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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).By similarity

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei149 – 1491NucleophileBy similarity
Active sitei173 – 1731Charge relay systemPROSITE-ProRule annotation
Active sitei258 – 2581Charge relay systemPROSITE-ProRule annotation

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).By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. chylomicron Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
  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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 465448Lipoprotein lipasePRO_0000017773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 57PROSITE-ProRule annotation
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Modified residuei111 – 1111Nitrated tyrosineBy similarity
Modified residuei181 – 1811Nitrated tyrosineBy similarity
Disulfide bondi233 ↔ 256PROSITE-ProRule annotation
Disulfide bondi281 ↔ 300PROSITE-ProRule annotation
Disulfide bondi292 ↔ 295PROSITE-ProRule annotation
Modified residuei333 – 3331Nitrated tyrosineBy similarity
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
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. Interacts with GPIHBP1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000003655.

Structurei

3D structure databases

ProteinModelPortaliP11153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini331 – 454124PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni336 – 43196Heparin-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

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

        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.

Cross-referencesi

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 .
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: October 29, 2014
This is version 112 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