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P30122 (CEL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase
Gene names
Name:CEL
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length597 AA.
Sequence statusFragment.
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.

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

Enzyme regulation

Activated by bile salts containing a 7-hydroxyl group in the infants intestine where it aids to digest milk fats.

Subunit structure

Interacts with CLC By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 18›18 Ref.2
Chain19 – 597579Bile salt-activated lipase
PRO_0000008630

Sites

Active site2121Acyl-ester intermediate
Active site3381Charge relay system
Active site4531Charge relay system

Amino acid modifications

Glycosylation2051N-linked (GlcNAc...)
Glycosylation3791N-linked (GlcNAc...)
Disulfide bond82 ↔ 98
Disulfide bond264 ↔ 275

Experimental info

Sequence conflict301F → P AA sequence Ref.2
Sequence conflict451I → V in AAA56788. Ref.1
Non-terminal residue11

Secondary structure

.............................................................................................................. 597
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30122 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: B23EB7AED90EBFD1

FASTA59765,162
        10         20         30         40         50         60 
LGASRLGPSP GCLAVASAAK LGSVYTEGGF VEGVNKKLSL FGDSIDIFKG IPFAAAPKAL 

        70         80         90        100        110        120 
EKPERHPGWQ GTLKAKSFKK RCLQATLTQD STYGNEDCLY LNIWVPQGRK EVSHDLPVMI 

       130        140        150        160        170        180 
WIYGGAFLMG ASQGANFLSN YLYDGEEIAT RGNVIVVTFN YRVGPLGFLS TGDSNLPGNY 

       190        200        210        220        230        240 
GLWDQHMAIA WVKRNIEAFG GDPDNITLFG ESAGGASVSL QTLSPYNKGL IKRAISQSGV 

       250        260        270        280        290        300 
GLCPWAIQQD PLFWAKRIAE KVGCPVDDTS KMAGCLKITD PRALTLAYKL PLGSTEYPKL 

       310        320        330        340        350        360 
HYLSFVPVID GDFIPDDPVN LYANAADVDY IAGTNDMDGH LFVGMDVPAI NSNKQDVTEE 

       370        380        390        400        410        420 
DFYKLVSGLT VTKGLRGANA TYEVYTEPWA QDSSQETRKK TMVDLETDIL FLIPTKIAVA 

       430        440        450        460        470        480 
QHKSHAKSAN TYTYLFSQPS RMPIYPKWMG ADHADDLQYV FGKPFATPLG YRAQDRTVSK 

       490        500        510        520        530        540 
AMIAYWTNFA RTGDPNTGHS TVPANWDPYT LEDDNYLEIN KQMDSNSMKL HLRTNYLQFW 

       550        560        570        580        590 
TQTYQALPTV TSAGASLLPP EDNSQASPVP PADNSGAPTE PSAGDSEVAQ MPVVIGF 

« Hide

References

[1]"Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase."
Kyger E.M., Wiegand R.C., Lange L.G.
Biochem. Biophys. Res. Commun. 164:1302-1309(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and characterization of bovine pancreatic bile salt-activated lipase."
Tanaka H., Mierau I., Ito F.
J. Biochem. 125:883-890(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-40.
Tissue: Pancreas.
[3]"The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism."
Wang X., Wang C.S., Tang J., Dyda F., Zhang X.C.
Structure 5:1209-1218(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-565, SEQUENCE REVISION TO 45.
[4]"Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel structural features involved in lipase activation."
Chen J.C.-H., Miercke L.J.W., Krucinski J., Starr J.R., Saenz G., Wang X., Spilburg C.A., Lange L.G., Ellsworth J.L., Stroud R.M.
Biochemistry 37:5107-5117(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-597.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28402 mRNA. Translation: AAA56788.1.
PIRA33668.
UniGeneBt.13160.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKNX-ray2.80A19-597[»]
1AQLX-ray2.80A/B19-550[»]
2BCEX-ray1.60A19-597[»]
ProteinModelPortalP30122.
SMRP30122. Positions 19-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000032584.

Chemistry

BindingDBP30122.
ChEMBLCHEMBL2988.

Protein family/group databases

MEROPSS09.985.

Proteomic databases

PRIDEP30122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2272.
HOGENOMHOG000091866.
HOVERGENHBG008839.

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

EvolutionaryTraceP30122.

Entry information

Entry nameCEL_BOVIN
AccessionPrimary (citable) accession number: P30122
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references