IICGFDSKNF NTSRLDVYLS HNPAGTSVQN MFHWTQAVKS
301 GKFQAYDWGS PVQNRMHYDQ SQPPYYNVTA MNVPIAVWNG GKDLLADPQD VGLLLPKLPN
361 LIYHKEIPFY NHLDFIWAMD APQEVYNDIV SMISEDKKLocalizationUniProt · AlphaFold · HPA
Whether an antibody against LIPF 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)
- 0.24
- Highest tissue expression
- 35,390 nTPM
Expression across tissuesHPA
Tissue
- stomach: 35,390 nTPM
- duodenum: 247 nTPM
- esophagus: 99 nTPM
- kidney: 11 nTPM
- cerebral cortex: 11 nTPM
- colon: 8 nTPM
Single-cell type
- gastric chief cells: 139,374 nCPM
- parietal cells: 42,347 nCPM
- mucous neck cells: 29,153 nCPM
- foveolar cells: 1,825 nCPM
- neuroendocrine cells: 1,460 nCPM
- submucosal glandular cells: 111 nCPM
Immune cell
- eosinophil: 0.1 nTPM
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- medulla oblongata: 0.6 nTPM
- midbrain: 0.3 nTPM
- cerebellum: 0.2 nTPM
- amygdala: 0.1 nTPM
- choroid plexus: 0.1 nTPM
- hippocampal formation: 0.1 nTPM
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)
- 0.82
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.42
- DepMap mean gene effect
- -0.05
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- lipid catabolic process
- lipid metabolic process
- malate metabolic process
- triglyceride metabolic process
Molecular functions
- lipid binding
- triacylglycerol lipase activity
- malate dehydrogenase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads LIPF as an antibody target. Whether an autoantibody or antibody against LIPF could matter depends on whether native LIPF is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
LIPF is annotated as secreted, so native LIPF 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 LIPF as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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