Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P19835 (CEL_HUMAN)

Last modified June 16, 2009. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Bile salt-activated lipase
      Short name=BAL
    EC=3.1.1.3
    EC=3.1.1.13
Alternative name(s):
    Bile salt-stimulated lipase
      Short name=BSSL
    Carboxyl ester lipase
    Sterol esterase
    Cholesterol esterase
    Pancreatic lysophospholipase
    Bucelipase
Gene names
Name: CEL
Synonyms: BAL
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length742 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

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.8

A steryl ester + H2O = a sterol + a fatty acid. Ref.8

Enzyme regulation

Activated by bile salts containing a 7-hydroxyl group.

Tissue specificity

Mammary gland and pancreas.

Involvement in disease

Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:609812]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY [MIM:606391] is an autosomal dominant form of diabetes mellitus. The pancreas serves both endocrine and exocrine functions. The endocrine cells are found in the islets of Langerhans. They synthesize insulin and other hormones, and are involved in the pathogenesis of diabetes mellitus. The exocrine cells produce bicarbonate and digestive enzymes and are involved in the pathogenesis of pancreatic malabsorption. The localization of the islets within exocrine pancreatic tissue is suggestive of an interdependency and cross-talk between these two cell populations in their normal and in their abnormal function. Ref.13

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

biophysicochemical properties

Kinetic parameters:

KM=24 µM for lipoyl-4-aminobenzoate

KM=15 µM for triacetin

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

Vmax=323 pmol/min/mg enzyme toward triacetin

Hide | Top

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.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.3
Chain21 – 742722Bile 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 – 69011
Repeat691 – 70111
Repeat702 – 71211
Repeat713 – 72311
Repeat724 – 73411
Region21 – 121101Heparin-binding
Region559 – 73417616 X 11 AA tandem repeats, glycodomain, O-linked (mucin type)

Sites

Active site2141Acyl-ester intermediate Ref.9
Active site3401Charge relay system Ref.9
Active site4551Charge relay system Ref.9

Amino acid modifications

Glycosylation2071N-linked (GlcNAc...) (complex)
CAR_000141
Glycosylation5581O-linked (GalNAc...) Ref.10
Glycosylation5691O-linked (GalNAc...) Ref.10
Glycosylation5791O-linked (GalNAc...) Ref.10
Glycosylation5961O-linked (GalNAc...) Ref.10
Glycosylation6071O-linked (GalNAc...) Ref.10
Glycosylation6181O-linked (GalNAc...) Ref.10
Glycosylation6291O-linked (GalNAc...) Ref.10
Glycosylation6401O-linked (GalNAc...) Ref.10
Glycosylation6511O-linked (GalNAc...) Ref.10
Glycosylation6621O-linked (GalNAc...) Ref.10
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.8
Sequence conflict731Missing AA sequence Ref.8
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 conflict6781A → P in AAB35488. Ref.5

Secondary structure

1 ............................................................................................... 742
Helix Strand Turn

Details...

Hide | Top

Sequences

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

Last modified April 1, 1993. Version 2.
Checksum: 1AAC23DACC8C2859

FASTA74278,346
        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 
PTGDAGPPPV PPTGDSGAPP VPPTGDSGAP PVTPTGDSET APVPPTGDSG APPVPPTGDS 

       730        740 
EAAPVPPTDD SKEAQMPAVI RF

« Hide

Isoform Short.

Checksum: 903AE505F462C5CB
Show »

FASTA67670,858

Hide | Top

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: 1698625] [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: 2265692] [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: 1988041] [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: 1639390] [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: 7578248] [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: 9530636] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]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].
[8]"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: 8471055] [Abstract]
Cited for: PROTEIN SEQUENCE OF 53-76 AND 366-374, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-455.
Tissue: Milk.
[9]"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: 1991511] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVE SITE.
[10]"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: 7654718] [Abstract]
Cited for: GLYCOSYLATION AT THR-558; THR-569; THR-579; THR-596; THR-607; THR-618; THR-629; THR-640; THR-651 AND THR-662.
[11]"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: 10024660] [Abstract]
Cited for: STRUCTURE OF N-LINKED CARBOHYDRATES.
[12]"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: 11045623] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-553.
[13]"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: 16369531] [Abstract]
Cited for: INVOLVEMENT IN MODY8.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

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.
CH471090 Genomic DNA. Translation: EAW88033.1. Different initiation.
IPIIPI00218674.
IPI00843810.
PIRS13586.
UniGeneHs.533258

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1F6WX-ray2.30A21-553[»]
1JMYX-ray2.60A21-538[»]
ModBaseSearch...

Protein family/group databases

MEROPSS09.985.

PTM databases

GlycoSuiteDBP19835.

Genome annotation databases

EnsemblENSG00000170835. Homo sapiens. [Contig view]

Organism-specific databases

GeneCardsGC09P134927.
H-InvDBHIX0025702.
HGNCHGNC:1848. CEL.
HPAHPA008023.
MIM114840. gene.
606391. phenotype.
609812. phenotype.
Orphanet552. MODY syndrome.
101057. MODY7.
PharmGKBPA26391.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP19835.

Enzyme and pathway databases

BRENDA3.1.1.13. 247.
3.1.1.3. 247.
ReactomeREACT_602. Lipid and lipoprotein metabolism.

Gene expression databases

ArrayExpressP19835.
BgeeP19835.
CleanExHS_CEL.
GermOnlineENSG00000170835. Homo sapiens.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PANTHERPTHR11559. CarbesteraseB. 1 hit.
PfamPF00135. COesterase. 1 hit.
[Graphical view]
ProDomPD003992. XGLTT_domain. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Hide | Top

Entry information

Entry nameCEL_HUMAN
AccessionPrimary (citable) accession number: P19835
Secondary accession number(s): Q16398, Q9UCH1, Q9UP41
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 1, 1993
Last modified: June 16, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 9

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents