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Protein

Lipoprotein lipase

Gene

LPL

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621NucleophileBy similarity
Active sitei186 – 1861Charge relay systemPROSITE-ProRule annotation
Active sitei271 – 2711Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. lipoprotein lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34)
Short name:
LPL
Gene namesi
Name:LPL
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Cell membrane By similarity; Lipid-anchorGPI-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).By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. chylomicron Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
  4. very-low-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 478451Lipoprotein lipasePRO_0000017780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 70PROSITE-ProRule annotation
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
Modified residuei124 – 1241Nitrated tyrosineBy similarity
Modified residuei194 – 1941Nitrated tyrosineBy similarity
Disulfide bondi246 ↔ 269PROSITE-ProRule annotation
Disulfide bondi294 ↔ 313PROSITE-ProRule annotation
Disulfide bondi305 ↔ 308PROSITE-ProRule annotation
Modified residuei346 – 3461Nitrated tyrosineBy similarity
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi448 ↔ 468PROSITE-ProRule annotation

Post-translational modificationi

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Nitration

Proteomic databases

PaxDbiP49923.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interacts with GPIHBP1 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP49923.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini344 – 467124PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni349 – 44496Heparin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP49923.
KOiK01059.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR03230. lipo_lipase. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKALLLVA LSVWLQSLIV SREGLATADR ISGGRDFTDI ESKFALRTPE
60 70 80 90 100
DTVEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA
110 120 130 140 150
ALYKREPDSN VIVVDWLSRA QQHYPISAGY TKLVGQDVAT FIDWMAVEFS
160 170 180 190 200
YPPNNVHLLG YSLGAHAAGI AGSLTKKKVN RITGLDPAGP NFEYAEAPSR
210 220 230 240 250
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE
260 270 280 290 300
AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCNSKEAF
310 320 330 340 350
EKGLCLSCRK NRCNNLGYEI NKVRAKRSSK MYLKTRAQMP YKVFHYQVKM
360 370 380 390 400
RFSGTESDTH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV
410 420 430 440 450
DIGELLMLKL KWVSDSYFSW SNWWSSPGFA IEKIRVKAGE TQKKVIFCSR
460 470
EKKSHLQKGK SSVVFVKCHD KSLNRKSG
Length:478
Mass (Da):53,455
Last modified:October 1, 1996 - v1
Checksum:iD0500324117261E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62984 mRNA. Translation: CAA44725.1.
PIRiI47146. S18158.
RefSeqiNP_999451.1. NM_214286.1.
UniGeneiSsc.95883.

Genome annotation databases

GeneIDi397537.
KEGGissc:397537.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62984 mRNA. Translation: CAA44725.1.
PIRiI47146. S18158.
RefSeqiNP_999451.1. NM_214286.1.
UniGeneiSsc.95883.

3D structure databases

ProteinModelPortaliP49923.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP49923.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397537.
KEGGissc:397537.

Organism-specific databases

CTDi4023.

Phylogenomic databases

eggNOGiNOG40923.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP49923.
KOiK01059.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR03230. lipo_lipase. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and sequencing of porcine lipoprotein lipase cDNA and its use in multiallelic restriction fragment length polymorphism detection."
    Harbitz I., Kristensen T., Kran S., Davies W.
    Anim. Genet. 23:517-522(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Norwegian Landrace.
    Tissue: Skeletal muscle.

Entry informationi

Entry nameiLIPL_PIG
AccessioniPrimary (citable) accession number: P49923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 4, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.