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Lipoprotein lipase (LPL) (EC 3.1.1.34)

 LIPL_SHEEP              Reviewed;         478 AA.
Q29524;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=Lipoprotein lipase;
Short=LPL;
EC=3.1.1.34 {ECO:0000250|UniProtKB:P11151};
Flags: Precursor;
Name=LPL;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Welsh Mountain/Dorset; TISSUE=Adipose tissue;
PubMed=8439555; DOI=10.1016/0167-4781(93)90286-M;
Edwards W.D., Daniels S.W., Page R.A., Volpe C.P., Kille P.,
Sweeney G.E., Cryer A.;
"Cloning and sequencing of a full length cDNA encoding ovine
lipoprotein lipase.";
Biochim. Biophys. Acta 1172:167-170(1993).
-!- FUNCTION: 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.
{ECO:0000250, ECO:0000250|UniProtKB:P06858}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000250|UniProtKB:P11151}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with APOC2; the
interaction activates LPL activity in the presence of lipids (By
similarity). Interacts with GPIHBP1. Interacts with LMF1 and SEL1L
(By similarity). {ECO:0000250|UniProtKB:P11151,
ECO:0000250|UniProtKB:P11152}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:P06858}.
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). {ECO:0000250}.
-!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge
down-regulates the lipase activity.
{ECO:0000250|UniProtKB:Q06000}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
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EMBL; X68308; CAA48384.1; -; mRNA.
PIR; S29846; S29846.
RefSeq; NP_001009394.1; NM_001009394.1.
UniGene; Oar.459; -.
ProteinModelPortal; Q29524; -.
SMR; Q29524; -.
ESTHER; sheep-lipli; Lipoprotein_Lipase.
Ensembl; ENSOART00000011666; ENSOARP00000011504; ENSOARG00000010719.
GeneID; 443408; -.
KEGG; oas:443408; -.
CTD; 4023; -.
GeneTree; ENSGT00760000119069; -.
HOVERGEN; HBG002259; -.
KO; K01059; -.
OMA; HYQVKIH; -.
OrthoDB; EOG091G052B; -.
Proteomes; UP000002356; Chromosome 2.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0004465; F:lipoprotein lipase activity; ISS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:Ensembl.
GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IEA:Ensembl.
GO; GO:0090197; P:positive regulation of chemokine secretion; IEA:Ensembl.
GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; ISS:AgBase.
GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
GO; GO:0019433; P:triglyceride catabolic process; ISS:UniProtKB.
GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IEA:Ensembl.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002330; Lipo_Lipase.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
PANTHER; PTHR11610:SF3; PTHR11610:SF3; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00822; LIPOLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
TIGRFAMs; TIGR03230; lipo_lipase; 1.
PROSITE; PS00120; LIPASE_SER; 1.
PROSITE; PS50095; PLAT; 1.
2: Evidence at transcript level;
Cell membrane; Chylomicron; Complete proteome; Disulfide bond;
Glycoprotein; GPI-anchor; Heparin-binding; Hydrolase;
Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Nitration;
Reference proteome; Secreted; Signal; VLDL.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 478 Lipoprotein lipase.
/FTId=PRO_0000017781.
DOMAIN 344 467 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
REGION 349 444 Heparin-binding. {ECO:0000250}.
ACT_SITE 162 162 Nucleophile.
ACT_SITE 186 186 Charge relay system.
ACT_SITE 271 271 Charge relay system.
MOD_RES 124 124 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q06000}.
MOD_RES 194 194 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q06000}.
MOD_RES 346 346 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q06000}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 70 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 246 269 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 294 313 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 305 308 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 448 468 {ECO:0000255|PROSITE-ProRule:PRU00152}.
SEQUENCE 478 AA; 53588 MW; 10F41EE1FFB9C882 CRC64;
MESKVLLLLA LSVWLQSLTV SRGGLVAADR ITRGKDFRDI ESKFALRTPE DTAEDTCHLI
PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA
QQHYPVSAGY TKLVGQDVAK FMNWMADEFN YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN
RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG
TFQPGCNIGE ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF
EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESNTY
TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV DIGELLMLKL KWISDSYFSW
SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR EKMSYLQKGK SPVIFVKCHD KSLNRKSG


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