ID G9K8I1_MUSPF Unreviewed; 474 AA. AC G9K8I1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 20-DEC-2017, entry version 40. DE RecName: Full=Lipoprotein lipase {ECO:0000256|RuleBase:RU362020}; DE Short=LPL {ECO:0000256|RuleBase:RU362020}; DE EC=3.1.1.34 {ECO:0000256|RuleBase:RU362020}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES01206.1}; RN [1] {ECO:0000313|EMBL:AES01206.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lungs {ECO:0000313|EMBL:AES01206.1}; RX PubMed=23236062; DOI=10.1128/JVI.02476-12; RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F., RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., RA Ross T.M., Farooqui A., Kelvin D.J.; RT "Sequencing, annotation, and characterization of the influenza ferret RT infectome."; RL J. Virol. 87:1957-1966(2013). CC -!- FUNCTION: The primary function of this lipase is the hydrolysis of CC triglycerides of circulating chylomicrons and very low density CC lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at CC the cell surface is vital to the function. The apolipoprotein, CC APOC2, acts as a coactivator of LPL activity in the presence of CC lipids on the luminal surface of vascular endothelium. CC {ECO:0000256|RuleBase:RU362020}. CC -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a CC carboxylate. {ECO:0000256|RuleBase:RU362020}. CC -!- SUBUNIT: Homodimer. Interacts with APOC2; the interaction CC activates LPL activity in the presence of lipids. CC {ECO:0000256|RuleBase:RU362020}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362020}; Lipid-anchor, GPI-anchor CC {ECO:0000256|RuleBase:RU362020}. Secreted CC {ECO:0000256|RuleBase:RU362020, ECO:0000256|SAAS:SAAS00553472}. CC Note=Locates to the plasma membrane of microvilli of hepatocytes CC with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound CC LPL is then internalized and located inside non-coated endocytic CC vesicles. {ECO:0000256|RuleBase:RU362020}. CC -!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge CC down-regulates the lipase activity. CC {ECO:0000256|RuleBase:RU362020}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase CC family. {ECO:0000256|RuleBase:RU362020, CC ECO:0000256|SAAS:SAAS00591292}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JP012608; AES01206.1; -; mRNA. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-UniRule. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-UniRule. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0004465; F:lipoprotein lipase activity; ISS:AgBase. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0009749; P:response to glucose; ISS:AgBase. DR CDD; cd00707; Pancreat_lipase_like; 1. DR Gene3D; 2.60.60.20; -; 1. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR013818; Lipase/vitellogenin. DR InterPro; IPR016272; Lipase_LIPH. DR InterPro; IPR033906; Lipase_N. DR InterPro; IPR002330; Lipo_Lipase. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR InterPro; IPR000734; TAG_lipase. DR PANTHER; PTHR11610; PTHR11610; 1. DR PANTHER; PTHR11610:SF3; PTHR11610:SF3; 1. DR Pfam; PF00151; Lipase; 1. DR Pfam; PF01477; PLAT; 1. DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1. DR PRINTS; PR00822; LIPOLIPASE. DR PRINTS; PR00821; TAGLIPASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR03230; lipo_lipase; 1. DR PROSITE; PS50095; PLAT; 1. PE 2: Evidence at transcript level; KW Cell membrane {ECO:0000256|RuleBase:RU362020}; KW Chylomicron {ECO:0000256|RuleBase:RU362020}; KW Disulfide bond {ECO:0000256|RuleBase:RU362020}; KW Glycoprotein {ECO:0000256|RuleBase:RU362020}; KW GPI-anchor {ECO:0000256|RuleBase:RU362020}; KW Heparin-binding {ECO:0000256|RuleBase:RU362020}; KW Hydrolase {ECO:0000256|RuleBase:RU362020}; KW Lipid degradation {ECO:0000256|RuleBase:RU362020}; KW Lipid metabolism {ECO:0000256|RuleBase:RU362020}; KW Lipoprotein {ECO:0000313|EMBL:AES01206.1}; KW Membrane {ECO:0000256|RuleBase:RU362020}; KW Nitration {ECO:0000256|RuleBase:RU362020}; KW Secreted {ECO:0000256|RuleBase:RU362020, KW ECO:0000256|SAAS:SAAS00439306}; KW Signal {ECO:0000256|RuleBase:RU362020}; KW VLDL {ECO:0000256|RuleBase:RU362020}. FT SIGNAL 1 20 {ECO:0000256|RuleBase:RU362020}. FT CHAIN 21 474 Lipoprotein lipase. FT {ECO:0000256|RuleBase:RU362020}. FT /FTId=PRO_5005133119. FT DOMAIN 341 464 PLAT. {ECO:0000259|PROSITE:PS50095}. FT ACT_SITE 159 159 Nucleophile. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT ACT_SITE 183 183 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT ACT_SITE 268 268 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AES01206.1}. FT NON_TER 474 474 {ECO:0000313|EMBL:AES01206.1}. SQ SEQUENCE 474 AA; 53115 MW; 4432A3B31451CAB4 CRC64; MESKALLLVA LGMWFQSLTA TRGGVAAADR GRDFIDIESK FALRTPEDTA EDTCHLIPGV TESVANCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLSRAQQH YPVSAGYTKL VGKDVAKFIN WMAEEFHYPL DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTESDTQTNQ AFEISLYGTV AESENIPFTL PEFSANKTYS FLIYTEVDIG ELLMLKLKWK NDSYFSWSDW WSSPSFAIEK IRVKAGETQK KVIFCSREKV SHLQKGKASV VFVKCHDKSL NKKS //