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P11152 (LIPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. 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:
Lipoprotein lipase

Short name=LPL
EC=3.1.1.34
Gene names
Name:Lpl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium By similarity.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids By similarity. Interacts with GPIHBP1. Ref.8

Subcellular location

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity. Secreted By similarity. Note: Locates to the plasma membrane of microvilli of hepatocytes with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles By similarity.

Tissue specificity

Expressed in liver, epididymal fat, heart, psoas muscle, lactating mammary gland, adrenal, lung, and ovary. Highest levels in heart and adrenal gland. Ref.1

Developmental stage

Maximum expression in adipose tissue during early development. In heart, low levels 6 days before birth increasing 278-fold as animals reach adulthood. Ref.1

Post-translational modification

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity By similarity.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Chylomicron
Membrane
Secreted
VLDL
   DomainSignal
   LigandHeparin-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
Nitration
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of cholesterol storage

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage derived foam cell differentiation

Inferred from genetic interaction PubMed 10858435. Source: BHF-UCL

positive regulation of sequestering of triglyceride

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

triglyceride biosynthetic process

Inferred from electronic annotation. Source: Ensembl

triglyceride catabolic process

Inferred from direct assay PubMed 15178420. Source: BHF-UCL

triglyceride homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 20620994. Source: BHF-UCL

chylomicron

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 15178420. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein lipase activity

Inferred from direct assay PubMed 16166565PubMed 2563260. Source: MGI

protein binding

Inferred from physical interaction PubMed 19783858. Source: MGI

triglyceride binding

Inferred from electronic annotation. Source: Ensembl

triglyceride lipase activity

Inferred from direct assay PubMed 15178420. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 474447Lipoprotein lipase
PRO_0000017776

Regions

Domain341 – 464124PLAT
Region346 – 44196Heparin-binding By similarity

Sites

Active site1591Nucleophile By similarity
Active site1831Charge relay system By similarity
Active site2681Charge relay system By similarity

Amino acid modifications

Modified residue1211Nitrated tyrosine By similarity
Modified residue1911Nitrated tyrosine By similarity
Modified residue3431Nitrated tyrosine By similarity
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 67 By similarity
Disulfide bond243 ↔ 266 By similarity
Disulfide bond291 ↔ 310 By similarity
Disulfide bond302 ↔ 305 By similarity
Disulfide bond445 ↔ 465 By similarity

Experimental info

Sequence conflict1291K → Y no nucleotide entry Ref.1
Sequence conflict1471N → K in AAA39441. Ref.2
Sequence conflict3541D → N no nucleotide entry Ref.1
Sequence conflict4101I → M no nucleotide entry Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11152 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: E5895C98B7AE16CD

FASTA47453,109
        10         20         30         40         50         60 
MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA EDTCHLIPGL 

        70         80         90        100        110        120 
ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLYRAQQH 

       130        140        150        160        170        180 
YPVSAGYTKL VGNDVARFIN WMEEEFNYPL DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT 

       190        200        210        220        230        240 
GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ 

       250        260        270        280        290        300 
PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 

       310        320        330        340        350        360 
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTEDGKQHNQ 

       370        380        390        400        410        420 
AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMMKLKWI SDSYFSWPDW 

       430        440        450        460        470 
WSSPSFVIER IRVKAGETQK KVIFCAREKV SHLQKGKDSA VFVKCHDKSL KKSG 

« Hide

References

« Hide 'large scale' references
[1]"Lipoprotein lipase and hepatic lipase mRNA tissue specific expression, developmental regulation, and evolution."
Semenkovich C.F., Chen S.H., Wims M., Luo C.C., Li W.H., Chan L.
J. Lipid Res. 30:423-431(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Macrophage.
[2]"The structure of the mouse lipoprotein lipase gene: a B1 repetitive element is inserted into the 3' untranslated region of the mRNA."
Zechner R., Newman T.C., Steiner E., Breslow J.L.
Genomics 11:62-76(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Embryo, Head, Heart and Kidney.
[4]"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].
[5]"Adipogenesis in a myeloid supporting bone marrow stromal cell line."
Gimble J.M., Hua X., Youkhana K., Bass H.W., Medina K., Sullivan M., Greenberger J.S., Wang C.S.
J. Cell. Biochem. 50:73-82(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-183.
[6]"Cloning and characterization of the promoter of the murine lipoprotein lipase-encoding gene: structural and functional analysis."
Hua X., Enerbaeck S., Hudson J., Youkhana K., Gimble J.M.
Gene 107:247-258(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
Strain: BALB/c.
Tissue: Liver.
[7]"The sequence of cDNA encoding lipoprotein lipase. A member of a lipase gene family."
Kirchgessner T.G., Svenson K.L., Lusis A.J., Schotz M.C.
J. Biol. Chem. 262:8463-8466(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-474.
[8]"Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons."
Beigneux A.P., Davies B.S.J., Gin P., Weinstein M.M., Farber E., Qiao X., Peale F., Bunting S., Walzem R.L., Wong J.S., Blaner W.S., Ding Z.-M., Melford K., Wongsiriroj N., Shu X., de Sauvage F., Ryan R.O., Fong L.G., Bensadoun A., Young S.G.
Cell Metab. 5:279-291(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GPIHBP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60847 expand/collapse EMBL AC list , M60838, M60839, M60840, M60842, M60843, M60844, M60845, M60846 Genomic DNA. Translation: AAA39441.1.
AK002645 mRNA. Translation: BAB22256.1.
AK017272 mRNA. No translation available.
AK045064 mRNA. Translation: BAC32204.1.
AK086023 mRNA. Translation: BAC39594.1.
AK150355 mRNA. Translation: BAE29491.1.
AK150375 mRNA. Translation: BAE29507.1.
AK150457 mRNA. Translation: BAE29577.1.
AK150488 mRNA. Translation: BAE29604.1.
AK150505 mRNA. Translation: BAE29618.1.
AK150593 mRNA. Translation: BAE29686.1.
AK150672 mRNA. Translation: BAE29754.1.
AK151006 mRNA. Translation: BAE30029.1.
AK151093 mRNA. Translation: BAE30105.1.
AK151105 mRNA. Translation: BAE30115.1.
AK151369 mRNA. Translation: BAE30343.1.
AK151434 mRNA. Translation: BAE30397.1.
AK151521 mRNA. Translation: BAE30470.1.
AK151540 mRNA. Translation: BAE30486.1.
AK151563 mRNA. Translation: BAE30505.1.
AK151630 mRNA. Translation: BAE30564.1.
AK151679 mRNA. Translation: BAE30604.1.
AK151727 mRNA. Translation: BAE30645.1.
AK151772 mRNA. Translation: BAE30678.1.
AK151801 mRNA. Translation: BAE30701.1.
AK151828 mRNA. Translation: BAE30723.1.
AK151866 mRNA. Translation: BAE30754.1.
AK151870 mRNA. Translation: BAE30758.1.
AK151872 mRNA. Translation: BAE30760.1.
AK151893 mRNA. Translation: BAE30777.1.
AK152014 mRNA. Translation: BAE30876.1.
AK152035 mRNA. Translation: BAE30894.1.
AK152049 mRNA. Translation: BAE30905.1.
AK152053 mRNA. Translation: BAE30909.1.
AK152079 mRNA. Translation: BAE30930.1.
AK152350 mRNA. Translation: BAE31144.1.
AK152657 mRNA. Translation: BAE31394.1.
AK153148 mRNA. Translation: BAE31758.1.
AK153242 mRNA. Translation: BAE31834.1.
AK153425 mRNA. Translation: BAE31984.1.
AK159268 mRNA. Translation: BAE34947.1.
AK170486 mRNA. Translation: BAE41828.1.
BC003305 mRNA. Translation: AAH03305.1.
M65258 mRNA. Translation: AAA39442.1.
J03302 mRNA. Translation: AAA39440.1.
M63335 Genomic DNA. Translation: AAC04464.1.
CCDSCCDS40357.1.
PIRA40570.
RefSeqNP_032535.2. NM_008509.2.
UniGeneMm.1514.

3D structure databases

ProteinModelPortalP11152.
SMRP11152. Positions 36-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11152. 1 interaction.

PTM databases

PhosphoSiteP11152.

Proteomic databases

MaxQBP11152.
PaxDbP11152.
PRIDEP11152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568.
ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568.
GeneID16956.
KEGGmmu:16956.
UCSCuc009lwq.1. mouse.

Organism-specific databases

CTD4023.
MGIMGI:96820. Lpl.

Phylogenomic databases

eggNOGNOG40923.
GeneTreeENSGT00750000117234.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidQ542L4.
KOK01059.
OMAESVANCH.
OrthoDBEOG757CX5.
TreeFamTF324997.

Enzyme and pathway databases

BRENDA3.1.1.34. 3474.

Gene expression databases

ArrayExpressP11152.
BgeeP11152.
CleanExMM_LPL.
GenevestigatorP11152.

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.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsTIGR03230. lipo_lipase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLPL. mouse.
NextBio291008.
PROP11152.
SOURCESearch...

Entry information

Entry nameLIPL_MOUSE
AccessionPrimary (citable) accession number: P11152
Secondary accession number(s): Q05956 expand/collapse secondary AC list , Q542L4, Q9D3M9, Q9DCM8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 146 of the entry and version 3 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