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Protein

Bile salt-activated lipase

Gene

Cel

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.
A steryl ester + H2O = a sterol + a fatty acid.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei214 – 2141Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei340 – 3401Charge relay systemBy similarity
Active sitei455 – 4551Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

  • ceramide catabolic process Source: MGI
  • cholesterol catabolic process Source: MGI
  • pancreatic juice secretion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_349013. Digestion of dietary lipid.

Protein family/group databases

ESTHERimouse-pches. Cholesterol_esterase.
MEROPSiS09.985.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile salt-activated lipase (EC:3.1.1.13, EC:3.1.1.3)
Short name:
BAL
Alternative name(s):
Bile salt-stimulated lipase
Short name:
BSSL
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase
Gene namesi
Name:Cel
Synonyms:Lip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:88374. Cel.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 599579Bile salt-activated lipasePRO_0000008632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi84 ↔ 100By similarity
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi266 ↔ 277By similarity
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ64285.
PaxDbiQ64285.
PRIDEiQ64285.

2D gel databases

SWISS-2DPAGEQ64285.

PTM databases

PhosphoSiteiQ64285.

Expressioni

Tissue specificityi

EXpressed by eosinophils.1 Publication

Gene expression databases

BgeeiQ64285.
CleanExiMM_CEL.
ExpressionAtlasiQ64285. baseline and differential.
GenevisibleiQ64285. MM.

Interactioni

Subunit structurei

Interacts with CLC.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028161.

Structurei

3D structure databases

ProteinModelPortaliQ64285.
SMRiQ64285. Positions 21-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati559 – 569111Add
BLAST
Repeati570 – 580112Add
BLAST
Repeati581 – 58883

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni559 – 588304 X 11 AA tandem repeats, O-glycosylated regionAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ64285.
KOiK12298.
OMAiPLLCRPQ.
OrthoDBiEOG7034GN.
PhylomeDBiQ64285.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64285-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLEVLFLG LTCCLAAACA AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI
60 70 80 90 100
FKGIPFATAK TLENPQRHPG WQGTLKATNF KKRCLQATIT QDNTYGQEDC
110 120 130 140 150
LYLNIWVPQG RKQVSHNLPV MVWIYGGAFL MGSGQGANFL KNYLYDGEEI
160 170 180 190 200
ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NFGLRDQHMA IAWVKRNIAA
210 220 230 240 250
FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS GMALSPWAIQ
260 270 280 290 300
KNPLFWAKTI AKKVGCPTED TGKMAACLKI TDPRALTLAY KLPVKKQEYP
310 320 330 340 350
VVHYLAFIPV IDGDFIPDDP INLYNNTADI DYIAGINNMD GHLFATIDVP
360 370 380 390 400
AVDKTKQTVT EEDFYRLVSG HTVAKGLKGA QATFDIYTES WAQDPSQENM
410 420 430 440 450
KKTVVAFETD VLFLIPTEIA LAQHKAHAKS AKTYSYLFSH PSRMPIYPKW
460 470 480 490 500
MGADHADDLQ YVFGKPFATP LGYRPQDRAV SKAMIAYWTN FARSGDPNMG
510 520 530 540 550
NSPVPTHWYP YTLENGNYLD ITKTITSASM KEHLREKFLK FWAVTFEVLP
560 570 580 590
TVTGDQDTLT PPEDDSEVAP DPPSDDSQVV PVPPTDDSVE AQMPATIGF
Length:599
Mass (Da):65,813
Last modified:November 1, 1996 - v1
Checksum:i9E4428FDFCA8602E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33169 mRNA. Translation: AAA92088.1.
U37386 mRNA. Translation: AAC52279.1.
CCDSiCCDS15841.1.
PIRiA57701.
RefSeqiNP_034015.1. NM_009885.1.
UniGeneiMm.236017.

Genome annotation databases

EnsembliENSMUST00000028161; ENSMUSP00000028161; ENSMUSG00000026818.
GeneIDi12613.
KEGGimmu:12613.
UCSCiuc008iyr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33169 mRNA. Translation: AAA92088.1.
U37386 mRNA. Translation: AAC52279.1.
CCDSiCCDS15841.1.
PIRiA57701.
RefSeqiNP_034015.1. NM_009885.1.
UniGeneiMm.236017.

3D structure databases

ProteinModelPortaliQ64285.
SMRiQ64285. Positions 21-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028161.

Protein family/group databases

ESTHERimouse-pches. Cholesterol_esterase.
MEROPSiS09.985.

PTM databases

PhosphoSiteiQ64285.

2D gel databases

SWISS-2DPAGEQ64285.

Proteomic databases

MaxQBiQ64285.
PaxDbiQ64285.
PRIDEiQ64285.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028161; ENSMUSP00000028161; ENSMUSG00000026818.
GeneIDi12613.
KEGGimmu:12613.
UCSCiuc008iyr.1. mouse.

Organism-specific databases

CTDi1056.
MGIiMGI:88374. Cel.

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ64285.
KOiK12298.
OMAiPLLCRPQ.
OrthoDBiEOG7034GN.
PhylomeDBiQ64285.
TreeFamiTF315470.

Enzyme and pathway databases

ReactomeiREACT_349013. Digestion of dietary lipid.

Miscellaneous databases

ChiTaRSiCel. mouse.
NextBioi281770.
PROiQ64285.
SOURCEiSearch...

Gene expression databases

BgeeiQ64285.
CleanExiMM_CEL.
ExpressionAtlasiQ64285. baseline and differential.
GenevisibleiQ64285. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of the mouse pancreatic/mammary gland cholesterol esterase-encoding cDNA and gene."
    Mackay K., Lawn R.M.
    Gene 165:255-259(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Mammary gland.
  2. "Molecular cloning and characterization of the mouse carboxyl ester lipase gene and evidence for expression in the lactating mammary gland."
    Lidmer A.S., Kannius M., Lundberg L., Bjursell G., Nilsson J.
    Genomics 29:115-122(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Lactating mammary gland.
  3. "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.

Entry informationi

Entry nameiCEL_MOUSE
AccessioniPrimary (citable) accession number: Q64285
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.