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UniProtKB - P06858 (LIPL_HUMAN)

UniProt

P06858 - LIPL_HUMAN

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Protein

Lipoprotein lipase

Gene

LPL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).By similarity1 Publication

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591Nucleophile
Active sitei183 – 1831Charge relay system
Active sitei268 – 2681Charge relay system

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • heparin binding Source: UniProtKB
  • lipoprotein lipase activity Source: UniProtKB
  • phospholipase activity Source: BHF-UCL
  • receptor binding Source: BHF-UCL
  • triglyceride binding Source: Ensembl
  • triglyceride lipase activity Source: BHF-UCL

GO - Biological processi

  • cholesterol homeostasis Source: BHF-UCL
  • chylomicron remodeling Source: BHF-UCL
  • fatty acid biosynthetic process Source: BHF-UCL
  • lipoprotein metabolic process Source: Reactome
  • phospholipid metabolic process Source: BHF-UCL
  • positive regulation of chemokine secretion Source: BHF-UCL
  • positive regulation of cholesterol storage Source: BHF-UCL
  • positive regulation of inflammatory response Source: BHF-UCL
  • positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • positive regulation of sequestering of triglyceride Source: BHF-UCL
  • response to cold Source: Ensembl
  • response to drug Source: Ensembl
  • response to glucose Source: AgBase
  • retinoid metabolic process Source: Reactome
  • triglyceride biosynthetic process Source: Ensembl
  • triglyceride catabolic process Source: UniProtKB
  • triglyceride homeostasis Source: BHF-UCL
  • triglyceride metabolic process Source: BHF-UCL
  • very-low-density lipoprotein particle remodeling Source: BHF-UCL
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. 2681.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-975634. Retinoid metabolism and transport.

Protein family/group databases

ESTHERihuman-LPL. Lipoprotein_Lipase.

Chemistry

SwissLipidsiSLP:000000568.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.341 Publication)
Short name:
LPL
Gene namesi
Name:LPL
Synonyms:LIPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:6677. LPL.

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchor › GPI-anchor By similarity
  • Secreted 1 Publication

    • 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

Pathology & Biotechi

Involvement in diseasei

Lipoprotein lipase deficiency (LPL deficiency)54 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRecessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.
See also OMIM:238600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 Publications
Corresponds to variant rs1801177 [ dbSNP | Ensembl ].		VAR_011948
Natural varianti70 – 701N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications
VAR_057914
Natural varianti96 – 961V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 Publication
Corresponds to variant rs373088068 [ dbSNP | Ensembl ].		VAR_057915
Natural varianti98 – 981A → T in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs145657341 [ dbSNP | Ensembl ].		VAR_057916
Natural varianti102 – 1021R → S in LPL deficiency. 1 Publication
Corresponds to variant rs118204073 [ dbSNP | Ensembl ].		VAR_004211
Natural varianti113 – 1131W → G in LPL deficiency.
VAR_004212
Natural varianti113 – 1131W → R in LPL deficiency. 2 Publications
Corresponds to variant rs118204069 [ dbSNP | Ensembl ].		VAR_004213
Natural varianti128 – 1281T → A in LPL deficiency. 2 Publications
VAR_057917
Natural varianti132 – 1321G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057918
Natural varianti163 – 1631H → R in LPL deficiency. 1 Publication
VAR_004214
Natural varianti169 – 1691G → E in LPL deficiency; loss of activity. 1 Publication
Corresponds to variant rs118204063 [ dbSNP | Ensembl ].		VAR_004215
Natural varianti181 – 1811G → S in LPL deficiency. 1 Publication
VAR_004216
Natural varianti181 – 1811G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057919
Natural varianti183 – 1831D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 Publications
Corresponds to variant rs118204064 [ dbSNP | Ensembl ].		VAR_004217
Natural varianti183 – 1831D → H in LPL deficiency. 1 Publication
Corresponds to variant rs781614031 [ dbSNP | Ensembl ].		VAR_057920
Natural varianti183 – 1831D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 Publications
VAR_004218
Natural varianti184 – 1841P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication
VAR_004219
Natural varianti185 – 1851A → T in LPL deficiency; 3.2% of activity.
Corresponds to variant rs748349562 [ dbSNP | Ensembl ].		VAR_004220
Natural varianti186 – 1861G → E in LPL deficiency. 1 Publication
VAR_057921
Natural varianti190 – 1901E → G in LPL deficiency. 1 Publication
VAR_057922
Natural varianti199 – 1991S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 Publications
Corresponds to variant rs118204072 [ dbSNP | Ensembl ].		VAR_004221
Natural varianti201 – 2011D → V in LPL deficiency. 1 Publication
VAR_057923
Natural varianti203 – 2031A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 Publication
Corresponds to variant rs118204056 [ dbSNP | Ensembl ].		VAR_004222
Natural varianti207 – 2071D → E in LPL deficiency. 1 Publication
Corresponds to variant rs118204076 [ dbSNP | Ensembl ].		VAR_004223
Natural varianti208 – 2081V → I in LPL deficiency; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057924
Natural varianti210 – 2101H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication
VAR_057925
Natural varianti210 – 2101H → Q in LPL deficiency; loss of activity.
VAR_004224
Natural varianti215 – 2151G → E in LPL deficiency; loss of activity. 12 Publications
Corresponds to variant rs118204057 [ dbSNP | Ensembl ].		VAR_004225
Natural varianti215 – 2151G → R in LPL deficiency. 2 Publications
VAR_057926
Natural varianti220 – 2201S → R in LPL deficiency; 2.0% of activity.
Corresponds to variant rs757546424 [ dbSNP | Ensembl ].		VAR_004226
Natural varianti221 – 2211I → T in LPL deficiency; loss of activity. 5 Publications
Corresponds to variant rs118204061 [ dbSNP | Ensembl ].		VAR_004227
Natural varianti222 – 2221G → E in LPL deficiency. 1 Publication
Corresponds to variant rs118204075 [ dbSNP | Ensembl ].		VAR_004228
Natural varianti225 – 2251K → R in LPL deficiency. 1 Publication
VAR_057927
Natural varianti227 – 2271V → A in LPL deficiency. 1 Publication
Corresponds to variant rs528243561 [ dbSNP | Ensembl ].		VAR_057928
Natural varianti231 – 2311D → E in LPL deficiency; loss of activity. 3 Publications
Corresponds to variant rs118204067 [ dbSNP | Ensembl ].		VAR_004229
Natural varianti232 – 2321I → S in LPL deficiency. 1 Publication
Corresponds to variant rs770601263 [ dbSNP | Ensembl ].		VAR_004230
Natural varianti234 – 2341P → L in LPL deficiency; loss of activity. 2 Publications
Corresponds to variant rs118204060 [ dbSNP | Ensembl ].		VAR_004231
Natural varianti243 – 2431C → S in LPL deficiency; loss of activity. 1 Publication
VAR_004232
Natural varianti252 – 2521I → T in LPL deficiency. 1 Publication
Corresponds to variant rs118204080 [ dbSNP | Ensembl ].		VAR_057929
Natural varianti266 – 2661C → W in LPL deficiency. 1 Publication
Corresponds to variant rs118204082 [ dbSNP | Ensembl ].		VAR_057930
Natural varianti270 – 2701R → C in LPL deficiency. 4 Publications
Corresponds to variant rs118204077 [ dbSNP | Ensembl ].		VAR_057931
Natural varianti270 – 2701R → H in LPL deficiency; loss of activity. 6 Publications
Corresponds to variant rs118204062 [ dbSNP | Ensembl ].		VAR_004233
Natural varianti271 – 2711S → T in LPL deficiency. 1 Publication
Corresponds to variant rs28934893 [ dbSNP | Ensembl ].		VAR_004234
Natural varianti277 – 2771D → N in LPL deficiency; 5% of full activity. 5 Publications
Corresponds to variant rs118204068 [ dbSNP | Ensembl ].		VAR_004235
Natural varianti278 – 2781S → C in LPL deficiency.
VAR_004236
Natural varianti279 – 2791L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 Publications
Corresponds to variant rs35414700 [ dbSNP | Ensembl ].		VAR_057932
Natural varianti279 – 2791L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs371282890 [ dbSNP | Ensembl ].		VAR_057933
Natural varianti286 – 2861S → G in LPL deficiency. 1 Publication
VAR_004237
Natural varianti286 – 2861S → R in LPL deficiency. 1 Publication
VAR_004238
Natural varianti288 – 2881A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 Publications
Corresponds to variant rs1800011 [ dbSNP | Ensembl ].		VAR_011949
Natural varianti289 – 2891Y → H in LPL deficiency; no enzyme activity. 1 Publication
VAR_057934
Natural varianti297 – 2971F → L in LPL deficiency and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. 2 Publications
VAR_057935
Natural varianti303 – 3031L → F in LPL deficiency; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. 1 Publication
VAR_057936
Natural varianti305 – 3051C → R in LPL deficiency. 1 Publication
Corresponds to variant rs773235712 [ dbSNP | Ensembl ].		VAR_057937
Natural varianti310 – 3101C → Y in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057938
Natural varianti313 – 3131L → P in LPL deficiency. 1 Publication
VAR_057939
Natural varianti318 – 3181N → S in LPL deficiency; loss of activity; frequent mutation. 8 Publications
Corresponds to variant rs268 [ dbSNP | Ensembl ].		VAR_004239
Natural varianti325 – 3251S → R in LPL deficiency; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs761265900 [ dbSNP | Ensembl ].		VAR_057940
Natural varianti328 – 3281M → R in LPL deficiency. 1 Publication
VAR_057941
Natural varianti328 – 3281M → T in LPL deficiency.
VAR_004240
Natural varianti330 – 3301L → F in LPL deficiency. 1 Publication
VAR_057942
Natural varianti330 – 3301L → P in LPL deficiency.
VAR_004241
Natural varianti361 – 3611A → T in LPL deficiency. 2 Publications
Corresponds to variant rs118204071 [ dbSNP | Ensembl ].		VAR_004242
Natural varianti365 – 3651S → F in LPL deficiency; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs546542623 [ dbSNP | Ensembl ].		VAR_057943
Natural varianti392 – 3921L → V in LPL deficiency; loss of activity. 1 Publication
Corresponds to variant rs118204078 [ dbSNP | Ensembl ].		VAR_004243
Natural varianti423 – 4242Missing in LPL deficiency; affects the protein folding.
VAR_004244
Natural varianti437 – 4371E → K in LPL deficiency. 1 Publication
VAR_004245
Natural varianti437 – 4371E → V in LPL deficiency. 1 Publication
VAR_004246
Natural varianti445 – 4451C → Y in LPL deficiency; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities. 1 Publication
Corresponds to variant rs118204079 [ dbSNP | Ensembl ].		VAR_057944
Natural varianti448 – 4481E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 Publication
Corresponds to variant rs149089920 [ dbSNP | Ensembl ].		VAR_057945

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591S → G: Lacks both triolein and tributyrin esterase activities. 1 Publication
Mutagenesisi159 – 1591S → T: Lacks both triolein and tributyrin esterase activities. 1 Publication
Mutagenesisi268 – 2681H → G: Lacks both triolein and tributyrin esterase activities. 1 Publication
Mutagenesisi268 – 2681H → Q: Lacks both triolein and tributyrin esterase activities. 1 Publication

Keywords - Diseasei

Disease mutation, Hyperlipidemia

Organism-specific databases

MalaCardsiLPL.
MIMi238600. phenotype.
Orphaneti309015. Familial lipoprotein lipase deficiency.
70470. Hyperlipoproteinemia type 5.
PharmGKBiPA232.

Chemistry

ChEMBLiCHEMBL2060.
DrugBankiDB05269. AST-120.
DB06439. Tyloxapol.

Polymorphism and mutation databases

BioMutaiLPL.
DMDMi126314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 475448Lipoprotein lipasePRO_0000017775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
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

Proteomic databases

EPDiP06858.
MaxQBiP06858.
PaxDbiP06858.
PeptideAtlasiP06858.
PRIDEiP06858.

PTM databases

iPTMnetiP06858.
PhosphoSiteiP06858.

Expressioni

Gene expression databases

BgeeiENSG00000175445.
CleanExiHS_LPL.
ExpressionAtlasiP06858. baseline and differential.
GenevisibleiP06858. HS.

Organism-specific databases

HPAiHPA048749.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1 (PubMed:17997385). Interacts with SEL1L and LMF1 (PubMed:25066055).By similarity2 Publications

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110205. 18 interactions.
IntActiP06858. 14 interactions.
MINTiMINT-1369348.
STRINGi9606.ENSP00000309757.

Chemistry

BindingDBiP06858.

Structurei

3D structure databases

ProteinModelPortaliP06858.
SMRiP06858. Positions 36-450.
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

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP06858.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG091G052B.
PhylomeDBiP06858.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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.

P06858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKALLVLT LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA 
        60         70         80         90        100
EDTCHLIPGV AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY 
       110        120        130        140        150
KREPDSNVIV VDWLSRAQEH 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):53,162
Last modified:January 1, 1988 - v1
Checksum:iFBD00FCD334FB8AA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 Publications
Corresponds to variant rs1801177 [ dbSNP | Ensembl ].		VAR_011948
Natural varianti70 – 701N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications
VAR_057914
Natural varianti71 – 711H → Q.
Corresponds to variant rs11542065 [ dbSNP | Ensembl ].		VAR_049819
Natural varianti96 – 961V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 Publication
Corresponds to variant rs373088068 [ dbSNP | Ensembl ].		VAR_057915
Natural varianti98 – 981A → T in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs145657341 [ dbSNP | Ensembl ].		VAR_057916
Natural varianti102 – 1021R → S in LPL deficiency. 1 Publication
Corresponds to variant rs118204073 [ dbSNP | Ensembl ].		VAR_004211
Natural varianti113 – 1131W → G in LPL deficiency.
VAR_004212
Natural varianti113 – 1131W → R in LPL deficiency. 2 Publications
Corresponds to variant rs118204069 [ dbSNP | Ensembl ].		VAR_004213
Natural varianti128 – 1281T → A in LPL deficiency. 2 Publications
VAR_057917
Natural varianti132 – 1321G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057918
Natural varianti163 – 1631H → R in LPL deficiency. 1 Publication
VAR_004214
Natural varianti169 – 1691G → E in LPL deficiency; loss of activity. 1 Publication
Corresponds to variant rs118204063 [ dbSNP | Ensembl ].		VAR_004215
Natural varianti181 – 1811G → S in LPL deficiency. 1 Publication
VAR_004216
Natural varianti181 – 1811G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057919
Natural varianti183 – 1831D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 Publications
Corresponds to variant rs118204064 [ dbSNP | Ensembl ].		VAR_004217
Natural varianti183 – 1831D → H in LPL deficiency. 1 Publication
Corresponds to variant rs781614031 [ dbSNP | Ensembl ].		VAR_057920
Natural varianti183 – 1831D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 Publications
VAR_004218
Natural varianti184 – 1841P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication
VAR_004219
Natural varianti185 – 1851A → T in LPL deficiency; 3.2% of activity.
Corresponds to variant rs748349562 [ dbSNP | Ensembl ].		VAR_004220
Natural varianti186 – 1861G → E in LPL deficiency. 1 Publication
VAR_057921
Natural varianti190 – 1901E → G in LPL deficiency. 1 Publication
VAR_057922
Natural varianti199 – 1991S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 Publications
Corresponds to variant rs118204072 [ dbSNP | Ensembl ].		VAR_004221
Natural varianti201 – 2011D → V in LPL deficiency. 1 Publication
VAR_057923
Natural varianti203 – 2031A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 Publication
Corresponds to variant rs118204056 [ dbSNP | Ensembl ].		VAR_004222
Natural varianti207 – 2071D → E in LPL deficiency. 1 Publication
Corresponds to variant rs118204076 [ dbSNP | Ensembl ].		VAR_004223
Natural varianti208 – 2081V → I in LPL deficiency; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057924
Natural varianti210 – 2101H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication
VAR_057925
Natural varianti210 – 2101H → Q in LPL deficiency; loss of activity.
VAR_004224
Natural varianti215 – 2151G → E in LPL deficiency; loss of activity. 12 Publications
Corresponds to variant rs118204057 [ dbSNP | Ensembl ].		VAR_004225
Natural varianti215 – 2151G → R in LPL deficiency. 2 Publications
VAR_057926
Natural varianti220 – 2201S → R in LPL deficiency; 2.0% of activity.
Corresponds to variant rs757546424 [ dbSNP | Ensembl ].		VAR_004226
Natural varianti221 – 2211I → T in LPL deficiency; loss of activity. 5 Publications
Corresponds to variant rs118204061 [ dbSNP | Ensembl ].		VAR_004227
Natural varianti222 – 2221G → E in LPL deficiency. 1 Publication
Corresponds to variant rs118204075 [ dbSNP | Ensembl ].		VAR_004228
Natural varianti225 – 2251K → R in LPL deficiency. 1 Publication
VAR_057927
Natural varianti227 – 2271V → A in LPL deficiency. 1 Publication
Corresponds to variant rs528243561 [ dbSNP | Ensembl ].		VAR_057928
Natural varianti231 – 2311D → E in LPL deficiency; loss of activity. 3 Publications
Corresponds to variant rs118204067 [ dbSNP | Ensembl ].		VAR_004229
Natural varianti232 – 2321I → S in LPL deficiency. 1 Publication
Corresponds to variant rs770601263 [ dbSNP | Ensembl ].		VAR_004230
Natural varianti234 – 2341P → L in LPL deficiency; loss of activity. 2 Publications
Corresponds to variant rs118204060 [ dbSNP | Ensembl ].		VAR_004231
Natural varianti243 – 2431C → S in LPL deficiency; loss of activity. 1 Publication
VAR_004232
Natural varianti252 – 2521I → T in LPL deficiency. 1 Publication
Corresponds to variant rs118204080 [ dbSNP | Ensembl ].		VAR_057929
Natural varianti266 – 2661C → W in LPL deficiency. 1 Publication
Corresponds to variant rs118204082 [ dbSNP | Ensembl ].		VAR_057930
Natural varianti270 – 2701R → C in LPL deficiency. 4 Publications
Corresponds to variant rs118204077 [ dbSNP | Ensembl ].		VAR_057931
Natural varianti270 – 2701R → H in LPL deficiency; loss of activity. 6 Publications
Corresponds to variant rs118204062 [ dbSNP | Ensembl ].		VAR_004233
Natural varianti271 – 2711S → T in LPL deficiency. 1 Publication
Corresponds to variant rs28934893 [ dbSNP | Ensembl ].		VAR_004234
Natural varianti277 – 2771D → N in LPL deficiency; 5% of full activity. 5 Publications
Corresponds to variant rs118204068 [ dbSNP | Ensembl ].		VAR_004235
Natural varianti278 – 2781S → C in LPL deficiency.
VAR_004236
Natural varianti279 – 2791L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 Publications
Corresponds to variant rs35414700 [ dbSNP | Ensembl ].		VAR_057932
Natural varianti279 – 2791L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs371282890 [ dbSNP | Ensembl ].		VAR_057933
Natural varianti286 – 2861S → G in LPL deficiency. 1 Publication
VAR_004237
Natural varianti286 – 2861S → R in LPL deficiency. 1 Publication
VAR_004238
Natural varianti288 – 2881A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 Publications
Corresponds to variant rs1800011 [ dbSNP | Ensembl ].		VAR_011949
Natural varianti289 – 2891Y → H in LPL deficiency; no enzyme activity. 1 Publication
VAR_057934
Natural varianti297 – 2971F → L in LPL deficiency and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. 2 Publications
VAR_057935
Natural varianti303 – 3031L → F in LPL deficiency; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. 1 Publication
VAR_057936
Natural varianti305 – 3051C → R in LPL deficiency. 1 Publication
Corresponds to variant rs773235712 [ dbSNP | Ensembl ].		VAR_057937
Natural varianti310 – 3101C → Y in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057938
Natural varianti313 – 3131L → P in LPL deficiency. 1 Publication
VAR_057939
Natural varianti318 – 3181N → S in LPL deficiency; loss of activity; frequent mutation. 8 Publications
Corresponds to variant rs268 [ dbSNP | Ensembl ].		VAR_004239
Natural varianti325 – 3251S → R in LPL deficiency; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs761265900 [ dbSNP | Ensembl ].		VAR_057940
Natural varianti328 – 3281M → R in LPL deficiency. 1 Publication
VAR_057941
Natural varianti328 – 3281M → T in LPL deficiency.
VAR_004240
Natural varianti330 – 3301L → F in LPL deficiency. 1 Publication
VAR_057942
Natural varianti330 – 3301L → P in LPL deficiency.
VAR_004241
Natural varianti361 – 3611A → T in LPL deficiency. 2 Publications
Corresponds to variant rs118204071 [ dbSNP | Ensembl ].		VAR_004242
Natural varianti365 – 3651S → F in LPL deficiency; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
Corresponds to variant rs546542623 [ dbSNP | Ensembl ].		VAR_057943
Natural varianti370 – 3701V → M.1 Publication
Corresponds to variant rs298 [ dbSNP | Ensembl ].		VAR_011950
Natural varianti379 – 3791T → A.1 Publication
Corresponds to variant rs300 [ dbSNP | Ensembl ].		VAR_011951
Natural varianti392 – 3921L → V in LPL deficiency; loss of activity. 1 Publication
Corresponds to variant rs118204078 [ dbSNP | Ensembl ].		VAR_004243
Natural varianti423 – 4242Missing in LPL deficiency; affects the protein folding.
VAR_004244
Natural varianti427 – 4271A → T.1 Publication
Corresponds to variant rs5934 [ dbSNP | Ensembl ].		VAR_011952
Natural varianti437 – 4371E → K in LPL deficiency. 1 Publication
VAR_004245
Natural varianti437 – 4371E → V in LPL deficiency. 1 Publication
VAR_004246
Natural varianti445 – 4451C → Y in LPL deficiency; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities. 1 Publication
Corresponds to variant rs118204079 [ dbSNP | Ensembl ].		VAR_057944
Natural varianti448 – 4481E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 Publication
Corresponds to variant rs149089920 [ dbSNP | Ensembl ].		VAR_057945

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15856 mRNA. Translation: AAB59536.1.
X14390 mRNA. Translation: CAA32564.1.
X54516 mRNA. Translation: CAA38372.1.
M76722 Genomic DNA. Translation: AAA59528.1.
S76076 Genomic DNA. Translation: AAB21000.1.
S76077 Genomic DNA. Translation: AAB20999.1.
BT006726 mRNA. Translation: AAP35372.1.
AK312311 mRNA. Translation: BAG35236.1.
CH471080 Genomic DNA. Translation: EAW63764.1.
BC011353 mRNA. Translation: AAH11353.1.
X68111 Genomic DNA. Translation: CAA48230.1.
CCDSiCCDS6012.1.
PIRiA26082. LIHUL.
RefSeqiNP_000228.1. NM_000237.2.
UniGeneiHs.180878.

Genome annotation databases

EnsembliENST00000311322; ENSP00000309757; ENSG00000175445.
GeneIDi4023.
KEGGihsa:4023.
UCSCiuc003wzk.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Lipoprotein lipase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15856 mRNA. Translation: AAB59536.1.
X14390 mRNA. Translation: CAA32564.1.
X54516 mRNA. Translation: CAA38372.1.
M76722 Genomic DNA. Translation: AAA59528.1.
S76076 Genomic DNA. Translation: AAB21000.1.
S76077 Genomic DNA. Translation: AAB20999.1.
BT006726 mRNA. Translation: AAP35372.1.
AK312311 mRNA. Translation: BAG35236.1.
CH471080 Genomic DNA. Translation: EAW63764.1.
BC011353 mRNA. Translation: AAH11353.1.
X68111 Genomic DNA. Translation: CAA48230.1.
CCDSiCCDS6012.1.
PIRiA26082. LIHUL.
RefSeqiNP_000228.1. NM_000237.2.
UniGeneiHs.180878.

3D structure databases

ProteinModelPortaliP06858.
SMRiP06858. Positions 36-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110205. 18 interactions.
IntActiP06858. 14 interactions.
MINTiMINT-1369348.
STRINGi9606.ENSP00000309757.

Chemistry

BindingDBiP06858.
ChEMBLiCHEMBL2060.
DrugBankiDB05269. AST-120.
DB06439. Tyloxapol.
SwissLipidsiSLP:000000568.

Protein family/group databases

ESTHERihuman-LPL. Lipoprotein_Lipase.

PTM databases

iPTMnetiP06858.
PhosphoSiteiP06858.

Polymorphism and mutation databases

BioMutaiLPL.
DMDMi126314.

Proteomic databases

EPDiP06858.
MaxQBiP06858.
PaxDbiP06858.
PeptideAtlasiP06858.
PRIDEiP06858.

Protocols and materials databases

DNASUi4023.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311322; ENSP00000309757; ENSG00000175445.
GeneIDi4023.
KEGGihsa:4023.
UCSCiuc003wzk.5. human.

Organism-specific databases

CTDi4023.
GeneCardsiLPL.
GeneReviewsiLPL.
HGNCiHGNC:6677. LPL.
HPAiHPA048749.
MalaCardsiLPL.
MIMi238600. phenotype.
609708. gene.
neXtProtiNX_P06858.
Orphaneti309015. Familial lipoprotein lipase deficiency.
70470. Hyperlipoproteinemia type 5.
PharmGKBiPA232.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP06858.
KOiK01059.
OMAiESVANCH.
OrthoDBiEOG091G052B.
PhylomeDBiP06858.
TreeFamiTF324997.

Enzyme and pathway databases

BRENDAi3.1.1.34. 2681.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-975634. Retinoid metabolism and transport.

Miscellaneous databases

GeneWikiiLipoprotein_lipase.
GenomeRNAii4023.
PROiP06858.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175445.
CleanExiHS_LPL.
ExpressionAtlasiP06858. baseline and differential.
GenevisibleiP06858. HS.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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]
ProtoNetiSearch...

Entry informationi

Entry nameiLIPL_HUMAN
AccessioniPrimary (citable) accession number: P06858
Secondary accession number(s): B2R5T9
, Q16282, Q16283, Q96FC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: September 7, 2016
This is version 202 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.