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Protein

Bile salt-activated lipase

Gene

CEL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication
A steryl ester + H2O = a sterol + a fatty acid.1 Publication

Enzyme regulationi

Activated by bile salts containing a 7-hydroxyl group.

Kineticsi

  1. KM=24 µM for lipoyl-4-aminobenzoate1 Publication
  2. KM=15 µM for triacetin1 Publication
  1. Vmax=45.5 pmol/min/mg enzyme toward lipoyl-4-aminobenzoate1 Publication
  2. Vmax=323 pmol/min/mg enzyme toward triacetin1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei214Acyl-ester intermediatePROSITE-ProRule annotation1 Publication1
Active sitei340Charge relay system1 Publication1
Active sitei455Charge relay system1 Publication1

GO - Molecular functioni

  • acylglycerol lipase activity Source: Reactome
  • carboxylic ester hydrolase activity Source: GO_Central
  • catalytic activity Source: UniProtKB
  • heparin binding Source: UniProtKB
  • hydrolase activity Source: UniProtKB
  • neurexin family protein binding Source: GO_Central
  • receptor activity Source: GO_Central
  • sterol esterase activity Source: UniProtKB
  • triglyceride lipase activity Source: UniProtKB

GO - Biological processi

  • cholesterol catabolic process Source: UniProtKB
  • fatty acid catabolic process Source: UniProtKB
  • intestinal cholesterol absorption Source: UniProtKB
  • intestinal lipid catabolic process Source: UniProtKB
  • lipid digestion Source: Reactome
  • lipid metabolic process Source: UniProtKB
  • modulation of synaptic transmission Source: GO_Central
  • neuron cell-cell adhesion Source: GO_Central
  • pancreatic juice secretion Source: UniProtKB
  • protein esterification Source: UniProtKB
  • synapse assembly Source: GO_Central
  • triglyceride metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciZFISH:HS10190-MONOMER.
ReactomeiR-HSA-192456. Digestion of dietary lipid.
SABIO-RKP19835.

Protein family/group databases

ESTHERihuman-CEL. Cholesterol_esterase.
MEROPSiS09.985.

Chemistry databases

SwissLipidsiSLP:000000874.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile salt-activated lipase (EC:3.1.1.13, EC:3.1.1.3)
Short name:
BAL
Alternative name(s):
Bile salt-stimulated lipase
Short name:
BSSL
Bucelipase
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase
Gene namesi
Name:CEL
Synonyms:BAL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:1848. CEL.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: GO_Central
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
  • synapse Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Maturity-onset diabetes of the young 8 with exocrine dysfunction (MODY8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. The disease can be caused by frameshift deletions in the variable number of tandem repeats (VNTR)-containing exon 11 of the CEL gene (PubMed:16369531).1 Publication
Disease descriptionA form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.
See also OMIM:609812

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi455H → Q: Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold. 1 Publication1

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

DisGeNETi1056.
MalaCardsiCEL.
MIMi606391. phenotype.
609812. phenotype.
Orphaneti552. MODY.
PharmGKBiPA26391.

Chemistry databases

ChEMBLiCHEMBL3219.

Polymorphism and mutation databases

DMDMi251757481.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000000863121 – 753Bile salt-activated lipaseAdd BLAST733

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi84 ↔ 100
GlycosylationiCAR_000141207N-linked (GlcNAc...) (complex)1
Disulfide bondi266 ↔ 277
Glycosylationi558O-linked (GalNAc...)1 Publication1
Glycosylationi569O-linked (GalNAc...)1 Publication1
Glycosylationi579O-linked (GalNAc...)1 Publication1
Glycosylationi607O-linked (GalNAc...)1 Publication1
Glycosylationi618O-linked (GalNAc...)1 Publication1
Glycosylationi629O-linked (GalNAc...)1 Publication1
Glycosylationi640O-linked (GalNAc...)1 Publication1
Glycosylationi651O-linked (GalNAc...)1 Publication1
Glycosylationi662O-linked (GalNAc...)1 Publication1
Glycosylationi673O-linked (GalNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP19835.
PeptideAtlasiP19835.
PRIDEiP19835.

PTM databases

iPTMnetiP19835.
PhosphoSitePlusiP19835.
UniCarbKBiP19835.

Expressioni

Tissue specificityi

Mammary gland and pancreas. Expressed by eosinophils.1 Publication

Gene expression databases

BgeeiENSG00000170835.
CleanExiHS_CEL.

Organism-specific databases

HPAiHPA008023.
HPA052701.

Interactioni

Subunit structurei

Interacts with CLC.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP19835. 1 interactor.
STRINGi9606.ENSP00000361151.

Chemistry databases

BindingDBiP19835.

Structurei

Secondary structure

1753
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 28Combined sources4
Beta strandi31 – 34Combined sources4
Beta strandi36 – 39Combined sources4
Beta strandi41 – 44Combined sources4
Beta strandi46 – 54Combined sources9
Beta strandi72 – 76Combined sources5
Beta strandi84 – 87Combined sources4
Beta strandi91 – 98Combined sources8
Beta strandi102 – 109Combined sources8
Beta strandi111 – 113Combined sources3
Beta strandi117 – 124Combined sources8
Turni128 – 130Combined sources3
Beta strandi137 – 139Combined sources3
Beta strandi142 – 145Combined sources4
Helixi148 – 154Combined sources7
Beta strandi157 – 161Combined sources5
Helixi166 – 170Combined sources5
Beta strandi174 – 178Combined sources5
Helixi182 – 197Combined sources16
Turni198 – 202Combined sources5
Beta strandi203 – 213Combined sources11
Helixi215 – 225Combined sources11
Helixi227 – 229Combined sources3
Turni230 – 232Combined sources3
Beta strandi234 – 240Combined sources7
Turni246 – 248Combined sources3
Helixi253 – 264Combined sources12
Helixi271 – 280Combined sources10
Helixi283 – 288Combined sources6
Helixi302 – 304Combined sources3
Beta strandi313 – 316Combined sources4
Helixi320 – 322Combined sources3
Helixi324 – 327Combined sources4
Beta strandi330 – 337Combined sources8
Turni338 – 341Combined sources4
Helixi342 – 348Combined sources7
Helixi350 – 353Combined sources4
Beta strandi355 – 357Combined sources3
Helixi361 – 371Combined sources11
Helixi376 – 388Combined sources13
Turni398 – 401Combined sources4
Helixi402 – 412Combined sources11
Helixi414 – 425Combined sources12
Beta strandi433 – 438Combined sources6
Turni455 – 458Combined sources4
Helixi459 – 462Combined sources4
Helixi465 – 468Combined sources4
Helixi470 – 472Combined sources3
Helixi475 – 494Combined sources20
Beta strandi499 – 502Combined sources4
Turni513 – 515Combined sources3
Beta strandi518 – 524Combined sources7
Helixi527 – 529Combined sources3
Helixi536 – 544Combined sources9
Turni545 – 548Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F6WX-ray2.30A21-553[»]
1JMYX-ray2.60A21-538[»]
ProteinModelPortaliP19835.
SMRiP19835.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19835.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati559 – 5691Add BLAST11
Repeati570 – 5802Add BLAST11
Repeati581 – 5913Add BLAST11
Repeati592 – 6024Add BLAST11
Repeati603 – 6135Add BLAST11
Repeati614 – 6246Add BLAST11
Repeati625 – 6357Add BLAST11
Repeati636 – 6468Add BLAST11
Repeati647 – 6579Add BLAST11
Repeati658 – 66810Add BLAST11
Repeati669 – 67911Add BLAST11
Repeati680 – 69012Add BLAST11
Repeati691 – 70113Add BLAST11
Repeati702 – 71214Add BLAST11
Repeati713 – 72315Add BLAST11
Repeati724 – 73416Add BLAST11
Repeati735 – 74517Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 121Heparin-bindingAdd BLAST101
Regioni559 – 74517 X 11 AA tandem repeats, glycodomain, O-linked (mucin type)Add BLAST187

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP19835.
PhylomeDBiP19835.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR033560. BAL.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR032059. Mucin-like.
[Graphical view]
PANTHERiPTHR11559:SF139. PTHR11559:SF139. 1 hit.
PfamiPF00135. COesterase. 1 hit.
PF16058. Mucin-like. 2 hits.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P19835-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGRLQLVVLG LTCCWAVASA AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF
60 70 80 90 100
KGIPFAAPTK ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC
110 120 130 140 150
LYLNIWVPQG RKQVSRDLPV MIWIYGGAFL MGSGHGANFL NNYLYDGEEI
160 170 180 190 200
ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NYGLRDQHMA IAWVKRNIAA
210 220 230 240 250
FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS GVALSPWVIQ
260 270 280 290 300
KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP
310 320 330 340 350
MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP
360 370 380 390 400
AINKGNKKVT EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK
410 420 430 440 450
KKTVVDFETD VLFLVPTEIA LAQHRANAKS AKTYAYLFSH PSRMPVYPKW
460 470 480 490 500
VGADHADDIQ YVFGKPFATP TGYRPQDRTV SKAMIAYWTN FAKTGDPNMG
510 520 530 540 550
DSAVPTHWEP YTTENSGYLE ITKKMGSSSM KRSLRTNFLR YWTLTYLALP
560 570 580 590 600
TVTDQEATPV PPTGDSEATP VPPTGDSETA PVPPTGDSGA PPVPPTGDSG
610 620 630 640 650
APPVPPTGDS GAPPVPPTGD SGAPPVPPTG DSGAPPVPPT GDSGAPPVPP
660 670 680 690 700
TGDSGAPPVP PTGDSGAPPV PPTGDAGPPP VPPTGDSGAP PVPPTGDSGA
710 720 730 740 750
PPVTPTGDSE TAPVPPTGDS GAPPVPPTGD SEAAPVPPTD DSKEAQMPAV

IRF
Length:753
Mass (Da):79,322
Last modified:July 7, 2009 - v3
Checksum:iB3253789D1EABF7F
GO
Isoform Short (identifier: P19835-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     430-495: Missing.

Show »
Length:687
Mass (Da):71,834
Checksum:iBD269A05F7FBB9CF
GO

Sequence cautioni

The sequence AAA51973 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAA52014 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAC26514 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA38325 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAI13412 differs from that shown. Reason: Erroneous initiation.Curated
The sequence EAW88033 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73Missing AA sequence (PubMed:8471055).Curated1
Sequence conflicti235R → A in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti284 – 288RALTL → AAVTV in AAB35488 (PubMed:7578248).Curated5
Sequence conflicti313G → E in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti403T → I in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti481S → F in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti689A → P in AAB35488 (PubMed:7578248).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001463430 – 495Missing in isoform Short. CuratedAdd BLAST66

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54457 mRNA. Translation: CAA38325.1. Different initiation.
M85201 mRNA. Translation: AAA52014.1. Different initiation.
M54994 mRNA. Translation: AAA63211.1.
M94579 Genomic DNA. Translation: AAA51973.1. Different initiation.
S79774 mRNA. Translation: AAB35488.2.
AF072711 Genomic DNA. Translation: AAC26514.1. Different initiation.
AL162417 Genomic DNA. Translation: CAI13412.1. Different initiation.
CH471090 Genomic DNA. Translation: EAW88033.1. Different initiation.
PIRiS13586.
UniGeneiHs.533258.

Genome annotation databases

EnsembliENST00000351304; ENSP00000342217; ENSG00000170835.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54457 mRNA. Translation: CAA38325.1. Different initiation.
M85201 mRNA. Translation: AAA52014.1. Different initiation.
M54994 mRNA. Translation: AAA63211.1.
M94579 Genomic DNA. Translation: AAA51973.1. Different initiation.
S79774 mRNA. Translation: AAB35488.2.
AF072711 Genomic DNA. Translation: AAC26514.1. Different initiation.
AL162417 Genomic DNA. Translation: CAI13412.1. Different initiation.
CH471090 Genomic DNA. Translation: EAW88033.1. Different initiation.
PIRiS13586.
UniGeneiHs.533258.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F6WX-ray2.30A21-553[»]
1JMYX-ray2.60A21-538[»]
ProteinModelPortaliP19835.
SMRiP19835.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP19835. 1 interactor.
STRINGi9606.ENSP00000361151.

Chemistry databases

BindingDBiP19835.
ChEMBLiCHEMBL3219.
SwissLipidsiSLP:000000874.

Protein family/group databases

ESTHERihuman-CEL. Cholesterol_esterase.
MEROPSiS09.985.

PTM databases

iPTMnetiP19835.
PhosphoSitePlusiP19835.
UniCarbKBiP19835.

Polymorphism and mutation databases

DMDMi251757481.

Proteomic databases

PaxDbiP19835.
PeptideAtlasiP19835.
PRIDEiP19835.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351304; ENSP00000342217; ENSG00000170835.

Organism-specific databases

DisGeNETi1056.
GeneCardsiCEL.
HGNCiHGNC:1848. CEL.
HPAiHPA008023.
HPA052701.
MalaCardsiCEL.
MIMi114840. gene.
606391. phenotype.
609812. phenotype.
neXtProtiNX_P19835.
Orphaneti552. MODY.
PharmGKBiPA26391.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP19835.
PhylomeDBiP19835.
TreeFamiTF315470.

Enzyme and pathway databases

BioCyciZFISH:HS10190-MONOMER.
ReactomeiR-HSA-192456. Digestion of dietary lipid.
SABIO-RKP19835.

Miscellaneous databases

ChiTaRSiCEL. human.
EvolutionaryTraceiP19835.
PROiP19835.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170835.
CleanExiHS_CEL.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR033560. BAL.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR032059. Mucin-like.
[Graphical view]
PANTHERiPTHR11559:SF139. PTHR11559:SF139. 1 hit.
PfamiPF00135. COesterase. 1 hit.
PF16058. Mucin-like. 2 hits.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCEL_HUMAN
AccessioniPrimary (citable) accession number: P19835
Secondary accession number(s): Q16398
, Q5T7U7, Q9UCH1, Q9UP41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 7, 2009
Last modified: November 2, 2016
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.