ID G9K8I1_MUSPF Unreviewed; 474 AA. AC G9K8I1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 19-JAN-2022, entry version 54. DE RecName: Full=Lipoprotein lipase {ECO:0000256|ARBA:ARBA00018617, ECO:0000256|RuleBase:RU362020}; DE Short=LPL {ECO:0000256|RuleBase:RU362020}; DE EC=3.1.1.34 {ECO:0000256|ARBA:ARBA00013181, ECO:0000256|RuleBase:RU362020}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae; OC 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., Ross T.M., RA 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 low CC density lipoproteins (VLDL), and thereby plays an important role in CC lipid clearance from the blood stream, lipid utilization and storage. CC Mediates margination of triglyceride-rich lipoprotein particles in CC capillaries. Recruited to its site of action on the luminal surface of CC vascular endothelium by binding to GPIHBP1 and cell surface heparan CC sulfate proteoglycans. {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, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34; CC Evidence={ECO:0000256|ARBA:ARBA00000137, CC ECO:0000256|RuleBase:RU362020}; CC -!- SUBUNIT: Homodimer. Interacts with APOC2; the interaction activates LPL CC activity in the presence of lipids. {ECO:0000256|RuleBase:RU362020}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362020}; CC Peripheral membrane protein {ECO:0000256|RuleBase:RU362020}; CC Extracellular side {ECO:0000256|RuleBase:RU362020}. Secreted CC {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU362020}. CC Secreted, extracellular space, extracellular matrix CC {ECO:0000256|RuleBase:RU362020}. Note=Newly synthesized LPL binds to CC cell surface heparan proteoglycans and is then released by heparanase. CC Subsequently, it becomes attached to heparan proteoglycan on CC endothelial cells. Locates to the plasma membrane of microvilli of CC hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the CC bound LPL is then internalized and located inside non-coated endocytic CC vesicles. {ECO:0000256|RuleBase:RU362020}. CC -!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down- CC regulates the lipase activity. {ECO:0000256|RuleBase:RU362020}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family. CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}. 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 ESTHER; muspf-g9k8i1; Lipoprotein_Lipase. DR OMA; TRDMMPY; -. DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule. DR GO; GO:0004465; F:lipoprotein lipase activity; ISS:AgBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009749; P:response to glucose; ISS:AgBase. DR GO; GO:0019433; P:triglyceride catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00707; Pancreat_lipase_like; 1. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR013818; Lipase. 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|ARBA:ARBA00022513, ECO:0000256|RuleBase:RU362020}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|RuleBase:RU362020}; KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674, KW ECO:0000256|RuleBase:RU362020}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362020}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, KW ECO:0000256|RuleBase:RU362020}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|RuleBase:RU362020}; Lipoprotein {ECO:0000313|EMBL:AES01206.1}; KW Membrane {ECO:0000256|RuleBase:RU362020}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2}; KW Nitration {ECO:0000256|ARBA:ARBA00023074, ECO:0000256|RuleBase:RU362020}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362020}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362020}; KW VLDL {ECO:0000256|RuleBase:RU362020}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|RuleBase:RU362020" FT CHAIN 21..474 FT /note="Lipoprotein lipase" FT /evidence="ECO:0000256|RuleBase:RU362020" FT /id="PRO_5005133119" FT DOMAIN 341..464 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT ACT_SITE 159 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 183 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 268 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT METAL 197 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT METAL 202 FT /note="Calcium" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AES01206.1" FT NON_TER 474 FT /evidence="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 //