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Protein

Lipoprotein lipase

Gene

Lpl

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

Functioni

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).By similarity

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591NucleophileBy similarity
Active sitei183 – 1831Charge relay systemPROSITE-ProRule annotation
Active sitei268 – 2681Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. apolipoprotein binding Source: MGI
  2. heparin binding Source: MGI
  3. lipoprotein lipase activity Source: MGI
  4. receptor binding Source: MGI
  5. triglyceride binding Source: Ensembl
  6. triglyceride lipase activity Source: BHF-UCL

GO - Biological processi

  1. fatty acid biosynthetic process Source: MGI
  2. positive regulation of cholesterol storage Source: MGI
  3. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  4. positive regulation of sequestering of triglyceride Source: MGI
  5. response to cold Source: Ensembl
  6. response to drug Source: Ensembl
  7. triglyceride biosynthetic process Source: Ensembl
  8. triglyceride catabolic process Source: BHF-UCL
  9. triglyceride homeostasis Source: MGI
  10. very-low-density lipoprotein particle remodeling Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BRENDAi3.1.1.34. 3474.
ReactomeiREACT_295031. Retinoid metabolism and transport.
REACT_314625. Chylomicron-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34)
Short name:
LPL
Gene namesi
Name:Lpl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96820. Lpl.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: BHF-UCL
  3. chylomicron Source: UniProtKB-KW
  4. extracellular matrix Source: Ensembl
  5. extracellular space Source: BHF-UCL
  6. extracellular vesicular exosome Source: MGI
  7. plasma membrane Source: UniProtKB-SubCell
  8. very-low-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 474447Lipoprotein lipasePRO_0000017776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Modified residuei121 – 1211Nitrated tyrosineBy similarity
Modified residuei191 – 1911Nitrated tyrosineBy similarity
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343 – 3431Nitrated tyrosineBy similarity
Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Nitration

Proteomic databases

MaxQBiP11152.
PaxDbiP11152.
PRIDEiP11152.

PTM databases

PhosphoSiteiP11152.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiP11152.
CleanExiMM_LPL.
ExpressionAtlasiP11152. baseline and differential.
GenevestigatoriP11152.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1.By similarity1 Publication

Protein-protein interaction databases

IntActiP11152. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP11152.
SMRiP11152. Positions 36-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 464124PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni346 – 44196Heparin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP11152.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG757CX5.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR03230. lipo_lipase. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P11152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WMEEEFNYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTEDGKQHNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMMKLKWI SDSYFSWPDW WSSPSFVIER IRVKAGETQK KVIFCAREKV
460 470
SHLQKGKDSA VFVKCHDKSL KKSG
Length:474
Mass (Da):53,109
Last modified:July 26, 2011 - v3
Checksum:iE5895C98B7AE16CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291K → Y no nucleotide entry (PubMed:2723548).Curated
Sequence conflicti147 – 1471N → K in AAA39441 (PubMed:1765386).Curated
Sequence conflicti354 – 3541D → N no nucleotide entry (PubMed:2723548).Curated
Sequence conflicti410 – 4101I → M no nucleotide entry (PubMed:2723548).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60847
, 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.
CCDSiCCDS40357.1.
PIRiA40570.
RefSeqiNP_032535.2. NM_008509.2.
UniGeneiMm.1514.

Genome annotation databases

EnsembliENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568.
ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568.
GeneIDi16956.
KEGGimmu:16956.
UCSCiuc009lwq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60847
, 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.
CCDSiCCDS40357.1.
PIRiA40570.
RefSeqiNP_032535.2. NM_008509.2.
UniGeneiMm.1514.

3D structure databases

ProteinModelPortaliP11152.
SMRiP11152. Positions 36-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11152. 1 interaction.

PTM databases

PhosphoSiteiP11152.

Proteomic databases

MaxQBiP11152.
PaxDbiP11152.
PRIDEiP11152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568.
ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568.
GeneIDi16956.
KEGGimmu:16956.
UCSCiuc009lwq.1. mouse.

Organism-specific databases

CTDi4023.
MGIiMGI:96820. Lpl.

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP11152.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG757CX5.
TreeFamiTF324997.

Enzyme and pathway databases

BRENDAi3.1.1.34. 3474.
ReactomeiREACT_295031. Retinoid metabolism and transport.
REACT_314625. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSiLpl. mouse.
NextBioi291008.
PROiP11152.
SOURCEiSearch...

Gene expression databases

BgeeiP11152.
CleanExiMM_LPL.
ExpressionAtlasiP11152. baseline and differential.
GenevestigatoriP11152.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR03230. lipo_lipase. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1988) [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(1990) [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.
    , 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(2004) [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(2003) [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(1991) [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(1990) [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(1986) [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPIHBP1.

Entry informationi

Entry nameiLIPL_MOUSE
AccessioniPrimary (citable) accession number: P11152
Secondary accession number(s): Q05956
, Q542L4, Q9D3M9, Q9DCM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1989
Last sequence update: July 26, 2011
Last modified: March 31, 2015
This is version 154 of the entry and version 3 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.