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Q64285

- CEL_MOUSE

UniProt

Q64285 - CEL_MOUSE

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Protein
Bile salt-activated lipase
Gene
Cel, Lip1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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 intermediate By similarity
Active sitei340 – 3401Charge relay system By similarity
Active sitei455 – 4551Charge relay system By similarity

GO - Molecular functioni

  1. acylglycerol lipase activity Source: RefGenome
  2. carboxylic ester hydrolase activity Source: RefGenome
  3. sterol esterase activity Source: UniProtKB-EC
  4. triglyceride lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. ceramide catabolic process Source: MGI
  2. cholesterol catabolic process Source: Ensembl
  3. pancreatic juice secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_204917. Digestion of dietary lipid.

Protein family/group databases

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: Chromosome 2

Organism-specific databases

MGIiMGI:88374. Cel.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
  3. extracellular space Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 By similarity
Add
BLAST
Chaini21 – 599579Bile salt-activated lipase
PRO_0000008632Add
BLAST

Amino acid modifications

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

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.
GenevestigatoriQ64285.

Interactioni

Subunit structurei

Interacts with CLC.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ64285.
SMRiQ64285. Positions 21-553.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00740000115241.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ64285.
KOiK12298.
OMAiARISTWS.
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

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MGRLEVLFLG LTCCLAAACA AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI    50
FKGIPFATAK TLENPQRHPG WQGTLKATNF KKRCLQATIT QDNTYGQEDC 100
LYLNIWVPQG RKQVSHNLPV MVWIYGGAFL MGSGQGANFL KNYLYDGEEI 150
ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NFGLRDQHMA IAWVKRNIAA 200
FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS GMALSPWAIQ 250
KNPLFWAKTI AKKVGCPTED TGKMAACLKI TDPRALTLAY KLPVKKQEYP 300
VVHYLAFIPV IDGDFIPDDP INLYNNTADI DYIAGINNMD GHLFATIDVP 350
AVDKTKQTVT EEDFYRLVSG HTVAKGLKGA QATFDIYTES WAQDPSQENM 400
KKTVVAFETD VLFLIPTEIA LAQHKAHAKS AKTYSYLFSH PSRMPIYPKW 450
MGADHADDLQ YVFGKPFATP LGYRPQDRAV SKAMIAYWTN FARSGDPNMG 500
NSPVPTHWYP YTLENGNYLD ITKTITSASM KEHLREKFLK FWAVTFEVLP 550
TVTGDQDTLT PPEDDSEVAP DPPSDDSQVV PVPPTDDSVE AQMPATIGF 599
Length:599
Mass (Da):65,813
Last modified:November 1, 1996 - v1
Checksum:i9E4428FDFCA8602E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U33169 mRNA. Translation: AAA92088.1 .
U37386 mRNA. Translation: AAC52279.1 .
CCDSi CCDS15841.1.
PIRi A57701.
RefSeqi NP_034015.1. NM_009885.1.
UniGenei Mm.236017.

3D structure databases

ProteinModelPortali Q64285.
SMRi Q64285. Positions 21-553.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.985.

PTM databases

PhosphoSitei Q64285.

2D gel databases

SWISS-2DPAGE Q64285.

Proteomic databases

MaxQBi Q64285.
PaxDbi Q64285.
PRIDEi Q64285.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028161 ; ENSMUSP00000028161 ; ENSMUSG00000026818 .
GeneIDi 12613.
KEGGi mmu:12613.
UCSCi uc008iyr.1. mouse.

Organism-specific databases

CTDi 1056.
MGIi MGI:88374. Cel.

Phylogenomic databases

eggNOGi COG2272.
GeneTreei ENSGT00740000115241.
HOGENOMi HOG000091866.
HOVERGENi HBG008839.
InParanoidi Q64285.
KOi K12298.
OMAi ARISTWS.
OrthoDBi EOG7034GN.
PhylomeDBi Q64285.
TreeFami TF315470.

Enzyme and pathway databases

Reactomei REACT_204917. Digestion of dietary lipid.

Miscellaneous databases

ChiTaRSi CEL. mouse.
NextBioi 281770.
PROi Q64285.
SOURCEi Search...

Gene expression databases

Bgeei Q64285.
CleanExi MM_CEL.
Genevestigatori Q64285.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 112 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

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