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.

P55031

- LIPL_FELCA

UniProt

P55031 - LIPL_FELCA

(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
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 4 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 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

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
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
ProteomesiUP000011712: 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

Pathology & Biotechi

Involvement in diseasei

Defects in LPL are a cause of chylomicronemia syndrome, also known as type I hyperlipoproteinemia. Animals exhibit reduced body mass, growth rates, and increased stillbirth rates.

Keywords - Diseasei

Disease mutation, Hyperlipidemia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed predictionAdd
BLAST
Chaini24 – 478455Lipoprotein lipasePRO_0000017774Add
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

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

STRINGi9685.ENSFCAP00000011284.

Structurei

3D structure databases

ProteinModelPortaliP55031.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
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.

P55031-1 [UniParc]FASTAAdd to Basket

« Hide

MESKTLFLMA LGIWLQSLTT TRGWVAADDR ITGGRDFIDI ESKFALRTPE    50
DIAEDTCHLI PGVTESVANC HFNHTSKTFV VIHGWTVTGM YESWVPKLVA 100
APYKREPDSN VIVVDWLSRA QQHYPVSAGY TKLVGKDVAK FINWMAEEFH 150
YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR 200
LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE 250
AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCNSKEAF 300
EKGLCLSCRK NRCNNLGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI 350
HFSGTESDTQ TNQVFEISLY GTVAESENIP FTLPEISANK TYSFLIYTEV 400
DIGELLMLKL KWKSDSYFSW SDWWSSPGFT IEKIRVKAGE TQKKVIFCSR 450
EKVSHLQKGK ASVVFVKCHD KSLNKKSG 478
Length:478
Mass (Da):53,668
Last modified:October 1, 1996 - v1
Checksum:iF57014446127E8C9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti435 – 4351R → G in chylomicronemia syndrome. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U42725 mRNA. Translation: AAB03848.1.
RefSeqiNP_001036032.1. NM_001042567.1.

Genome annotation databases

GeneIDi727696.
KEGGifca:727696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U42725 mRNA. Translation: AAB03848.1 .
RefSeqi NP_001036032.1. NM_001042567.1.

3D structure databases

ProteinModelPortali P55031.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9685.ENSFCAP00000011284.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 727696.
KEGGi fca:727696.

Organism-specific databases

CTDi 4023.

Phylogenomic databases

eggNOGi NOG40923.
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. "A mutation in the lipoprotein lipase gene is the molecular basis of chylomicronemia in a colony of domestic cats."
    Ginzinger D.G., Lewis M.E.S., Ma Y., Jones B.R., Liu G., Jones S.D.
    J. Clin. Invest. 97:1257-1266(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CHYLOMICRONEMIA SYNDROME GLY-435.

Entry informationi

Entry nameiLIPL_FELCA
AccessioniPrimary (citable) accession number: P55031
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 95 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