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Reviewed, UniProtKB/Swiss-Prot P30122 (CEL_BOVIN)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Gene names
Name: CEL
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length597 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

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Ontologies

Keywords
   Biological processLipid degradation
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionsterol esterase activity

Inferred from electronic annotation. Source: EC

triacylglycerol lipase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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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

1 ....................................................................................................... 597
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P30122-1 [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

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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: 2590203] [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: 10220579] [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: 9331420] [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: 9548741] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-597.

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Cross-references

Sequence databases

M28402 mRNA. Translation: AAA56788.1.
IPIIPI00696108.
PIRA33668.
UniGeneBt.13160

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AKNX-ray2.80A19-597[»]
1AQLX-ray2.80A/B19-550[»]
2BCEX-ray1.60A19-597[»]
ModBaseSearch...

Protein family/group databases

MEROPSS09.985.

Genome annotation databases

EnsemblENSBTAG00000007486. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGENP30122.

Enzyme and pathway databases

BRENDA3.1.1.13. 251.
3.1.1.3. 251.

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]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents