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P49923

- LIPL_PIG

UniProt

P49923 - LIPL_PIG

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Protein
Lipoprotein lipase
Gene
LPL
Organism
Sus scrofa (Pig)
Status
Reviewed - 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.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Nucleophile By similarity
Active sitei186 – 1861Charge relay system By similarity
Active sitei271 – 2711Charge relay system By similarity

GO - Molecular functioni

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

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.

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 – 2727 By similarity
Add
BLAST
Chaini28 – 478451Lipoprotein lipase
PRO_0000017780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 70 By similarity
Glycosylationi73 – 731N-linked (GlcNAc...) Reviewed prediction
Modified residuei124 – 1241Nitrated tyrosine By similarity
Modified residuei194 – 1941Nitrated tyrosine By similarity
Disulfide bondi246 ↔ 269 By similarity
Disulfide bondi294 ↔ 313 By similarity
Disulfide bondi305 ↔ 308 By similarity
Modified residuei346 – 3461Nitrated tyrosine By similarity
Glycosylationi389 – 3891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi448 ↔ 468 By similarity

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.

Structurei

3D structure databases

ProteinModelPortaliP49923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini344 – 467124PLAT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni349 – 44496Heparin-binding By similarity
Add
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
KOiK01059.

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.

P49923-1 [UniParc]FASTAAdd to Basket

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MESKALLLVA LSVWLQSLIV SREGLATADR ISGGRDFTDI ESKFALRTPE    50
DTVEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA 100
ALYKREPDSN VIVVDWLSRA QQHYPISAGY TKLVGQDVAT FIDWMAVEFS 150
YPPNNVHLLG YSLGAHAAGI AGSLTKKKVN RITGLDPAGP NFEYAEAPSR 200
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE 250
AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCNSKEAF 300
EKGLCLSCRK NRCNNLGYEI NKVRAKRSSK MYLKTRAQMP YKVFHYQVKM 350
RFSGTESDTH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV 400
DIGELLMLKL KWVSDSYFSW SNWWSSPGFA IEKIRVKAGE TQKKVIFCSR 450
EKKSHLQKGK SSVVFVKCHD KSLNRKSG 478
Length:478
Mass (Da):53,455
Last modified:October 1, 1996 - v1
Checksum:iD0500324117261E3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X62984 mRNA. Translation: CAA44725.1 .
PIRi I47146. S18158.
RefSeqi NP_999451.1. NM_214286.1.
UniGenei Ssc.95883.

3D structure databases

ProteinModelPortali P49923.
ModBasei Search...

Proteomic databases

PaxDbi P49923.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397537.
KEGGi ssc:397537.

Organism-specific databases

CTDi 4023.

Phylogenomic databases

eggNOGi NOG40923.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
KOi K01059.

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. "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: June 11, 2014
This is version 96 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

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