P11153 (LIPL_CAVPO) 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

Cavia porcellus (Guinea pig) [Reference proteome]

Taxonomic identifier

10141 [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 › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Tissue specificity	High level of expression in expression in adipocytes, heart muscle and mammary gland. 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 GPI-anchor Glycoprotein Lipoprotein Nitration
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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 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 electronic annotation. Source: EC 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 – 17	17	Potential
	Chain	18 – 465	448	Lipoprotein lipase		PRO_0000017773
Regions
	Domain	331 – 454	124	PLAT
	Region	336 – 431	96	Heparin-binding By similarity
Sites
	Active site	149	1	Nucleophile By similarity
	Active site	173	1	Charge relay system By similarity
	Active site	258	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	111	1	Nitrated tyrosine By similarity
	Modified residue	181	1	Nitrated tyrosine By similarity
	Modified residue	333	1	Nitrated tyrosine By similarity
	Glycosylation	60	1	N-linked (GlcNAc...) Potential
	Glycosylation	376	1	N-linked (GlcNAc...) Potential
	Disulfide bond	44 ↔ 57		By similarity
	Disulfide bond	233 ↔ 256		By similarity
	Disulfide bond	281 ↔ 300		By similarity
	Disulfide bond	292 ↔ 295		By similarity
	Disulfide bond	435 ↔ 455		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11153 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: E2515F36BEFD5F10	FASTA	465	52,781
	10 20 30 40 50 60 MNIDRKILNK ALAKEKVANC QKDYTDIESK FARRTPENTV EDTCHLIPGV TESVANCHFN 70 80 90 100 110 120 HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLRRAQHH YPESADYTKL 130 140 150 160 170 180 VGEDVARFIN WMEDEFKYSV DNVHLLGYSL GAHAAGVAGS RTNTKVSRIT GLDPAGPNFE 190 200 210 220 230 240 YAEATSRLSP DDAQFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGSFQ PGCNIQDALR 250 260 270 280 290 300 VISQKGFGDM DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC 310 320 330 340 350 360 NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIYFS GTETTTYTNQ AFEISLYGTV 370 380 390 400 410 420 AESENIPFTL PEVSANNTYS FLIYTEVDIG ELLMLKLKWI TESYFSWSSW WGRPTFTIEK 430 440 450 460 IRVKAGETQK KIVFCSREKV SKLQKGKEAP VFVKCHDKSL NKKSG

References

[1]	"Molecular cloning and sequence analysis of cDNA encoding lipoprotein lipase of guinea pig." Enerbaeck S., Semb H., Bengtsson-Olivecrona G., Carlsson P., Hermansson M.-L., Olivecrona T., Bjursell G. Gene 58:1-12(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"Genomic organization of the region encoding guinea pig lipoprotein lipase; evidence for exon fusion and unconventional splicing." Enerbaeck S., Bjursell G. Gene 84:391-397(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15483 mRNA. Translation: AAA37046.1. M33381 , M33377, M33378, M33379, M33380 Genomic DNA. Translation: AAA37039.1.
PIR	A27330. JS0398.
RefSeq	NP_001166449.1. NM_001172978.1.
3D structure databases
ProteinModelPortal	P11153.
ModBase	Search...
Protein-protein interaction databases
STRING	10141.ENSCPOP00000003655.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100135570.
Organism-specific databases
CTD	4023.
Phylogenomic databases
eggNOG	NOG40923.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	P11153.
OrthoDB	EOG480HWP.
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...

Entry information

Entry name

LIPL_CAVPO

Accession

Primary (citable) accession number: P11153

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program