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P49060

- LIPL_PAPAN

UniProt

P49060 - LIPL_PAPAN

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Protein

Lipoprotein lipase

Gene

LPL

Organism
Papio anubis (Olive baboon)
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 sitei159 – 1591Nucleophile
Active sitei183 – 1831Charge relay system
Active sitei268 – 2681Charge relay system

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
OrganismiPapio anubis (Olive baboon)
Taxonomic identifieri9555 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaePapio

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 – 2727By similarityAdd
BLAST
Chaini28 – 475448Lipoprotein lipasePRO_0000017778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Modified residuei121 – 1211Nitrated tyrosineBy similarity
Modified residuei191 – 1911Nitrated tyrosineBy similarity
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343 – 3431Nitrated tyrosineBy similarity
Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi445 ↔ 465PROSITE-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

Highest levels in the spinal cord.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

Structurei

3D structure databases

ProteinModelPortaliP49060.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 464124PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni346 – 44196Heparin-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

HOVERGENiHBG002259.

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.

P49060-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESKALLLLA LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGV AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLSRAQQH YPVSAGYTKL VGQDVARFIN WMEEEFNYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CSSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTESETHTNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMLKLKWK SDSYFSWSDW WSSPGFAIQK IRVKAGETQK KVIFCSREKV
460 470
SHLQKGKAPA VFVKCHDKSL NKKSG
Length:475
Mass (Da):53,146
Last modified:February 1, 1996 - v1
Checksum:i6E4602679C750C91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18091 mRNA. Translation: AAC50199.1.
RefSeqiNP_001106082.1. NM_001112612.1.
UniGeneiPan.6840.

Genome annotation databases

GeneIDi100126663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18091 mRNA. Translation: AAC50199.1 .
RefSeqi NP_001106082.1. NM_001112612.1.
UniGenei Pan.6840.

3D structure databases

ProteinModelPortali P49060.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100126663.

Organism-specific databases

CTDi 4023.

Phylogenomic databases

HOVERGENi HBG002259.

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. "Baboon lipoprotein lipase: cDNA sequence and variable tissue-specific expression of two transcripts."
    Cole S.A., Hixson J.E.
    Gene 161:265-269(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Heart muscle.

Entry informationi

Entry nameiLIPL_PAPAN
AccessioniPrimary (citable) accession number: P49060
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3