P11151 (LIPL_BOVIN) 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

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	478 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.
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.7
Subunit structure	Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interacts with GPIHBP1 By similarity. Ref.7
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Secreted. 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. Ref.5 Ref.6
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 GPI-anchor Glycoprotein Lipoprotein Nitration
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from direct assay PubMed 18635818. Source: BHF-UCL phospholipid metabolic process Inferred from direct assay Ref.7. Source: BHF-UCL 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 triglyceride catabolic process Inferred from direct assay PubMed 18635818. Source: BHF-UCL triglyceride homeostasis Inferred from electronic annotation. Source: Compara very-low-density lipoprotein particle remodeling Inferred from direct assay PubMed 18635818. Source: BHF-UCL
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 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 Ref.7PubMed 18635818. Source: BHF-UCL phospholipase activity Inferred from direct assay Ref.7. Source: BHF-UCL triglyceride lipase activity Inferred from direct assay Ref.7. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Ref.3 Ref.4
	Chain	29 – 478	450	Lipoprotein lipase		PRO_0000017772
Regions
	Domain	344 – 467	124	PLAT
	Region	349 – 444	96	Heparin-binding By similarity
Sites
	Active site	162	1	Nucleophile By similarity
	Active site	186	1	Charge relay system By similarity
	Active site	271	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	124	1	Nitrated tyrosine By similarity
	Modified residue	194	1	Nitrated tyrosine By similarity
	Modified residue	346	1	Nitrated tyrosine By similarity
	Glycosylation	73	1	N-linked (GlcNAc...)
	Glycosylation	389	1	N-linked (GlcNAc...)
	Disulfide bond	57 ↔ 70		Ref.3
	Disulfide bond	246 ↔ 269		Ref.3
	Disulfide bond	294 ↔ 313		Ref.3
	Disulfide bond	305 ↔ 308		Ref.3
	Disulfide bond	448 ↔ 468		Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P11151 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 06FDD429DD194A1F	FASTA	478	53,378
	10 20 30 40 50 60 MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE DTAEDTCHLI 70 80 90 100 110 120 PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA 130 140 150 160 170 180 QQHYPVSAGY TKLVGQDVAK FMNWMADEFN YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN 190 200 210 220 230 240 RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG 250 260 270 280 290 300 TFQPGCNIGE ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF 310 320 330 340 350 360 EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESNTY 370 380 390 400 410 420 TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV DIGELLMLKL KWISDSYFSW 430 440 450 460 470 SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR EKMSYLQKGK SPVIFVKCHD KSLNRKSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.
[2]	"Molecular cloning and sequence of a cDNA coding for bovine lipoprotein lipase." Senda M., Oka K., Brown W.V., Qasba P.K., Furuichi Y. Proc. Natl. Acad. Sci. U.S.A. 84:4369-4373(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-478.
[3]	"Structure of bovine milk lipoprotein lipase." Yang C.-Y., Gu Z.-W., Yang H.-X., Rohde M.F., Gotto A.M. Jr., Pownall H.J. J. Biol. Chem. 264:16822-16827(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-478, DISULFIDE BONDS. Tissue: Mammary gland.
[4]	"Lipoprotein lipases from cow, guinea-pig and man. Structural characterization and identification of protease-sensitive internal regions." Bengtsson-Olivecrona G., Olivecrona T., Joernvall H. Eur. J. Biochem. 161:281-288(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-55.
[5]	"Metabolism of endothelial cell-bound lipoprotein lipase. Evidence for heparan sulfate proteoglycan-mediated internalization and recycling." Saxena U., Klein M.G., Goldberg I.J. J. Biol. Chem. 265:12880-12886(1990) [PubMed] [Europe PMC] [Abstract] Cited for: HEPARIN BINDING, SUBCELLULAR LOCATION.
[6]	"Binding and intracellular trafficking of lipoprotein lipase and triacylglycerol-rich lipoproteins by liver cells." Casaroli-Marano R.P., Garcia R., Vilella E., Olivecrona G., Reina M., Vilaro S. J. Lipid Res. 39:789-806(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding." MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J. Biochemistry 39:3433-3440(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APOC2, ENZYME ACTIVITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC118091 mRNA. Translation: AAI18092.1. M16966 mRNA. Translation: AAA30624.1.
IPI	IPI00692291.
PIR	A27053.
RefSeq	NP_001068588.1. NM_001075120.1.
UniGene	Bt.5387.
3D structure databases
ProteinModelPortal	P11151.
ModBase	Search...
Proteomic databases
PaxDb	P11151.
PRIDE	P11151.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000017086; ENSBTAP00000017086; ENSBTAG00000012855.
GeneID	280843.
KEGG	bta:280843.
Organism-specific databases
CTD	4023.
Phylogenomic databases
eggNOG	NOG40923.
GeneTree	ENSGT00560000077136.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	P11151.
KO	K01059.
OMA	ESVANCH.
OrthoDB	EOG480HWP.
Enzyme and pathway databases
BRENDA	3.1.1.34. 908.
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
ChEMBL	CHEMBL3064.
NextBio	20804991.

Entry information

Entry name

LIPL_BOVIN

Accession

Primary (citable) accession number: P11151
Secondary accession number(s): Q17R03

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	December 12, 2006
Last modified:	April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program