SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q06000

- LIPL_RAT

UniProt

Q06000 - LIPL_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Lipoprotein lipase
Gene
Lpl
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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 sitei159 – 1591Nucleophile By similarity
Active sitei183 – 1831Charge relay system By similarity
Active sitei268 – 2681Charge relay system By similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. lipoprotein lipase activity Source: RGD
  3. triglyceride binding Source: RGD

GO - Biological processi

  1. lipid catabolic process Source: RGD
  2. positive regulation of cholesterol storage Source: Ensembl
  3. positive regulation of macrophage derived foam cell differentiation Source: Ensembl
  4. positive regulation of sequestering of triglyceride Source: Ensembl
  5. response to cold Source: RGD
  6. response to drug Source: RGD
  7. triglyceride biosynthetic process Source: RGD
  8. triglyceride catabolic process Source: Ensembl
  9. triglyceride homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BRENDAi3.1.1.34. 5301.
ReactomeiREACT_199015. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34)
Short name:
LPL
Gene namesi
Name:Lpl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi3017. Lpl.

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. cell surface Source: Ensembl
  3. chylomicron Source: UniProtKB-KW
  4. extracellular matrix Source: RGD
  5. plasma membrane Source: UniProtKB-SubCell
  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 – 2727 By similarity
Add
BLAST
Chaini28 – 474447Lipoprotein lipase
PRO_0000017779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67 By similarity
Glycosylationi70 – 701N-linked (GlcNAc...) Reviewed prediction
Modified residuei121 – 1211Nitrated tyrosine1 Publication
Modified residuei191 – 1911Nitrated tyrosine1 Publication
Disulfide bondi243 ↔ 266 By similarity
Disulfide bondi291 ↔ 310 By similarity
Disulfide bondi302 ↔ 305 By similarity
Modified residuei343 – 3431Nitrated tyrosine1 Publication
Glycosylationi386 – 3861N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi445 ↔ 465 By similarity

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

PaxDbiQ06000.
PRIDEiQ06000.

Expressioni

Inductioni

Induced by insulin. Inhibited by isoproterenol.1 Publication

Gene expression databases

GenevestigatoriQ06000.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016543.

Structurei

3D structure databases

ProteinModelPortaliQ06000.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 464124PLAT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni346 – 44196Heparin-binding By similarity
Add
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00750000117234.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ06000.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG757CX5.
PhylomeDBiQ06000.
TreeFamiTF324997.

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.

Q06000-1 [UniParc]FASTAAdd to Basket

« Hide

MESKALLLVA LGVWLQSLTA FRGGVAAADG GRDFSDIESK FALRTPEDTA    50
EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY 100
KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WLEEEFNYPL 150
DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP 200
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR 250
VIAEKGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 300
LCLSCRKNRC NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS 350
GTENDKQNNQ AFEISLYGTV AESENIPFTL PEVATNKTYS FLIYTEVDIG 400
ELLMMKLKWK NDSYFRWSDW WSSPSFVIEK IRVKAGETQK KVIFCAREKV 450
SHLQKGKDAA VFVKCHDKSL KKSG 474
Length:474
Mass (Da):53,082
Last modified:February 1, 1994 - v1
Checksum:iF4F6F4BCCA4F1626
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361M → V no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L03294 mRNA. Translation: AAA41534.1.
BC081836 mRNA. Translation: AAH81836.1.
PIRiJH0790.
RefSeqiNP_036730.1. NM_012598.2.
UniGeneiRn.3834.

Genome annotation databases

EnsembliENSRNOT00000016543; ENSRNOP00000016543; ENSRNOG00000012181.
GeneIDi24539.
KEGGirno:24539.
UCSCiRGD:3017. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L03294 mRNA. Translation: AAA41534.1 .
BC081836 mRNA. Translation: AAH81836.1 .
PIRi JH0790.
RefSeqi NP_036730.1. NM_012598.2.
UniGenei Rn.3834.

3D structure databases

ProteinModelPortali Q06000.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000016543.

Chemistry

BindingDBi Q06000.
ChEMBLi CHEMBL5906.

Proteomic databases

PaxDbi Q06000.
PRIDEi Q06000.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000016543 ; ENSRNOP00000016543 ; ENSRNOG00000012181 .
GeneIDi 24539.
KEGGi rno:24539.
UCSCi RGD:3017. rat.

Organism-specific databases

CTDi 4023.
RGDi 3017. Lpl.

Phylogenomic databases

eggNOGi NOG40923.
GeneTreei ENSGT00750000117234.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi Q06000.
KOi K01059.
OMAi ESVANCH.
OrthoDBi EOG757CX5.
PhylomeDBi Q06000.
TreeFami TF324997.

Enzyme and pathway databases

BRENDAi 3.1.1.34. 5301.
Reactomei REACT_199015. Retinoid metabolism and transport.

Miscellaneous databases

NextBioi 603620.
PROi Q06000.

Gene expression databases

Genevestigatori Q06000.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Lipoprotein lipase gene expression in rat adipocytes is regulated by isoproterenol and insulin through different mechanisms."
    Raynolds M.V., Awald P.D., Gordon D.F., Gutierrez-Hartmann A., Rule D.C., Wood W.M., Eckel R.H.
    Mol. Endocrinol. 4:1416-1422(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 336-474, INDUCTION.
    Tissue: Heart.
  4. "Lipoprotein lipase is nitrated in vivo after lipopolysaccharide challenge."
    Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
    Free Radic. Biol. Med. 47:1553-1560(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION AT TYR-121; TYR-191 AND TYR-343, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Discovery of lipoprotein lipase pI isoforms and contributions to their characterization."
    Casanovas A., Carrascal M., Abian J., Lopez-Tejero M.D., Llobera M.
    J. Proteomics 72:1031-1039(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.

Entry informationi

Entry nameiLIPL_RAT
AccessioniPrimary (citable) accession number: Q06000
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 123 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