Skip Header

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

Q64285 (CEL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. 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
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
Synonyms:Lip1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length599 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 By similarity.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

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

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 599579Bile salt-activated lipase
PRO_0000008632

Regions

Repeat559 – 569111
Repeat570 – 580112
Repeat581 – 58883
Region559 – 588304 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
Glycosylation3251N-linked (GlcNAc...) Potential
Disulfide bond84 ↔ 100 By similarity
Disulfide bond266 ↔ 277 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64285 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9E4428FDFCA8602E

FASTA59965,813
        10         20         30         40         50         60 
MGRLEVLFLG LTCCLAAACA AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI FKGIPFATAK 

        70         80         90        100        110        120 
TLENPQRHPG WQGTLKATNF KKRCLQATIT QDNTYGQEDC LYLNIWVPQG RKQVSHNLPV 

       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 
GMALSPWAIQ KNPLFWAKTI AKKVGCPTED TGKMAACLKI TDPRALTLAY KLPVKKQEYP 

       310        320        330        340        350        360 
VVHYLAFIPV IDGDFIPDDP INLYNNTADI DYIAGINNMD GHLFATIDVP AVDKTKQTVT 

       370        380        390        400        410        420 
EEDFYRLVSG HTVAKGLKGA QATFDIYTES WAQDPSQENM KKTVVAFETD VLFLIPTEIA 

       430        440        450        460        470        480 
LAQHKAHAKS AKTYSYLFSH PSRMPIYPKW MGADHADDLQ YVFGKPFATP LGYRPQDRAV 

       490        500        510        520        530        540 
SKAMIAYWTN FARSGDPNMG NSPVPTHWYP YTLENGNYLD ITKTITSASM KEHLREKFLK 

       550        560        570        580        590 
FWAVTFEVLP TVTGDQDTLT PPEDDSEVAP DPPSDDSQVV PVPPTDDSVE AQMPATIGF

« Hide

References

[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: 8522186] [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: 8530060] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Lactating mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U33169 mRNA. Translation: AAA92088.1.
U37386 mRNA. Translation: AAC52279.1.
IPIIPI00132296.
PIRA57701.
RefSeqNP_034015.1. NM_009885.1.
UniGeneMm.236017.

3D structure databases

ProteinModelPortalQ64285.
SMRQ64285. Positions 21-553.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ64285.

Protein family/group databases

MEROPSS09.985.

2D gel databases

SWISS-2DPAGEQ64285.

Proteomic databases

PRIDEQ64285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028161; ENSMUSP00000028161; ENSMUSG00000026818.
GeneID12613.
KEGGmmu:12613.

Organism-specific databases

CTD1056.
MGIMGI:88374. Cel.

Phylogenomic databases

HOGENOMHBG716688.
HOVERGENHBG008839.
InParanoidQ64285.
OMADPNMGNS.
OrthoDBEOG4CC40T.
PhylomeDBQ64285.

Gene expression databases

ArrayExpressQ64285.
BgeeQ64285.
CleanExMM_CEL.
GenevestigatorQ64285.
GermOnlineENSMUSG00000026818. Mus musculus.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
KOK12298.
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio281770.
SOURCESearch...

Entry information

Entry nameCEL_MOUSE
AccessionPrimary (citable) accession number: Q64285
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents