LIPL_MOUSE
ID LIPL_MOUSE Reviewed; 474 AA.
AC P11152; Q05956; Q542L4; Q9D3M9; Q9DCM8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Lipoprotein lipase;
DE Short=LPL;
DE EC=3.1.1.34 {ECO:0000269|PubMed:8675619};
DE AltName: Full=Phospholipase A1;
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:P06858};
DE Flags: Precursor;
GN Name=Lpl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Macrophage;
RX PubMed=2723548;
RA Semenkovich C.F., Chen S.H., Wims M., Luo C.C., Li W.H., Chan L.;
RT "Lipoprotein lipase and hepatic lipase mRNA tissue specific expression,
RT developmental regulation, and evolution.";
RL J. Lipid Res. 30:423-431(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1765386; DOI=10.1016/0888-7543(91)90102-k;
RA Zechner R., Newman T.C., Steiner E., Breslow J.L.;
RT "The structure of the mouse lipoprotein lipase gene: a B1 repetitive
RT element is inserted into the 3' untranslated region of the mRNA.";
RL Genomics 11:62-76(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryo, Head, Heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-183.
RX PubMed=1339460; DOI=10.1002/jcb.240500112;
RA Gimble J.M., Hua X., Youkhana K., Bass H.W., Medina K., Sullivan M.,
RA Greenberger J.S., Wang C.S.;
RT "Adipogenesis in a myeloid supporting bone marrow stromal cell line.";
RL J. Cell. Biochem. 50:73-82(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1748295; DOI=10.1016/0378-1119(91)90325-6;
RA Hua X., Enerbaeck S., Hudson J., Youkhana K., Gimble J.M.;
RT "Cloning and characterization of the promoter of the murine lipoprotein
RT lipase-encoding gene: structural and functional analysis.";
RL Gene 107:247-258(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-474.
RX PubMed=3597382; DOI=10.1016/s0021-9258(18)47435-2;
RA Kirchgessner T.G., Svenson K.L., Lusis A.J., Schotz M.C.;
RT "The sequence of cDNA encoding lipoprotein lipase. A member of a lipase
RT gene family.";
RL J. Biol. Chem. 262:8463-8466(1987).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=8675619; DOI=10.1172/jci118319;
RA Weinstock P.H., Bisgaier C.L., Aalto-Setaelae K., Radner H.,
RA Ramakrishnan R., Levak-Frank S., Essenburg A.D., Zechner R., Breslow J.L.;
RT "Severe hypertriglyceridemia, reduced high density lipoprotein, and
RT neonatal death in lipoprotein lipase knockout mice. Mild
RT hypertriglyceridemia with impaired very low density lipoprotein clearance
RT in heterozygotes.";
RL J. Clin. Invest. 96:2555-2568(1995).
RN [9]
RP INTERACTION WITH GPIHBP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17403372; DOI=10.1016/j.cmet.2007.02.002;
RA Beigneux A.P., Davies B.S.J., Gin P., Weinstein M.M., Farber E., Qiao X.,
RA Peale F., Bunting S., Walzem R.L., Wong J.S., Blaner W.S., Ding Z.-M.,
RA Melford K., Wongsiriroj N., Shu X., de Sauvage F., Ryan R.O., Fong L.G.,
RA Bensadoun A., Young S.G.;
RT "Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding
RT protein 1 plays a critical role in the lipolytic processing of
RT chylomicrons.";
RL Cell Metab. 5:279-291(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GPIHBP1, AND TISSUE
RP SPECIFICITY.
RX PubMed=20620994; DOI=10.1016/j.cmet.2010.04.016;
RA Davies B.S., Beigneux A.P., Barnes R.H. II, Tu Y., Gin P., Weinstein M.M.,
RA Nobumori C., Nyren R., Goldberg I., Olivecrona G., Bensadoun A.,
RA Young S.G., Fong L.G.;
RT "GPIHBP1 is responsible for the entry of lipoprotein lipase into
RT capillaries.";
RL Cell Metab. 12:42-52(2010).
RN [12]
RP INTERACTION WITH LMF1 AND SEL1L, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=25066055; DOI=10.1016/j.cmet.2014.06.015;
RA Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L., Lawrence P.,
RA Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T., Shi H., Xue B.,
RA Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.;
RT "The ER-associated degradation adaptor protein Sel1L regulates LPL
RT secretion and lipid metabolism.";
RL Cell Metab. 20:458-470(2014).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GPIHBP1.
RX PubMed=24726386; DOI=10.1016/j.cmet.2014.01.017;
RA Goulbourne C.N., Gin P., Tatar A., Nobumori C., Hoenger A., Jiang H.,
RA Grovenor C.R., Adeyo O., Esko J.D., Goldberg I.J., Reue K., Tontonoz P.,
RA Bensadoun A., Beigneux A.P., Young S.G., Fong L.G.;
RT "The GPIHBP1-LPL complex is responsible for the margination of
RT triglyceride-rich lipoproteins in capillaries.";
RL Cell Metab. 19:849-860(2014).
RN [14]
RP FUNCTION, INTERACTION WITH GPIHBP1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=27811232; DOI=10.1194/jlr.m072520;
RA Allan C.M., Larsson M., Jung R.S., Ploug M., Bensadoun A., Beigneux A.P.,
RA Fong L.G., Young S.G.;
RT "Mobility of 'HSPG-bound' LPL explains how LPL is able to reach GPIHBP1 on
RT capillaries.";
RL J. Lipid Res. 58:216-225(2017).
CC -!- FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the
CC hydrolysis of triglycerides from circulating chylomicrons and very low
CC density lipoproteins (VLDL), and thereby plays an important role in
CC lipid clearance from the blood stream, lipid utilization and storage
CC (PubMed:8675619). Although it has both phospholipase and triglyceride
CC lipase activities it is primarily a triglyceride lipase with low but
CC detectable phospholipase activity (By similarity). Mediates margination
CC of triglyceride-rich lipoprotein particles in capillaries
CC (PubMed:24726386). Recruited to its site of action on vascular
CC endothelium by binding to GPIHBP1 and cell surface heparan sulfate
CC proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232).
CC {ECO:0000250|UniProtKB:P06858, ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232,
CC ECO:0000269|PubMed:8675619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34;
CC Evidence={ECO:0000269|PubMed:8675619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P06858};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000250|UniProtKB:P06858};
CC -!- ACTIVITY REGULATION: The apolipoprotein APOC2 acts as a coactivator of
CC LPL activity (By similarity). Ca(2+) binding promotes protein stability
CC and formation of the active homodimer. Interaction with GPIHBP1
CC protects LPL against inactivation by ANGPTL4 (By similarity).
CC {ECO:0000250|UniProtKB:P06858, ECO:0000250|UniProtKB:P11151}.
CC -!- SUBUNIT: Homodimer (PubMed:25066055). Interacts with GPIHBP1 with 1:1
CC stoichiometry (PubMed:17403372, PubMed:20620994, PubMed:24726386).
CC Interacts with APOC2; the interaction activates LPL activity in the
CC presence of lipids (By similarity). Interaction with heparan sulfate
CC proteoglycans is required to protect LPL against loss of activity.
CC Associates with lipoprotein particles in blood plasma (By similarity).
CC Interacts with LMF1 and SEL1L; interaction with SEL1L is required to
CC prevent aggregation of newly synthesized LPL in the endoplasmic
CC reticulum (ER), and for normal export of LPL from the ER to the
CC extracellular space (PubMed:25066055). Interacts with SORL1; SORL1 acts
CC as a sorting receptor, promoting LPL localization to endosomes and
CC later to lysosomes, leading to degradation of newly synthesized LPL (By
CC similarity). {ECO:0000250|UniProtKB:P06858,
CC ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:17403372,
CC ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386,
CC ECO:0000269|PubMed:25066055}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}; Peripheral
CC membrane protein {ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232};
CC Extracellular side {ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}. Secreted
CC {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:25066055}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:27811232}. Note=Newly synthesized LPL binds to cell
CC surface heparan proteoglycans and is then released by heparanase.
CC Subsequently, it becomes attached to heparan proteoglycan on
CC endothelial cells (PubMed:27811232). Locates to the plasma membrane of
CC microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL).
CC Some of the bound LPL is then internalized and located inside non-
CC coated endocytic vesicles (By similarity).
CC {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}.
CC -!- TISSUE SPECIFICITY: Detected in white and brown adipose tissue and
CC heart muscle, especially at the lumenal surface of capillaries
CC (PubMed:25066055, PubMed:27811232, PubMed:20620994). Detected on
CC capillary endothelium in the lactating mammary gland (PubMed:27811232).
CC Detected in blood plasma (at protein level) (PubMed:17403372,
CC PubMed:25066055). Expressed in liver, epididymal fat, heart, psoas
CC muscle, lactating mammary gland, adrenal, lung, and ovary. Highest
CC levels in heart and adrenal gland. {ECO:0000269|PubMed:17403372,
CC ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25066055,
CC ECO:0000269|PubMed:2723548, ECO:0000269|PubMed:27811232}.
CC -!- DEVELOPMENTAL STAGE: Maximum expression in adipose tissue during early
CC development. In heart, low levels 6 days before birth increasing 278-
CC fold as animals reach adulthood. {ECO:0000269|PubMed:2723548}.
CC -!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-
CC regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:25066055}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate. At
CC birth, mutant pups have threefold higher plasma triglyceride levels and
CC sevenfold higher VLDL cholesterol levels relative to wild-type. After
CC suckling they become progressively pale, then cyanotic, and die at
CC about 18 hours after birth. At 18 hours after birth, their plasma
CC triglyceride levels reach 15'090 mg/dl, compared to 188 mg/dl for wild-
CC type. At the same time point, VLDL cholesterol levels reach 280 mg/dl
CC in mutant pups, compared to 6 mg/dl in wild-type. Mutant pups show
CC severly reduced adipose tissue, and their livers are deficient in
CC intracellular lipid droplets. Likewise, the numbers of intracellular
CC lipid droplets in skeletal muscle are severely reduced. Lungs display
CC lipid-filled alveoli and dilated capillaries that are engorged with
CC lipoprotein particles. These particles are marginated and seem to block
CC the access of red blood cells to the vascular endothelium.
CC {ECO:0000269|PubMed:8675619}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; M60847; AAA39441.1; -; Genomic_DNA.
DR EMBL; M60838; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; M60839; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; M60840; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; M60842; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; M60843; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; M60844; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; M60845; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; M60846; AAA39441.1; JOINED; Genomic_DNA.
DR EMBL; AK002645; BAB22256.1; -; mRNA.
DR EMBL; AK017272; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK045064; BAC32204.1; -; mRNA.
DR EMBL; AK086023; BAC39594.1; -; mRNA.
DR EMBL; AK150355; BAE29491.1; -; mRNA.
DR EMBL; AK150375; BAE29507.1; -; mRNA.
DR EMBL; AK150457; BAE29577.1; -; mRNA.
DR EMBL; AK150488; BAE29604.1; -; mRNA.
DR EMBL; AK150505; BAE29618.1; -; mRNA.
DR EMBL; AK150593; BAE29686.1; -; mRNA.
DR EMBL; AK150672; BAE29754.1; -; mRNA.
DR EMBL; AK151006; BAE30029.1; -; mRNA.
DR EMBL; AK151093; BAE30105.1; -; mRNA.
DR EMBL; AK151105; BAE30115.1; -; mRNA.
DR EMBL; AK151369; BAE30343.1; -; mRNA.
DR EMBL; AK151434; BAE30397.1; -; mRNA.
DR EMBL; AK151521; BAE30470.1; -; mRNA.
DR EMBL; AK151540; BAE30486.1; -; mRNA.
DR EMBL; AK151563; BAE30505.1; -; mRNA.
DR EMBL; AK151630; BAE30564.1; -; mRNA.
DR EMBL; AK151679; BAE30604.1; -; mRNA.
DR EMBL; AK151727; BAE30645.1; -; mRNA.
DR EMBL; AK151772; BAE30678.1; -; mRNA.
DR EMBL; AK151801; BAE30701.1; -; mRNA.
DR EMBL; AK151828; BAE30723.1; -; mRNA.
DR EMBL; AK151866; BAE30754.1; -; mRNA.
DR EMBL; AK151870; BAE30758.1; -; mRNA.
DR EMBL; AK151872; BAE30760.1; -; mRNA.
DR EMBL; AK151893; BAE30777.1; -; mRNA.
DR EMBL; AK152014; BAE30876.1; -; mRNA.
DR EMBL; AK152035; BAE30894.1; -; mRNA.
DR EMBL; AK152049; BAE30905.1; -; mRNA.
DR EMBL; AK152053; BAE30909.1; -; mRNA.
DR EMBL; AK152079; BAE30930.1; -; mRNA.
DR EMBL; AK152350; BAE31144.1; -; mRNA.
DR EMBL; AK152657; BAE31394.1; -; mRNA.
DR EMBL; AK153148; BAE31758.1; -; mRNA.
DR EMBL; AK153242; BAE31834.1; -; mRNA.
DR EMBL; AK153425; BAE31984.1; -; mRNA.
DR EMBL; AK159268; BAE34947.1; -; mRNA.
DR EMBL; AK170486; BAE41828.1; -; mRNA.
DR EMBL; BC003305; AAH03305.1; -; mRNA.
DR EMBL; M65258; AAA39442.1; -; mRNA.
DR EMBL; J03302; AAA39440.1; -; mRNA.
DR EMBL; M63335; AAC04464.1; -; Genomic_DNA.
DR CCDS; CCDS40357.1; -.
DR PIR; A40570; A40570.
DR RefSeq; NP_032535.2; NM_008509.2.
DR AlphaFoldDB; P11152; -.
DR SMR; P11152; -.
DR BioGRID; 201196; 1.
DR IntAct; P11152; 5.
DR MINT; P11152; -.
DR STRING; 10090.ENSMUSP00000015712; -.
DR ChEMBL; CHEMBL3309051; -.
DR ESTHER; mouse-lipli; Lipoprotein_Lipase.
DR GlyGen; P11152; 2 sites.
DR iPTMnet; P11152; -.
DR PhosphoSitePlus; P11152; -.
DR SwissPalm; P11152; -.
DR jPOST; P11152; -.
DR MaxQB; P11152; -.
DR PaxDb; P11152; -.
DR PeptideAtlas; P11152; -.
DR PRIDE; P11152; -.
DR ProteomicsDB; 292096; -.
DR Antibodypedia; 9132; 564 antibodies from 35 providers.
DR DNASU; 16956; -.
DR Ensembl; ENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568.
DR Ensembl; ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568.
DR GeneID; 16956; -.
DR KEGG; mmu:16956; -.
DR UCSC; uc009lwq.1; mouse.
DR CTD; 4023; -.
DR MGI; MGI:96820; Lpl.
DR VEuPathDB; HostDB:ENSMUSG00000015568; -.
DR eggNOG; ENOG502QQ7P; Eukaryota.
DR GeneTree; ENSGT00940000157178; -.
DR HOGENOM; CLU_027171_1_0_1; -.
DR InParanoid; P11152; -.
DR OMA; TIWITLG; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; P11152; -.
DR TreeFam; TF324997; -.
DR BRENDA; 3.1.1.34; 3474.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-MMU-8963901; Chylomicron remodeling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 16956; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Lpl; mouse.
DR PRO; PR:P11152; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P11152; protein.
DR Bgee; ENSMUSG00000015568; Expressed in epididymal fat pad and 276 other tissues.
DR Genevisible; P11152; MM.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004465; F:lipoprotein lipase activity; IDA:MGI.
DR GO; GO:0071813; F:lipoprotein particle binding; ISS:UniProtKB.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0017129; F:triglyceride binding; ISO:MGI.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:BHF-UCL.
DR GO; GO:0071398; P:cellular response to fatty acid; IDA:ARUK-UCL.
DR GO; GO:0031670; P:cellular response to nutrient; IDA:ARUK-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0034371; P:chylomicron remodeling; ISS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; ISO:MGI.
DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; ISO:MGI.
DR GO; GO:1900077; P:negative regulation of cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IGI:ARUK-UCL.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISO:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:ARUK-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IGI:ARUK-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:ARUK-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IGI:BHF-UCL.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISO:MGI.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:MGI.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISO:MGI.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR002330; Lipo_Lipase.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR PANTHER; PTHR11610:SF3; PTHR11610:SF3; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00822; LIPOLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03230; lipo_lipase; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Chylomicron; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparin-binding; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Nitration; Reference proteome;
KW Secreted; Signal; VLDL.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..474
FT /note="Lipoprotein lipase"
FT /id="PRO_0000017776"
FT DOMAIN 341..464
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 32..53
FT /note="Interaction with GPIHBP1"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT REGION 243..266
FT /note="Essential for determining substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT REGION 417..421
FT /note="Important for interaction with lipoprotein
FT particles"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT REGION 430..434
FT /note="Important for heparin binding"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT REGION 443..467
FT /note="Interaction with GPIHBP1"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT ACT_SITE 159
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P06858"
FT MOD_RES 121
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q06000"
FT MOD_RES 191
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q06000"
FT MOD_RES 343
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q06000"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 243..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 291..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 302..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 445..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT CONFLICT 129
FT /note="K -> Y (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="N -> K (in Ref. 2; AAA39441)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="D -> N (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="I -> M (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53109 MW; E5895C98B7AE16CD CRC64;
MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA EDTCHLIPGL
ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLYRAQQH
YPVSAGYTKL VGNDVARFIN WMEEEFNYPL DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT
GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ
PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTEDGKQHNQ
AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMMKLKWI SDSYFSWPDW
WSSPSFVIER IRVKAGETQK KVIFCAREKV SHLQKGKDSA VFVKCHDKSL KKSG
