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Protein

Lipoprotein lipase

Gene

LPL

Organism
Cavia porcellus (Guinea 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 sitei149NucleophileBy similarity1
Active sitei173Charge relay systemPROSITE-ProRule annotation1
Active sitei258Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Protein family/group databases

ESTHERicavpo-lipli Lipoprotein_Lipase

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34By similarity)
Short name:
LPL
Gene namesi
Name:LPL
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricomorphaCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

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 – 17Sequence analysisAdd BLAST17
ChainiPRO_000001777318 – 465Lipoprotein lipaseAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 57PROSITE-ProRule annotation
Glycosylationi60N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei111Nitrated tyrosineBy similarity1
Modified residuei181Nitrated tyrosineBy similarity1
Disulfide bondi233 ↔ 256PROSITE-ProRule annotation
Disulfide bondi281 ↔ 300PROSITE-ProRule annotation
Disulfide bondi292 ↔ 295PROSITE-ProRule annotation
Modified residuei333Nitrated tyrosineBy similarity1
Glycosylationi376N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 455PROSITE-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

Expressioni

Tissue specificityi

High level of expression in expression in adipocytes, heart muscle and mammary gland.1 Publication

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

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000003655

Structurei

3D structure databases

ProteinModelPortaliP11153
SMRiP11153
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini331 – 454PLATPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni336 – 431Heparin-bindingBy similarityAdd BLAST96

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJUA Eukaryota
ENOG4111GMM LUCA
HOGENOMiHOG000038553
HOVERGENiHBG002259
InParanoidiP11153

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.

P11153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIDRKILNK ALAKEKVANC QKDYTDIESK FARRTPENTV EDTCHLIPGV
60 70 80 90 100
TESVANCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV
110 120 130 140 150
VDWLRRAQHH YPESADYTKL VGEDVARFIN WMEDEFKYSV DNVHLLGYSL
160 170 180 190 200
GAHAAGVAGS RTNTKVSRIT GLDPAGPNFE YAEATSRLSP DDAQFVDVLH
210 220 230 240 250
TFTRGSPGRS IGIQKPVGHV DIYPNGGSFQ PGCNIQDALR VISQKGFGDM
260 270 280 290 300
DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC
310 320 330 340 350
NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIYFS GTETTTYTNQ
360 370 380 390 400
AFEISLYGTV AESENIPFTL PEVSANNTYS FLIYTEVDIG ELLMLKLKWI
410 420 430 440 450
TESYFSWSSW WGRPTFTIEK IRVKAGETQK KIVFCSREKV SKLQKGKEAP
460
VFVKCHDKSL NKKSG
Length:465
Mass (Da):52,781
Last modified:July 1, 1989 - v1
Checksum:iE2515F36BEFD5F10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15483 mRNA Translation: AAA37046.1
M33381
, M33377, M33378, M33379, M33380 Genomic DNA Translation: AAA37039.1
PIRiJS0398 A27330
RefSeqiNP_001166449.1, NM_001172978.1

Genome annotation databases

GeneIDi100135570

Similar proteinsi

Entry informationi

Entry nameiLIPL_CAVPO
AccessioniPrimary (citable) accession number: P11153
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 28, 2018
This is version 125 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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