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Q6P8U6 (LIPP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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

Names and origin

Protein namesRecommended name:
Pancreatic triacylglycerol lipase

Short name=PL
Short name=PTL
Short name=Pancreatic lipase
EC=3.1.1.3
Gene names
Name:Pnlip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones By similarity.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.4

Subcellular location

Secreted By similarity.

Tissue specificity

Pancreas. Ref.4

Induction

By colipase/CLPS in the presence of bile salts.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintestinal cholesterol absorption

Inferred from mutant phenotype PubMed 12915407. Source: MGI

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride lipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 465449Pancreatic triacylglycerol lipase
PRO_0000401139

Regions

Domain355 – 465111PLAT

Sites

Active site1691Nucleophile By similarity
Active site1931Charge relay system By similarity
Active site2801Charge relay system By similarity
Metal binding2041Calcium; via carbonyl oxygen By similarity
Metal binding2071Calcium; via carbonyl oxygen By similarity
Metal binding2091Calcium By similarity
Metal binding2121Calcium By similarity

Amino acid modifications

Disulfide bond20 ↔ 26 By similarity
Disulfide bond107 ↔ 118 By similarity
Disulfide bond254 ↔ 278 By similarity
Disulfide bond302 ↔ 313 By similarity
Disulfide bond316 ↔ 321 By similarity
Disulfide bond449 ↔ 465 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6P8U6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5CD39E8ABDF43A64

FASTA46551,428
        10         20         30         40         50         60 
MLMLWTFAVL LGAVAGREVC FDKLGCFSDD APWSGTLDRP LKALPWSPAQ INTRFLLYTN 

        70         80         90        100        110        120 
ENPDNYQLIT SDASNIRNSN FRTNRKTRII IHGFIDKGEE NWLSDMCKNM FRVESVNCIC 

       130        140        150        160        170        180 
VDWKGGSRTT YTQATQNVRV VGAEVALLVN VLQSDLGYSL NNVHLIGHSL GSHIAGEAGK 

       190        200        210        220        230        240 
RTFGAIGRIT GLDPAEPYFQ GTPEEVRLDP TDAQFVDAIH TDAGPIIPNL GFGMSQTVGH 

       250        260        270        280        290        300 
LDFFPNGGIE MPGCQKNILS QIVDIDGIWE GTRNFAACNH LRSYKFYTDS IVNPTGFAGF 

       310        320        330        340        350        360 
SCSSYSLFTA NKCFPCGSGG CPQMGHYADR YPGKTSRLYQ TFYLNTGDKS NFARWRYQVT 

       370        380        390        400        410        420 
VTLSGQKVTG HILVSLFGNG GNSKQYEVFK GSLQPGTSHV NEFDSDVDVG DLQKVKFIWY 

       430        440        450        460 
NNVINPTLPK VGASRITVER NDGRVFNFCS QETVREDVLL TLSPC 

« Hide

References

« Hide 'large scale' references
[1]"Feeding activates protein synthesis in mouse pancreas at the translational level without increase in mRNA."
Sans M.D., Lee S.H., D'Alecy L.G., Williams J.A.
Am. J. Physiol. 287:G667-G675(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[4]"Hydrolysis of retinyl esters by pancreatic triglyceride lipase."
van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.
Biochemistry 39:4900-4906(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY387690 mRNA. Translation: AAQ90020.1.
CH466585 Genomic DNA. Translation: EDL01803.1.
BC061061 mRNA. Translation: AAH61061.1.
CCDSCCDS29930.1.
RefSeqNP_081201.2. NM_026925.3.
UniGeneMm.20407.

3D structure databases

ProteinModelPortalQ6P8U6.
SMRQ6P8U6. Positions 18-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000056377.

PTM databases

PhosphoSiteQ6P8U6.

Proteomic databases

MaxQBQ6P8U6.
PaxDbQ6P8U6.
PRIDEQ6P8U6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057270; ENSMUSP00000056377; ENSMUSG00000046008.
GeneID69060.
KEGGmmu:69060.
UCSCuc008iaq.1. mouse.

Organism-specific databases

CTD5406.
MGIMGI:97722. Pnlip.

Phylogenomic databases

eggNOGNOG40923.
GeneTreeENSGT00750000117234.
HOGENOMHOG000038552.
HOVERGENHBG003243.
InParanoidQ6P8U6.
KOK14073.
OMAVKFIWYN.
OrthoDBEOG7KSX8B.
PhylomeDBQ6P8U6.
TreeFamTF324997.

Gene expression databases

BgeeQ6P8U6.
GenevestigatorQ6P8U6.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPNLIP. mouse.
NextBio328500.
PROQ6P8U6.
SOURCESearch...

Entry information

Entry nameLIPP_MOUSE
AccessionPrimary (citable) accession number: Q6P8U6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 87 of the entry and version 1 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

MGD cross-references

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