P19835 · CEL_HUMAN
- ProteinBile salt-activated lipase
- GeneCEL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids753 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFAs) (PubMed:10220579, PubMed:27509211, PubMed:27650499, PubMed:8471055).
Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity).
Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (PubMed:10220579, PubMed:27509211, PubMed:27650499, PubMed:8471055).
Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity).
Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (PubMed:10220579, PubMed:27509211, PubMed:27650499, PubMed:8471055).
Catalytic activity
- a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+This reaction proceeds in the forward direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+This reaction proceeds in the forward direction.
- 1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H+ + octanoateThis reaction proceeds in the forward direction.
- cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H+This reaction proceeds in the forward direction.
- a butanoate ester + H2O = an aliphatic alcohol + butanoate + H+This reaction proceeds in the forward direction.
- 9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 9-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholineThis reaction proceeds in the forward direction.
- 12-hexadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 12-hydroxyoctadecanoate + H+This reaction proceeds in the forward direction.
- 13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 13-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 9-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H+This reaction proceeds in the forward direction.
- 13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 13-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 12-octadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 13-octadecanoyloxy-octadecanoate + H2O = 13-hydroxy-octadecanoate + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 5-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 5-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 9-octadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H+ + octadecanoateThis reaction proceeds in the forward direction.
Activity regulation
Activated by bile salts such as sodium taurocholate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
24 μM | lipoyl-4-aminobenzoate | |||||
15 μM | triacetin |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
45.5 pmol/min/mg | toward lipoyl-4-aminobenzoate | ||||
323 pmol/min/mg | toward triacetin |
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 214 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Active site | 340 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 455 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | acetylesterase activity | |
Molecular Function | catalytic activity | |
Molecular Function | heparin binding | |
Molecular Function | hydrolase activity | |
Molecular Function | retinyl-palmitate esterase activity | |
Molecular Function | sterol esterase activity | |
Molecular Function | triglyceride lipase activity | |
Biological Process | ceramide catabolic process | |
Biological Process | intestinal cholesterol absorption | |
Biological Process | lipid metabolic process | |
Biological Process | pancreatic juice secretion |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameBile salt-activated lipase
- EC number
- Short namesBAL
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP19835
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Maturity-onset diabetes of the young 8 with exocrine dysfunction (MODY8)
- Note
- DescriptionAn autosomal dominant form of diabetes characterized by a primary defect in insulin secretion, exocrine pancreatic dysfunction, altered pancreatic morphology, recurrent abdominal pain, and fecal elastase deficiency. Disease onset is at less than 25 years of age.
- See alsoMIM:609812
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 455 | Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold. | ||||
Sequence: H → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 993 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MGRLQLVVLGLTCCWAVASA | ||||||
Chain | PRO_0000008631 | 21-753 | Bile salt-activated lipase | |||
Sequence: AKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPVMIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQSGVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYPMLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVTEEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIALAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTVSKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLRYWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF | ||||||
Disulfide bond | 84↔100 | |||||
Sequence: CLQATITQDSTYGDEDC | ||||||
Glycosylation | CAR_000141 | 207 | N-linked (GlcNAc...) (complex) asparagine | |||
Sequence: N | ||||||
Disulfide bond | 266↔277 | |||||
Sequence: CPVGDAARMAQC | ||||||
Glycosylation | 558 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 569 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 579 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 607 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 618 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 629 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 640 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 651 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 662 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 673 | O-linked (GalNAc...) threonine | ||||
Sequence: T |
Post-translational modification
N- and O-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 21-121 | Heparin-binding | ||||
Sequence: AKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPVM | ||||||
Region | 555-753 | Disordered | ||||
Sequence: QEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF | ||||||
Repeat | 559-569 | 1 | ||||
Sequence: PVPPTGDSEAT | ||||||
Region | 559-745 | 17 X 11 AA tandem repeats, glycodomain, O-linked (mucin type) | ||||
Sequence: PVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDSEAAPVPPTDDSKEA | ||||||
Repeat | 570-580 | 2 | ||||
Sequence: PVPPTGDSETA | ||||||
Repeat | 581-591 | 3 | ||||
Sequence: PVPPTGDSGAP | ||||||
Compositional bias | 585-700 | Pro residues | ||||
Sequence: TGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGA | ||||||
Repeat | 592-602 | 4 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 603-613 | 5 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 614-624 | 6 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 625-635 | 7 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 636-646 | 8 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 647-657 | 9 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 658-668 | 10 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 669-679 | 11 | ||||
Sequence: PVPPTGDAGPP | ||||||
Repeat | 680-690 | 12 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 691-701 | 13 | ||||
Sequence: PVPPTGDSGAP | ||||||
Repeat | 702-712 | 14 | ||||
Sequence: PVTPTGDSETA | ||||||
Repeat | 713-723 | 15 | ||||
Sequence: PVPPTGDSGAP | ||||||
Compositional bias | 717-733 | Pro residues | ||||
Sequence: TGDSGAPPVPPTGDSEA | ||||||
Repeat | 724-734 | 16 | ||||
Sequence: PVPPTGDSEAA | ||||||
Repeat | 735-745 | 17 | ||||
Sequence: PVPPTDDSKEA |
Sequence similarities
Belongs to the type-B carboxylesterase/lipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P19835-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameLong
- Length753
- Mass (Da)79,322
- Last updated2009-07-07 v3
- ChecksumB3253789D1EABF7F
P19835-2
- NameShort
- Differences from canonical
- 430-495: Missing
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 73 | in Ref. 9; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 235 | in Ref. 5; AAB35488 | ||||
Sequence: R → A | ||||||
Sequence conflict | 284-288 | in Ref. 5; AAB35488 | ||||
Sequence: RALTL → AAVTV | ||||||
Sequence conflict | 313 | in Ref. 5; AAB35488 | ||||
Sequence: G → E | ||||||
Sequence conflict | 403 | in Ref. 5; AAB35488 | ||||
Sequence: T → I | ||||||
Alternative sequence | VSP_001463 | 430-495 | in isoform Short | |||
Sequence: Missing | ||||||
Sequence conflict | 481 | in Ref. 5; AAB35488 | ||||
Sequence: S → F | ||||||
Compositional bias | 585-700 | Pro residues | ||||
Sequence: TGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGA | ||||||
Sequence conflict | 689 | in Ref. 5; AAB35488 | ||||
Sequence: A → P | ||||||
Compositional bias | 717-733 | Pro residues | ||||
Sequence: TGDSGAPPVPPTGDSEA |
Polymorphism
The variable number of tandem repeats (VNTR)-region in exon 11 is highly polymorphic, and VNTR number varies between 3 and 23. The most common allele contains 16 repeats (PubMed:12166660, PubMed:16369531, PubMed:19760265).
Some alleles contain common single base insertions in the VNTR region that are predicted to lead to protein truncation and may be associated with an increased risk of exocrine pancreatic dysfunction in autoimmune diabetes (PubMed:16369531).
Some alleles contain common single base insertions in the VNTR region that are predicted to lead to protein truncation and may be associated with an increased risk of exocrine pancreatic dysfunction in autoimmune diabetes (PubMed:16369531).
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54457 EMBL· GenBank· DDBJ | CAA38325.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
M85201 EMBL· GenBank· DDBJ | AAA52014.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
M54994 EMBL· GenBank· DDBJ | AAA63211.1 EMBL· GenBank· DDBJ | mRNA | ||
M94579 EMBL· GenBank· DDBJ | AAA51973.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
S79774 EMBL· GenBank· DDBJ | AAB35488.2 EMBL· GenBank· DDBJ | mRNA | ||
AF072711 EMBL· GenBank· DDBJ | AAC26514.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AL162417 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471090 EMBL· GenBank· DDBJ | EAW88033.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |