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P07882 (CEL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length612 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.

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

Enzyme regulation

Activated by bile salts containing a 7-hydroxyl group.

Subcellular location

Secreted.

Tissue specificity

Synthesized primarily in the pancreas and then transported to the intestine.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 612592Bile salt-activated lipase
PRO_0000008633

Regions

Repeat556 – 566111
Repeat567 – 577112
Repeat578 – 588113
Repeat589 – 599114
Region556 – 599444 X 11 AA tandem repeats, O-glycosylated region

Sites

Active site2141Acyl-ester intermediate By similarity
Active site3401Charge relay system By similarity
Active site4551Charge relay system By similarity

Amino acid modifications

Glycosylation2071N-linked (GlcNAc...) Potential
Disulfide bond84 ↔ 100 By similarity
Disulfide bond266 ↔ 277 By similarity

Experimental info

Mutagenesis4401H → Q: No effect on activity.
Mutagenesis4551H → Q, R, A, S or D: Abolishes activity.
Sequence conflict261V → L in AAA41540. Ref.2
Sequence conflict1541G → A in AAA41540. Ref.2
Sequence conflict2171A → G in AAA41540. Ref.2
Sequence conflict2191S → I in AAA41540. Ref.2
Sequence conflict4191M → T in AAB46376. Ref.3
Sequence conflict5131T → M in AAA41540. Ref.2
Sequence conflict5131T → M in AAB46376. Ref.3
Sequence conflict576 – 5772GG → VV in AAB46376. Ref.3
Sequence conflict608 – 6092GP → VA in AAB46376. Ref.3
Sequence conflict6111G → A in AAB46376. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P07882 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 1569CE4EA71ED02A

FASTA61267,040
        10         20         30         40         50         60 
MGRLEVLFLG LTCCLAAACA AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI FKGIPFATAK 

        70         80         90        100        110        120 
TLENPQRHPG WQGTLKATDF KKRCLQATIT QDDTYGQEDC LYLNIWVPQG RKQVSHDLPV 

       130        140        150        160        170        180 
MVWIYGGAFL MGSGQGANFL KNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG 

       190        200        210        220        230        240 
NFGLRDQHMA IAWVKRNIAA FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS 

       250        260        270        280        290        300 
GVALSPWAIQ ENPLFWAKTI AKKVGCPTED TAKMAGCLKI TDPRALTLAY RLPLKSQEYP 

       310        320        330        340        350        360 
IVHYLAFIPV VDGDFIPDDP INLYDNAADI DYLAGINDMD GHLFATVDVP AIDKAKQDVT 

       370        380        390        400        410        420 
EEDFYRLVSG HTVAKGLKGT QATFDIYTES WAQDPSQENM KKTVVAFETD ILFLIPTEMA 

       430        440        450        460        470        480 
LAQHRAHAKS AKTYSYLFSH PSRMPIYPKW MGADHADDLQ YVFGKPFATP LGYRAQDRTV 

       490        500        510        520        530        540 
SKAMIAYWTN FAKSGDPNMG NSPVPTHWYP YTTENGNYLD INKKITSTSM KEHLREKFLK 

       550        560        570        580        590        600 
FWAVTFEMLP TVVGDHTPPE DDSEAAPVPP TDDSQGGPVP PTDDSQTTPV PPTDNSQAGD 

       610 
SVEAQMPGPI GF

« Hide

References

[1]"Molecular cloning and expression of cDNA for rat pancreatic cholesterol esterase."
Kissel J.A., Fontaine R.N., Turck C.W., Brockman H.L., Hui D.Y.
Biochim. Biophys. Acta 1006:227-237(1989) [PubMed: 2688744] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Pancreas.
[2]"Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning."
Han J.H., Stratowa C., Rutter W.J.
Biochemistry 26:1617-1625(1987) [PubMed: 3593682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of the rat pancreatic cholesterol esterase gene."
Fontaine R.N., Carter C.P., Hui D.Y.
Biochemistry 30:7008-7014(1991) [PubMed: 2069957] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Identification of the active site serine in pancreatic cholesterol esterase by chemical modification and site-specific mutagenesis."
Dipersio L.P., Fontaine R.N., Hui D.Y.
J. Biol. Chem. 265:16801-16806(1990) [PubMed: 2211595] [Abstract]
Cited for: ACTIVE SITE SER-214.
[5]"Site-specific mutagenesis of an essential histidine residue in pancreatic cholesterol esterase."
Dipersio L.P., Fontaine R.N., Hui D.Y.
J. Biol. Chem. 266:4033-4036(1991) [PubMed: 1999399] [Abstract]
Cited for: ACTIVE SITE HIS-455.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X16054 mRNA. Translation: CAA34189.1.
M15893 mRNA. Translation: AAA41540.1.
M69157 Genomic DNA. Translation: AAB46376.1.
IPIIPI00211548.
PIRA34967.
UniGeneRn.91234.

3D structure databases

ProteinModelPortalP07882.
SMRP07882. Positions 21-552.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07882.

Protein family/group databases

MEROPSS09.985.

Proteomic databases

PRIDEP07882.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCNM_016997. rat.

Organism-specific databases

RGD2331. Cel.

Phylogenomic databases

eggNOGroNOG05185.
HOVERGENHBG008839.
InParanoidP07882.
OrthoDBEOG4CC40T.

Gene expression databases

ArrayExpressP07882.
GenevestigatorP07882.
GermOnlineENSRNOG00000010406. Rattus norvegicus.

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

NextBio602777.

Entry information

Entry nameCEL_RAT
AccessionPrimary (citable) accession number: P07882
Secondary accession number(s): P14722
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 1, 1993
Last modified: September 21, 2011
This is version 98 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

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