ID G9K8I1_MUSPF Unreviewed; 474 AA. AC G9K8I1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 08-MAY-2019, entry version 46. 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: Key enzyme in triglyceride metabolism. Catalyzes the CC hydrolysis of triglycerides from circulating chylomicrons and very CC low density lipoproteins (VLDL), and thereby plays an important CC role in lipid clearance from the blood stream, lipid utilization CC and storage. Mediates margination of triglyceride-rich lipoprotein CC particles in capillaries. Recruited to its site of action on the CC luminal surface of vascular endothelium by binding to GPIHBP1 and CC cell surface heparan sulfate proteoglycans. CC {ECO:0000256|RuleBase:RU362020}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid CC + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, CC ChEBI:CHEBI:28868; EC=3.1.1.34; CC Evidence={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}; Peripheral membrane protein CC {ECO:0000256|RuleBase:RU362020}; Extracellular side CC {ECO:0000256|RuleBase:RU362020}. Secreted CC {ECO:0000256|RuleBase:RU362020, ECO:0000256|SAAS:SAAS00553472}. CC Secreted, extracellular space, extracellular matrix CC {ECO:0000256|RuleBase:RU362020}. Note=Newly synthesized LPL binds CC to cell surface heparan proteoglycans and is then released by CC heparanase. Subsequently, it becomes attached to heparan CC proteoglycan on endothelial cells. Locates to the plasma membrane CC of microvilli of hepatocytes with triglyceride-rich lipoproteins CC (TRL). Some of the bound LPL is then internalized and located CC inside non-coated endocytic vesicles. CC {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:RU004262, 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; 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 Calcium {ECO:0000256|PIRSR:PIRSR000865-2}; KW Cell membrane {ECO:0000256|RuleBase:RU362020}; KW Chylomicron {ECO:0000256|RuleBase:RU362020}; KW Disulfide bond {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 Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2}; KW Nitration {ECO:0000256|RuleBase:RU362020}; KW Secreted {ECO:0000256|RuleBase:RU362020, KW ECO:0000256|SAAS:SAAS00288740}; 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 METAL 197 197 Calcium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000865-2}. FT METAL 202 202 Calcium. {ECO:0000256|PIRSR:PIRSR000865- FT 2}. 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 //