ID A0A3Q2XLN1_HIPCM Unreviewed; 520 AA. AC A0A3Q2XLN1; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 24-JAN-2024, entry version 17. 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}; OS Hippocampus comes (Tiger tail seahorse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Syngnathiaria; Syngnathiformes; Syngnathoidei; Syngnathidae; Hippocampus. OX NCBI_TaxID=109280 {ECO:0000313|Ensembl:ENSHCOP00000000886.1, ECO:0000313|Proteomes:UP000264820}; RN [1] {ECO:0000313|Ensembl:ENSHCOP00000000886.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. 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|RuleBase:RU362020}. Secreted, extracellular space, CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498, 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 AlphaFoldDB; A0A3Q2XLN1; -. DR STRING; 109280.ENSHCOP00000000886; -. DR Ensembl; ENSHCOT00000013022.1; ENSHCOP00000000886.1; ENSHCOG00000002080.1. DR GeneTree; ENSGT00940000157178; -. DR Proteomes; UP000264820; Unplaced. 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; alpha/beta hydrolase; 1. DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 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 NCBIfam; TIGR03230; lipo_lipase; 1. DR PANTHER; PTHR11610; LIPASE; 1. DR PANTHER; PTHR11610:SF3; LIPOPROTEIN LIPASE; 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; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1. DR PROSITE; PS50095; PLAT; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW 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|RuleBase:RU362020}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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 VLDL {ECO:0000256|ARBA:ARBA00023313, ECO:0000256|RuleBase:RU362020}. FT DOMAIN 368..491 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT ACT_SITE 183 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 207 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 295 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT BINDING 226 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" 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 //