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Protein

Lipoprotein lipase

Gene

LPL

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei162NucleophileBy similarity1
Active sitei186Charge relay systemPROSITE-ProRule annotation1
Active sitei271Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Protein family/group databases

ESTHERisussc-lipli Lipoprotein_Lipase

Names & Taxonomyi

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

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
ChainiPRO_000001778028 – 478Lipoprotein lipaseAdd BLAST451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi57 ↔ 70PROSITE-ProRule annotation
Glycosylationi73N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei124Nitrated tyrosineBy similarity1
Modified residuei194Nitrated tyrosineBy similarity1
Disulfide bondi246 ↔ 269PROSITE-ProRule annotation
Disulfide bondi294 ↔ 313PROSITE-ProRule annotation
Disulfide bondi305 ↔ 308PROSITE-ProRule annotation
Modified residuei346Nitrated tyrosineBy similarity1
Glycosylationi389N-linked (GlcNAc...) asparagineSequence analysis1
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

PeptideAtlasiP49923
PRIDEiP49923

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1. Interacts with LMF1 and SEL1L (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP49923
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini344 – 467PLATPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni349 – 444Heparin-bindingBy similarityAdd BLAST96

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000038553
HOVERGENiHBG002259
InParanoidiP49923
KOiK01059

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013818 Lipase/vitellogenin
IPR016272 Lipase_LIPH
IPR033906 Lipase_N
IPR002330 Lipo_Lipase
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
IPR000734 TAG_lipase
PANTHERiPTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00822 LIPOLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR03230 lipo_lipase, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiLIPL_PIG
AccessioniPrimary (citable) accession number: P49923
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 113 of the entry and version 1 of the sequence. See 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

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