P11152 (LIPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoprotein lipase
Short name=LPL
EC=3.1.1.34

Gene names

Name:

Lpl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-anchor › GPI-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 process	Lipid degradation Lipid metabolism
Cellular component	Cell membrane Chylomicron Membrane Secreted VLDL
Domain	Signal
Ligand	Heparin-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein GPI-anchor Lipoprotein Nitration
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive 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_component	anchored 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_function	heparin 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 474	447	Lipoprotein lipase		PRO_0000017776
Regions
	Domain	341 – 464	124	PLAT
	Region	346 – 441	96	Heparin-binding By similarity
Sites
	Active site	159	1	Nucleophile By similarity
	Active site	183	1	Charge relay system By similarity
	Active site	268	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	121	1	Nitrated tyrosine By similarity
	Modified residue	191	1	Nitrated tyrosine By similarity
	Modified residue	343	1	Nitrated tyrosine By similarity
	Glycosylation	70	1	N-linked (GlcNAc...) Potential
	Glycosylation	386	1	N-linked (GlcNAc...) Potential
	Disulfide bond	54 ↔ 67		By similarity
	Disulfide bond	243 ↔ 266		By similarity
	Disulfide bond	291 ↔ 310		By similarity
	Disulfide bond	302 ↔ 305		By similarity
	Disulfide bond	445 ↔ 465		By similarity
Experimental info
	Sequence conflict	129	1	K → Y no nucleotide entry Ref.1
	Sequence conflict	147	1	N → K in AAA39441. Ref.2
	Sequence conflict	354	1	D → N no nucleotide entry Ref.1
	Sequence conflict	410	1	I → M no nucleotide entry Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P11152 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: E5895C98B7AE16CD	FASTA	474	53,109
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.
CCDS	CCDS40357.1.
PIR	A40570.
RefSeq	NP_032535.2. NM_008509.2.
UniGene	Mm.1514.
3D structure databases
ProteinModelPortal	P11152.
SMR	P11152. Positions 36-450.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
IntAct	P11152. 1 interaction.
PTM databases
PhosphoSite	P11152.
Proteomic databases
MaxQB	P11152.
PaxDb	P11152.
PRIDE	P11152.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568. ENSMUST00000168401; ENSMUSP00000132259; ENSMUSG00000015568.
GeneID	16956.
KEGG	mmu:16956.
UCSC	uc009lwq.1. mouse.
Organism-specific databases
CTD	4023.
MGI	MGI:96820. Lpl.
Phylogenomic databases
eggNOG	NOG40923.
GeneTree	ENSGT00750000117234.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	Q542L4.
KO	K01059.
OMA	ESVANCH.
OrthoDB	EOG757CX5.
TreeFam	TF324997.
Enzyme and pathway databases
BRENDA	3.1.1.34. 3474.
Gene expression databases
ArrayExpress	P11152.
Bgee	P11152.
CleanEx	MM_LPL.
Genevestigator	P11152.
Family and domain databases
Gene3D	2.60.60.20. 1 hit. 3.40.50.1820. 1 hit.
InterPro	IPR029058. AB_hydrolase. IPR000734. Lipase. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002330. Lipo_Lipase. IPR016272. Lipoprotein_lipase_LIPH. IPR001024. PLAT/LH2_dom. [Graphical view]
PANTHER	PTHR11610. PTHR11610. 1 hit. PTHR11610:SF3. PTHR11610:SF3. 1 hit.
Pfam	PF00151. Lipase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PIRSF	PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTS	PR00822. LIPOLIPASE. PR00821. TAGLIPASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
SUPFAM	SSF49723. SSF49723. 1 hit. SSF53474. SSF53474. 1 hit.
TIGRFAMs	TIGR03230. lipo_lipase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LPL. mouse.
NextBio	291008.
PRO	P11152.
SOURCE	Search...

Entry information

Entry name

LIPL_MOUSE

Accession

Primary (citable) accession number: P11152
Secondary accession number(s): Q05956 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program