ID A0A3Q2XLN1_HIPCM Unreviewed; 520 AA. AC A0A3Q2XLN1; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 03-JUL-2019, entry version 4. 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}; OS Hippocampus comes (Tiger tail seahorse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Syngnathiaria; Syngnathiformes; Syngnathoidei; Syngnathidae; OC Hippocampus. OX NCBI_TaxID=109280 {ECO:0000313|Ensembl:ENSHCOP00000000886, ECO:0000313|Proteomes:UP000264820}; RN [1] {ECO:0000313|Ensembl:ENSHCOP00000000886, ECO:0000313|Proteomes:UP000264820} RP NUCLEOTIDE SEQUENCE. RA Lin Q.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSHCOP00000000886} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2019) to UniProtKB. 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 Ensembl; ENSHCOT00000013022; ENSHCOP00000000886; ENSHCOG00000002080. DR GeneTree; ENSGT00940000157178; -. DR Proteomes; UP000264820; Whole Genome Shotgun Assembly. 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; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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/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 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2}; KW Cell membrane {ECO:0000256|RuleBase:RU362020}; KW Chylomicron {ECO:0000256|RuleBase:RU362020}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000264820}; KW Disulfide bond {ECO:0000256|RuleBase:RU362020, KW ECO:0000256|SAAS:SAAS00709807}; 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 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}; VLDL {ECO:0000256|RuleBase:RU362020}. FT DOMAIN 368 491 PLAT. {ECO:0000259|PROSITE:PS50095}. FT COILED 491 511 {ECO:0000256|SAM:Coils}. FT ACT_SITE 183 183 Nucleophile. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT ACT_SITE 207 207 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT ACT_SITE 295 295 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT METAL 226 226 Calcium. {ECO:0000256|PIRSR:PIRSR000865- FT 2}. SQ SEQUENCE 520 AA; 58872 MW; 4F8F78A72FD64ABC CRC64; KLLKLLFFNE HNYEKLPNLV FCAPMTSHIS VSACVTTVNG SVTPTSLPVT TTEWLTDYTD IVSKFSLRSA DTPDDDMCYI VAGRPDTIQE CKFNAQTQTF VIIHGWTVTG MFESWVPKLV SALYERVPNA NVIVVDWLTR ANQHYSTSAA YTKLAGRDVA KFVTWIQKEL QLPWDKIHLL GYSLGAHVAG IAGYLTDHKI SRITGLDPAG PTFEHAEDQN TLSRDDAQFV DVLHTNTRGS PGRSIGIQKP VGHIDIYPNG GAFQPGCDIQ NTLKGIALEG LKGLQNMDQL VKCSHERSIH LFIDSLLNTQ QQSMAYRCNS RESFNKGLCL SCRKNRCNKI GYNINKVRTA RSAMMYLKTR EKMPYKVFHY QVKMHMFSDR RLTFNEQPIK VSLYGTHGEK EDISFVLPVM NHNSTVSFLI TTDVDIGDLM IVKLRWEKDS IFSWPDWRGS NKFYIRKLRI KSGETQSKVS FRAKEAEFSD LVRGGEAAVF VKSKEDNLSR KERLMHKIKT QGSLFGQTDA //