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P11152

- LIPL_MOUSE

UniProt

P11152 - LIPL_MOUSE

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Protein

Lipoprotein lipase

Gene
Lpl
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591Nucleophile By similarity
Active sitei183 – 1831Charge relay system By similarity
Active sitei268 – 2681Charge relay system By similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. lipoprotein lipase activity Source: MGI
  3. protein binding Source: MGI
  4. triglyceride binding Source: Ensembl
  5. triglyceride lipase activity Source: BHF-UCL

GO - Biological processi

  1. positive regulation of cholesterol storage Source: Ensembl
  2. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  3. positive regulation of sequestering of triglyceride Source: Ensembl
  4. response to cold Source: Ensembl
  5. response to drug Source: Ensembl
  6. triglyceride biosynthetic process Source: Ensembl
  7. triglyceride catabolic process Source: BHF-UCL
  8. triglyceride homeostasis Source: Ensembl
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_198569. Retinoid metabolism and transport.
REACT_216017. 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: 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.

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. plasma membrane Source: UniProtKB-SubCell
  7. 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 – 2727 Reviewed predictionAdd
BLAST
Chaini28 – 474447Lipoprotein lipasePRO_0000017776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67 By similarity
Glycosylationi70 – 701N-linked (GlcNAc...) Reviewed prediction
Modified residuei121 – 1211Nitrated tyrosine By similarity
Modified residuei191 – 1911Nitrated tyrosine By similarity
Disulfide bondi243 ↔ 266 By similarity
Disulfide bondi291 ↔ 310 By similarity
Disulfide bondi302 ↔ 305 By similarity
Modified residuei343 – 3431Nitrated tyrosine By similarity
Glycosylationi386 – 3861N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi445 ↔ 465 By similarity

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

ArrayExpressiP11152.
BgeeiP11152.
CleanExiMM_LPL.
GenevestigatoriP11152.

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids By similarity. Interacts with GPIHBP1.1 Publication

Protein-protein interaction databases

IntActiP11152. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP11152.
SMRiP11152. Positions 36-450.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 464124PLATAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00750000117234.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ542L4.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG757CX5.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[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

MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA    50
EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY 100
KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WMEEEFNYPL 150
DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP 200
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR 250
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 300
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS 350
GTEDGKQHNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG 400
ELLMMKLKWI SDSYFSWPDW WSSPSFVIER IRVKAGETQK KVIFCAREKV 450
SHLQKGKDSA VFVKCHDKSL KKSG 474
Length:474
Mass (Da):53,109
Last modified:July 27, 2011 - v3
Checksum:iE5895C98B7AE16CD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291K → Y no nucleotide entry 1 Publication
Sequence conflicti147 – 1471N → K in AAA39441. 1 Publication
Sequence conflicti354 – 3541D → N no nucleotide entry 1 Publication
Sequence conflicti410 – 4101I → M no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS40357.1.
PIRi A40570.
RefSeqi NP_032535.2. NM_008509.2.
UniGenei Mm.1514.

3D structure databases

ProteinModelPortali P11152.
SMRi P11152. Positions 36-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11152. 1 interaction.

PTM databases

PhosphoSitei P11152.

Proteomic databases

MaxQBi P11152.
PaxDbi P11152.
PRIDEi P11152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015712 ; ENSMUSP00000015712 ; ENSMUSG00000015568 .
ENSMUST00000168401 ; ENSMUSP00000132259 ; ENSMUSG00000015568 .
GeneIDi 16956.
KEGGi mmu:16956.
UCSCi uc009lwq.1. mouse.

Organism-specific databases

CTDi 4023.
MGIi MGI:96820. Lpl.

Phylogenomic databases

eggNOGi NOG40923.
GeneTreei ENSGT00750000117234.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi Q542L4.
KOi K01059.
OMAi ESVANCH.
OrthoDBi EOG757CX5.
TreeFami TF324997.

Enzyme and pathway databases

BRENDAi 3.1.1.34. 3474.
Reactomei REACT_198569. Retinoid metabolism and transport.
REACT_216017. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSi LPL. mouse.
NextBioi 291008.
PROi P11152.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11152.
Bgeei P11152.
CleanExi MM_LPL.
Genevestigatori P11152.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsi TIGR03230. lipo_lipase. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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.

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: July 1, 1989
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 147 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