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P19835 (CEL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bile salt-activated lipase

Short name=BAL
EC=3.1.1.13
EC=3.1.1.3
Alternative name(s):
Bile salt-stimulated lipase
Short name=BSSL
Bucelipase
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase
Gene names
Name:CEL
Synonyms:BAL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.9

A steryl ester + H2O = a sterol + a fatty acid. Ref.9

Enzyme regulation

Activated by bile salts containing a 7-hydroxyl group.

Subunit structure

Interacts with CLC. Ref.13

Subcellular location

Secreted.

Tissue specificity

Mammary gland and pancreas. Expressed by eosinophils. Ref.13

Involvement in disease

Maturity-onset diabetes of the young 8 with exocrine dysfunction (MODY8) [MIM:609812]: A 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.
Note: 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 (Ref.15). Ref.15

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Biophysicochemical properties

Kinetic parameters:

KM=24 µM for lipoyl-4-aminobenzoate Ref.9

KM=15 µM for triacetin

Vmax=45.5 pmol/min/mg enzyme toward lipoyl-4-aminobenzoate

Vmax=323 pmol/min/mg enzyme toward triacetin

Sequence caution

The sequence AAA51973.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA52014.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAC26514.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA38325.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI13412.1 differs from that shown. Reason: Erroneous initiation.

The sequence EAW88033.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DiseaseDiabetes mellitus
   DomainRepeat
Signal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processceramide catabolic process

Inferred from electronic annotation. Source: Ensembl

cholesterol catabolic process

Inferred from direct assay PubMed 12031288. Source: UniProtKB

fatty acid catabolic process

Non-traceable author statement Ref.5. Source: UniProtKB

intestinal cholesterol absorption

Non-traceable author statement PubMed 12031288. Source: UniProtKB

intestinal lipid catabolic process

Non-traceable author statement Ref.5. Source: UniProtKB

lipid digestion

Traceable author statement. Source: Reactome

lipid metabolic process

Non-traceable author statement PubMed 8639615. Source: UniProtKB

pancreatic juice secretion

Inferred from direct assay PubMed 1854805. Source: UniProtKB

protein esterification

Non-traceable author statement Ref.5. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride metabolic process

Inferred by curator Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionacylglycerol lipase activity

Traceable author statement. Source: Reactome

catalytic activity

Traceable author statement Ref.2. Source: UniProtKB

heparin binding

Non-traceable author statement Ref.5. Source: UniProtKB

hydrolase activity

Traceable author statement Ref.2. Source: UniProtKB

sterol esterase activity

Non-traceable author statement PubMed 12031288. Source: UniProtKB

triglyceride lipase activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: 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.
Isoform Short (identifier: P19835-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.3
Chain21 – 753733Bile salt-activated lipase
PRO_0000008631

Regions

Repeat559 – 569111
Repeat570 – 580112
Repeat581 – 591113
Repeat592 – 602114
Repeat603 – 613115
Repeat614 – 624116
Repeat625 – 635117
Repeat636 – 646118
Repeat647 – 657119
Repeat658 – 6681110
Repeat669 – 6791111
Repeat680 – 6901112
Repeat691 – 7011113
Repeat702 – 7121114
Repeat713 – 7231115
Repeat724 – 7341116
Repeat735 – 7451117
Region21 – 121101Heparin-binding
Region559 – 74518717 X 11 AA tandem repeats, glycodomain, O-linked (mucin type)

Sites

Active site2141Acyl-ester intermediate Ref.10
Active site3401Charge relay system Ref.10
Active site4551Charge relay system Ref.10

Amino acid modifications

Glycosylation2071N-linked (GlcNAc...) (complex)
CAR_000141
Glycosylation5581O-linked (GalNAc...) Ref.11
Glycosylation5691O-linked (GalNAc...) Ref.11
Glycosylation5791O-linked (GalNAc...) Ref.11
Glycosylation6071O-linked (GalNAc...) Ref.11
Glycosylation6181O-linked (GalNAc...) Ref.11
Glycosylation6291O-linked (GalNAc...) Ref.11
Glycosylation6401O-linked (GalNAc...) Ref.11
Glycosylation6511O-linked (GalNAc...) Ref.11
Glycosylation6621O-linked (GalNAc...) Ref.11
Glycosylation6731O-linked (GalNAc...) Ref.11
Disulfide bond84 ↔ 100
Disulfide bond266 ↔ 277

Natural variations

Alternative sequence430 – 49566Missing in isoform Short.
VSP_001463

Experimental info

Mutagenesis4551H → Q: Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold. Ref.9
Sequence conflict731Missing AA sequence Ref.9
Sequence conflict2351R → A in AAB35488. Ref.5
Sequence conflict284 – 2885RALTL → AAVTV in AAB35488. Ref.5
Sequence conflict3131G → E in AAB35488. Ref.5
Sequence conflict4031T → I in AAB35488. Ref.5
Sequence conflict4811S → F in AAB35488. Ref.5
Sequence conflict6891A → P in AAB35488. Ref.5

Secondary structure

....................................................................................................... 753
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 7, 2009. Version 3.
Checksum: B3253789D1EABF7F

FASTA75379,322
        10         20         30         40         50         60 
MGRLQLVVLG LTCCWAVASA AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF KGIPFAAPTK 

        70         80         90        100        110        120 
ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC LYLNIWVPQG RKQVSRDLPV 

       130        140        150        160        170        180 
MIWIYGGAFL MGSGHGANFL NNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG 

       190        200        210        220        230        240 
NYGLRDQHMA IAWVKRNIAA FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS 

       250        260        270        280        290        300 
GVALSPWVIQ KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP 

       310        320        330        340        350        360 
MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP AINKGNKKVT 

       370        380        390        400        410        420 
EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK KKTVVDFETD VLFLVPTEIA 

       430        440        450        460        470        480 
LAQHRANAKS AKTYAYLFSH PSRMPVYPKW VGADHADDIQ YVFGKPFATP TGYRPQDRTV 

       490        500        510        520        530        540 
SKAMIAYWTN FAKTGDPNMG DSAVPTHWEP YTTENSGYLE ITKKMGSSSM KRSLRTNFLR 

       550        560        570        580        590        600 
YWTLTYLALP TVTDQEATPV PPTGDSEATP VPPTGDSETA PVPPTGDSGA PPVPPTGDSG 

       610        620        630        640        650        660 
APPVPPTGDS GAPPVPPTGD SGAPPVPPTG DSGAPPVPPT GDSGAPPVPP TGDSGAPPVP 

       670        680        690        700        710        720 
PTGDSGAPPV PPTGDAGPPP VPPTGDSGAP PVPPTGDSGA PPVTPTGDSE TAPVPPTGDS 

       730        740        750 
GAPPVPPTGD SEAAPVPPTD DSKEAQMPAV IRF 

« Hide

Isoform Short [UniParc].

Checksum: BD269A05F7FBB9CF
Show »

FASTA68771,834

References

« Hide 'large scale' references
[1]"cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase."
Nilsson J., Blaeckberg L., Carlsson P., Enerbaeck S., Hernell O., Bjursell G.
Eur. J. Biochem. 192:543-550(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PARTIAL PROTEIN SEQUENCE.
Tissue: Mammary gland.
[2]"Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase."
Hui D.Y., Kissel J.A.
FEBS Lett. 276:131-134(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Pancreas.
[3]"Structure of human milk bile salt activated lipase."
Baba T., Downs D., Jackson K.W., Tang J., Wang C.-S.
Biochemistry 30:500-510(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF 21-81; 122-126; 190-194; 275-279; 302-306; 445-449; 485-490; 500-507; 526-528 AND 531-538.
Tissue: Mammary gland and Milk.
[4]"Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene."
Lidberg U., Nilsson J., Stroemberg K., Stenman G., Sahlin P., Enerbaeck S., Bjursell G.
Genomics 13:630-640(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Bile salt-dependent lipase transcripts in human fetal tissues."
Roudani S., Miralles F., Margotat A., Escribano M.J., Lombardo D.
Biochim. Biophys. Acta 1264:141-150(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[6]"Structure and organization of the human carboxyl ester lipase locus."
Madeyski K., Lidberg U., Bjursell G., Nilsson J.
Mamm. Genome 9:334-338(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase)."
Hui D.Y., Hayakawa K., Oizumi J.
Biochem. J. 291:65-69(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 53-76 AND 366-374, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-455.
Tissue: Milk.
[10]"Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases."
Christie D.L., Cleverly D.R., O'Connor C.J.O.
FEBS Lett. 278:190-194(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVE SITE.
[11]"Isolation and characterization of human milk bile salt-activated lipase C-tail fragment."
Wang C.S., Dashti A., Jackson K.W., Yeh J.C., Cummings R.D., Tang J.
Biochemistry 34:10639-10644(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-558; THR-569; THR-579; THR-607; THR-618; THR-629; THR-640; THR-651; THR-662 AND THR-673.
[12]"Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk."
Mechref Y., Chen P., Novotny M.V.
Glycobiology 9:227-234(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF N-LINKED CARBOHYDRATES.
[13]"Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion."
Ackerman S.J., Liu L., Kwatia M.A., Savage M.P., Leonidas D.D., Swaminathan G.J., Acharya K.R.
J. Biol. Chem. 277:14859-14868(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLC, TISSUE SPECIFICITY.
[14]"Crystal structure of the catalytic domain of human bile salt activated lipase."
Terzyan S., Wang C.S., Downs D., Hunter B., Zhang X.C.
Protein Sci. 9:1783-1790(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-553.
[15]"Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction."
Raeder H., Johansson S., Holm P.I., Haldorsen I.S., Mas E., Sbarra V., Nermoen I., Eide S.A., Grevle L., Bjoerkhaug L., Sagen J.V., Aksnes L., Soevik O., Lombardo D., Molven A., Njoelstad P.R.
Nat. Genet. 38:54-62(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MODY8.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS13586.
UniGeneHs.533258.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F6WX-ray2.30A21-553[»]
1JMYX-ray2.60A21-538[»]
ProteinModelPortalP19835.
SMRP19835. Positions 21-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107485. 1 interaction.
IntActP19835. 1 interaction.
STRING9606.ENSP00000361151.

Chemistry

BindingDBP19835.
ChEMBLCHEMBL3219.

Protein family/group databases

MEROPSS09.985.

PTM databases

PhosphoSiteP19835.
UniCarbKBP19835.

Polymorphism databases

DMDM251757481.

Proteomic databases

PaxDbP19835.
PRIDEP19835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351304; ENSP00000342217; ENSG00000170835. [P19835-2]
UCSCuc010naa.2. human. [P19835-1]

Organism-specific databases

GeneCardsGC09P135937.
HGNCHGNC:1848. CEL.
HPAHPA008023.
HPA052701.
MIM114840. gene.
606391. phenotype.
609812. phenotype.
neXtProtNX_P19835.
Orphanet552. MODY syndrome.
PharmGKBPA26391.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2272.
HOGENOMHOG000091866.
HOVERGENHBG008839.
OrthoDBEOG7034GN.
PhylomeDBP19835.
TreeFamTF315470.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP19835.

Gene expression databases

ArrayExpressP19835.
BgeeP19835.
CleanExHS_CEL.
GenevestigatorP19835.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19835.
NextBio4419.
PROP19835.
SOURCESearch...

Entry information

Entry nameCEL_HUMAN
AccessionPrimary (citable) accession number: P19835
Secondary accession number(s): Q16398 expand/collapse secondary AC list , Q5T7U7, Q9UCH1, Q9UP41
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM