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Q29524

- LIPL_SHEEP

UniProt

Q29524 - LIPL_SHEEP

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Protein

Lipoprotein lipase

Gene

LPL

Organism
Ovis aries (Sheep)
Status
Reviewed - Annotation score: 5 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 – 1621Nucleophile
Active sitei186 – 1861Charge relay system
Active sitei271 – 2711Charge relay system

GO - Molecular functioni

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

GO - Biological processi

  1. positive regulation of cholesterol storage Source: Ensembl
  2. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
  3. positive regulation of sequestering of triglyceride Source: Ensembl
  4. triglyceride catabolic process Source: Ensembl
  5. triglyceride homeostasis Source: Ensembl
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
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356: Chromosome 2

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. cell surface Source: Ensembl
  3. chylomicron Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: Ensembl
  5. plasma membrane Source: UniProtKB-KW
  6. 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 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 478451Lipoprotein lipasePRO_0000017781Add
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

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

ProteinModelPortaliQ29524.
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

GeneTreeiENSGT00760000119069.
HOVERGENiHBG002259.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[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.

Q29524-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESKVLLLLA LSVWLQSLTV SRGGLVAADR ITRGKDFRDI ESKFALRTPE
60 70 80 90 100
DTAEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA
110 120 130 140 150
ALYKREPDSN VIVVDWLSRA QQHYPVSAGY TKLVGQDVAK FMNWMADEFN
160 170 180 190 200
YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR
210 220 230 240 250
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE
260 270 280 290 300
ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF
310 320 330 340 350
EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI
360 370 380 390 400
HFSGTESNTY TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV
410 420 430 440 450
DIGELLMLKL KWISDSYFSW SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR
460 470
EKMSYLQKGK SPVIFVKCHD KSLNRKSG
Length:478
Mass (Da):53,588
Last modified:November 1, 1997 - v1
Checksum:i10F41EE1FFB9C882
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68308 mRNA. Translation: CAA48384.1.
PIRiS29846.
RefSeqiNP_001009394.1. NM_001009394.1.
UniGeneiOar.459.

Genome annotation databases

EnsembliENSOART00000011666; ENSOARP00000011504; ENSOARG00000010719.
GeneIDi443408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68308 mRNA. Translation: CAA48384.1 .
PIRi S29846.
RefSeqi NP_001009394.1. NM_001009394.1.
UniGenei Oar.459.

3D structure databases

ProteinModelPortali Q29524.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSOART00000011666 ; ENSOARP00000011504 ; ENSOARG00000010719 .
GeneIDi 443408.

Organism-specific databases

CTDi 4023.

Phylogenomic databases

GeneTreei ENSGT00760000119069.
HOVERGENi HBG002259.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsi TIGR03230. lipo_lipase. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequencing of a full length cDNA encoding ovine lipoprotein lipase."
    Edwards W.D., Daniels S.W., Page R.A., Volpe C.P., Kille P., Sweeney G.E., Cryer A.
    Biochim. Biophys. Acta 1172:167-170(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Welsh Mountain/Dorset.
    Tissue: Adipose tissue.

Entry informationi

Entry nameiLIPL_SHEEP
AccessioniPrimary (citable) accession number: Q29524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 97 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