Reviewed, UniProtKB/Swiss-Prot Q9WVG5 (LIPE_MOUSE)

Names and origin

Protein names

Recommended name:
    Endothelial lipase
    EC=3.1.1.3
Alternative name(s):
    Endothelial cell-derived lipase
      Short name=EDL

Gene names

Name:

Lipg

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	500 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	Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin By similarity.
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Subcellular location	Secreted.
Tissue specificity	Expressed in placenta, lung, liver, testis and spleen.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Heparin-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of lipoprotein metabolic process Inferred from mutant phenotype. Source: MGI
Molecular function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW lipoprotein lipase activity Inferred from electronic annotation. Source: InterPro triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 500	480	Endothelial lipase		PRO_0000017798
Regions
	Domain	347 – 482	136	PLAT
	Region	325 – 337	13	Heparin-binding By similarity
	Compositional bias	118 – 121	4	Poly-Val
Sites
	Active site	169	1	Nucleophile By similarity
	Active site	193	1	Charge relay system By similarity
	Active site	274	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	65	1	N-linked (GlcNAc...) Potential
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	136	1	N-linked (GlcNAc...) Potential
	Glycosylation	359	1	N-linked (GlcNAc...) Potential
	Glycosylation	393	1	N-linked (GlcNAc...) Potential
	Glycosylation	491	1	N-linked (GlcNAc...) Potential
	Disulfide bond	64 ↔ 77		By similarity
	Disulfide bond	252 ↔ 272		By similarity
	Disulfide bond	297 ↔ 316		By similarity
	Disulfide bond	308 ↔ 311		By similarity
	Disulfide bond	463 ↔ 483		By similarity
Experimental info
	Sequence conflict	28	1	E → Q in AAD30435. Ref.1
	Sequence conflict	424	1	Y → C in AAD30435. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9WVG5-1 [UniParc]. Last modified July 26, 2002. Version 2. Checksum: B153EF437ACAE6B2	FASTA	500	56,630
	10 20 30 40 50 60 MRNTVFLLGF WSVYCYFPAG SITTLRPEGS LRDEHHKPTG VPATARPSVA FNIRTSKDPE 70 80 90 100 110 120 QEGCNLSLGD SKLLENCGFN MTAKTFFIIH GWTMSGMFES WLHKLVSALQ MREKDANVVV 130 140 150 160 170 180 VDWLPLAHQL YTDAVNNTRV VGQRVAGMLD WLQEKEEFSL GNVHLIGYSL GAHVAGYAGN 190 200 210 220 230 240 FVKGTVGRIT GLDPAGPMFE GVDINRRLSP DDADFVDVLH TYTLSFGLSI GIRMPVGHID 250 260 270 280 290 300 IYPNGGDFQP GCGFNDVIGS FAYGTISEMV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS 310 320 330 340 350 360 SRFKRGICLS CRKNRCNNIG YNAKKMRKKR NSKMYLKTRA GMPFKVYHYQ LKVHMFSYNN 370 380 390 400 410 420 SGDTQPTLYI TLYGSNADSQ NLPLEIVEKI ELNATNTFLV YTEEDLGDLL KMRLTWEGVA 430 440 450 460 470 480 HSWYNLWNEF RNYLSQPSNP SRELYIRRIR VKSGETQRKV TFCTQDPTKS SISPGQELWF 490 500 HKCQDGWKMK NKTSPFVNLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a unique lipase from endothelial cells extends the lipase gene family." Hirata K., Dichek H.L., Cioffi J.A., Choi S.Y., Leeper N.J., Quintana L., Kronmal G.S., Cooper A.D., Quertermous T. J. Biol. Chem. 274:14170-14175(1999) [PubMed: 10318835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Endothelial cell.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF118768 mRNA. Translation: AAD30435.1. BC020991 mRNA. Translation: AAH20991.1.
IPI	IPI00323023.
UniGene	Mm.299647
3D structure databases
SMR	Q9WVG5. Positions 48-469.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9WVG5.
Proteomic databases
PRIDE	Q9WVG5.
Genome annotation databases
Ensembl	ENSMUST00000066532; ENSMUSP00000066536; ENSMUSG00000053846; Mus musculus. [Genome view]
UCSC	uc008fpu.1. mouse.
Organism-specific databases
MGI	MGI:1341803. Lipg.
Phylogenomic databases
HOGENOM	HBG445376.
HOVERGEN	Q9WVG5.
InParanoid	Q9WVG5.
Enzyme and pathway databases
BRENDA	3.1.1.3. 244.
Gene expression databases
ArrayExpress	Q9WVG5.
Bgee	Q9WVG5.
CleanEx	MM_LIPG.
Genevestigator	Q9WVG5.
GermOnline	ENSMUSG00000053846. Mus musculus.
Family and domain databases
InterPro	IPR000734. Lipase. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002330. Lipo_Lipase. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view]
PANTHER	PTHR11610. Lipase. 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]
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

LIPE_MOUSE

Accession

Primary (citable) accession number: Q9WVG5
Secondary accession number(s): Q8VDU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	July 26, 2002
Last modified:	January 19, 2010
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)