Reviewed, UniProtKB/Swiss-Prot P11152 (LIPL_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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). The enzyme functions in the presence of apolipoprotein C-2 on the luminal surface of vascular endothelium.
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Subunit structure	Homodimer. Interacts with apolipoprotein C-2. Interacts with GPIHBP1. Ref.8
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cell membrane Chylomicron Membrane VLDL
Domain	Signal
Ligand	Heparin-binding
Molecular function	Hydrolase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Gene Ontology (GO)
Biological process	positive regulation of macrophage derived foam cell differentiation Inferred from genetic interaction. Source: UniProtKB triglyceride catabolic process Inferred from direct assay. Source: UniProtKB
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell chylomicron Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW 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. Source: MGI triglyceride binding Inferred by curator. Source: UniProtKB triglyceride lipase activity Inferred from direct assay. Source: UniProtKB
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	319 – 331	13	Heparin-binding Potential
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
	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 Ref.1
	Sequence conflict	147	1	N → K in AAA39441. Ref.2
	Sequence conflict	354	1	N → D in BAB22256. Ref.3
	Sequence conflict	410	1	M → I in BAB22256. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P11152-1 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: E7AF969E716E1CCD	FASTA	474	53,126
	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 GTENGKQHNQ 370 380 390 400 410 420 AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMMKLKWM 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: 2723548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 1765386] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head 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: 15489334] [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: 1339460] [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: 1748295] [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: 3597382] [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: 17403372] [Abstract] Cited for: INTERACTION WITH GPIHBP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60847 , M60838, M60839, M60840, M60842, M60843, M60844, M60845, M60846 Genomic DNA. Translation: AAA39441.1. AK002645 mRNA. Translation: BAB22256.1. AK017272 mRNA. No translation available. BC003305 mRNA. Translation: AAH03305.1. M65258 mRNA. Translation: AAA39442.1. J03302 mRNA. Translation: AAA39440.1. M63335 Genomic DNA. Translation: AAC04464.1.
IPI	IPI00319188.
PIR	A40570.
RefSeq	NP_032535.2. XP_001476512.1.
UniGene	Mm.1514
3D structure databases
HSSP	HSSP built from PDB template 1RP1 based on UniProtKB P06857.
ModBase	Search...
Protein-protein interaction databases
STRING	P11152.
Proteomic databases
PRIDE	P11152.
Genome annotation databases
Ensembl	ENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568; Mus musculus. [Genome view]
GeneID	16956. 669888.
KEGG	mmu:16956. mmu:669888.
Organism-specific databases
MGI	MGI:96820. Lpl.
Phylogenomic databases
HOGENOM	P11152.
HOVERGEN	P11152.
Enzyme and pathway databases
BRENDA	3.1.1.34. 244.
Gene expression databases
ArrayExpress	P11152.
Bgee	P11152.
CleanEx	MM_LPL.
Genevestigator	P11152.
GermOnline	ENSMUSG00000015568. Mus musculus.
Family and domain databases
InterPro	IPR000734. Lipase. IPR013818. Lipase_N. IPR008262. Lipase_Ser_AS. IPR002330. Lipo_Lipase. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view]
PANTHER	PTHR11610. Lipase. 1 hit. PTHR11610:SF3. Lipase_lipo. 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]
TIGRFAMs	TIGR03230. lipo_lipase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	436339.
SOURCE	Search...

Entry information

Entry name

LIPL_MOUSE

Accession

Primary (citable) accession number: P11152
Secondary accession number(s): Q05956, Q9D3M9, Q9DCM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1993
Last modified:	October 13, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)