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P11153

- LIPL_CAVPO

UniProt

P11153 - LIPL_CAVPO

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Protein
Lipoprotein lipase
Gene
LPL
Organism
Cavia porcellus (Guinea 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 sitei149 – 1491Nucleophile By similarity
Active sitei173 – 1731Charge relay system By similarity
Active sitei258 – 2581Charge relay system By similarity

GO - Molecular functioni

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

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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447: 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 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 465448Lipoprotein lipase
PRO_0000017773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 57 By similarity
Glycosylationi60 – 601N-linked (GlcNAc...) Reviewed prediction
Modified residuei111 – 1111Nitrated tyrosine By similarity
Modified residuei181 – 1811Nitrated tyrosine By similarity
Disulfide bondi233 ↔ 256 By similarity
Disulfide bondi281 ↔ 300 By similarity
Disulfide bondi292 ↔ 295 By similarity
Modified residuei333 – 3331Nitrated tyrosine By similarity
Glycosylationi376 – 3761N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi435 ↔ 455 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

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. Interacts with GPIHBP1 By similarity.

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000003655.

Structurei

3D structure databases

ProteinModelPortaliP11153.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini331 – 454124PLAT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni336 – 43196Heparin-binding By similarity
Add
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP11153.

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.

P11153-1 [UniParc]FASTAAdd to Basket

« Hide

MNIDRKILNK ALAKEKVANC QKDYTDIESK FARRTPENTV EDTCHLIPGV    50
TESVANCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV 100
VDWLRRAQHH YPESADYTKL VGEDVARFIN WMEDEFKYSV DNVHLLGYSL 150
GAHAAGVAGS RTNTKVSRIT GLDPAGPNFE YAEATSRLSP DDAQFVDVLH 200
TFTRGSPGRS IGIQKPVGHV DIYPNGGSFQ PGCNIQDALR VISQKGFGDM 250
DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC 300
NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIYFS GTETTTYTNQ 350
AFEISLYGTV AESENIPFTL PEVSANNTYS FLIYTEVDIG ELLMLKLKWI 400
TESYFSWSSW WGRPTFTIEK IRVKAGETQK KIVFCSREKV SKLQKGKEAP 450
VFVKCHDKSL NKKSG 465
Length:465
Mass (Da):52,781
Last modified:July 1, 1989 - v1
Checksum:iE2515F36BEFD5F10
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15483 mRNA. Translation: AAA37046.1 .
M33381
, M33377 , M33378 , M33379 , M33380 Genomic DNA. Translation: AAA37039.1 .
PIRi JS0398. A27330.
RefSeqi NP_001166449.1. NM_001172978.1.

3D structure databases

ProteinModelPortali P11153.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10141.ENSCPOP00000003655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100135570.

Organism-specific databases

CTDi 4023.

Phylogenomic databases

eggNOGi NOG40923.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi P11153.

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. "Molecular cloning and sequence analysis of cDNA encoding lipoprotein lipase of guinea pig."
    Enerbaeck S., Semb H., Bengtsson-Olivecrona G., Carlsson P., Hermansson M.-L., Olivecrona T., Bjursell G.
    Gene 58:1-12(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Genomic organization of the region encoding guinea pig lipoprotein lipase; evidence for exon fusion and unconventional splicing."
    Enerbaeck S., Bjursell G.
    Gene 84:391-397(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiLIPL_CAVPO
AccessioniPrimary (citable) accession number: P11153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 110 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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