Q06000 (LIPL_RAT) 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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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. Interacts with GPIHBP1 By similarity.
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.
Induction	Induced by insulin. Inhibited by isoproterenol. Ref.3
Post-translational modification	Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.
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 GPI-anchor Glycoprotein Lipoprotein Nitration
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from direct assay PubMed 12551943. Source: RGD positive regulation of cholesterol storage Inferred from electronic annotation. Source: Compara positive regulation of macrophage derived foam cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of sequestering of triglyceride Inferred from electronic annotation. Source: Compara response to cold Inferred from expression pattern PubMed 18722549. Source: RGD response to drug Inferred from expression pattern PubMed 11016888. Source: RGD triglyceride biosynthetic process Inferred from mutant phenotype PubMed 11788374. Source: RGD triglyceride catabolic process Inferred from electronic annotation. Source: Compara triglyceride homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from electronic annotation. Source: Compara chylomicron Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix Inferred from direct assay PubMed 12551943. Source: RGD 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 11788374PubMed 12551943. Source: RGD triglyceride binding Inferred from direct assay PubMed 12551943. Source: RGD triglyceride lipase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	By similarity
	Chain	28 – 474	447	Lipoprotein lipase		PRO_0000017779
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 Ref.4
	Modified residue	191	1	Nitrated tyrosine Ref.4
	Modified residue	343	1	Nitrated tyrosine Ref.4
	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	336	1	M → V no nucleotide entry Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q06000 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: F4F6F4BCCA4F1626	FASTA	474	53,082
	10 20 30 40 50 60 MESKALLLVA LGVWLQSLTA FRGGVAAADG GRDFSDIESK FALRTPEDTA EDTCHLIPGL 70 80 90 100 110 120 ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLYRAQQH 130 140 150 160 170 180 YPVSAGYTKL VGNDVARFIN WLEEEFNYPL DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT 190 200 210 220 230 240 GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ 250 260 270 280 290 300 PGCNIGEAIR VIAEKGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 310 320 330 340 350 360 LCLSCRKNRC NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTENDKQNNQ 370 380 390 400 410 420 AFEISLYGTV AESENIPFTL PEVATNKTYS FLIYTEVDIG ELLMMKLKWK NDSYFRWSDW 430 440 450 460 470 WSSPSFVIEK IRVKAGETQK KVIFCAREKV SHLQKGKDAA VFVKCHDKSL KKSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of rat lipoprotein lipase-encoding cDNA." Brault D., Noe L., Etienne J., Hamelin J., Raisonnier A., Souli A., Chuat J.-C., Dugail I., Quignard-Boulange A., Lavau M., Galibert F. Gene 121:237-246(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Testis.
[2]	"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]. Tissue: Kidney.
[3]	"Lipoprotein lipase gene expression in rat adipocytes is regulated by isoproterenol and insulin through different mechanisms." Raynolds M.V., Awald P.D., Gordon D.F., Gutierrez-Hartmann A., Rule D.C., Wood W.M., Eckel R.H. Mol. Endocrinol. 4:1416-1422(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 336-474, INDUCTION. Tissue: Heart.
[4]	"Lipoprotein lipase is nitrated in vivo after lipopolysaccharide challenge." Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M. Free Radic. Biol. Med. 47:1553-1560(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NITRATION AT TYR-121; TYR-191 AND TYR-343, MASS SPECTROMETRY.
[5]	"Discovery of lipoprotein lipase pI isoforms and contributions to their characterization." Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M. J. Proteomics 72:1031-1039(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L03294 mRNA. Translation: AAA41534.1. BC081836 mRNA. Translation: AAH81836.1.
IPI	IPI00189471.
PIR	JH0790.
RefSeq	NP_036730.1. NM_012598.2.
UniGene	Rn.3834.
3D structure databases
ProteinModelPortal	Q06000.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000016543.
Proteomic databases
PaxDb	Q06000.
PRIDE	Q06000.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000016543; ENSRNOP00000016543; ENSRNOG00000012181.
GeneID	24539.
KEGG	rno:24539.
UCSC	RGD:3017. rat.
Organism-specific databases
CTD	4023.
RGD	3017. Lpl.
Phylogenomic databases
eggNOG	NOG40923.
GeneTree	ENSGT00560000077136.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	Q06000.
KO	K01059.
OMA	ESVANCH.
OrthoDB	EOG480HWP.
Enzyme and pathway databases
BRENDA	3.1.1.34. 5301.
Gene expression databases
Genevestigator	Q06000.
GermOnline	ENSRNOG00000012181. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR000734. Lipase. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002330. Lipo_Lipase. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [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. Lipase_LipOase. 1 hit.
TIGRFAMs	TIGR03230. lipo_lipase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q06000.
ChEMBL	CHEMBL5906.
NextBio	603620.

Entry information

Entry name

LIPL_RAT

Accession

Primary (citable) accession number: Q06000

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program