ID   A0A8D0GW52_SPHPU        Unreviewed;       451 AA.
AC   A0A8D0GW52;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   12-OCT-2022, 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};
GN   Name=LPL {ECO:0000313|Ensembl:ENSSPUP00000012319};
OS   Sphenodon punctatus (Tuatara) (Hatteria punctata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Sphenodontia; Sphenodontidae; Sphenodon.
OX   NCBI_TaxID=8508 {ECO:0000313|Ensembl:ENSSPUP00000012319, ECO:0000313|Proteomes:UP000694392};
RN   [1] {ECO:0000313|Ensembl:ENSSPUP00000012319}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2021) 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|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   Ensembl; ENSSPUT00000013132.1; ENSSPUP00000012319.1; ENSSPUG00000009443.1.
DR   GeneTree; ENSGT00940000157178; -.
DR   Proteomes; UP000694392; 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: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   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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|RuleBase:RU362020};
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|RuleBase:RU362020};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Nitration {ECO:0000256|RuleBase:RU362020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694392};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362020};
KW   VLDL {ECO:0000256|RuleBase:RU362020}.
FT   DOMAIN          320..443
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   ACT_SITE        138
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        162
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        247
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ   SEQUENCE   451 AA;  51340 MW;  F02738A6196D645C CRC64;
     PCLAWASPEK RDFGGIESKF ALRTVKEPDE DTCYLVPGQE DTVAKCNFNH TSKTFVVIHG
     WTVTGMYESW IPKLVYALYK REPESNVIVV DWLRRAQQHY PVSAAYAQQV GEDIATFVDW
     MEEQFNYQLD NLHLLGYSLG AHAAGIAGSL TKTKINRITG LDPAGPNFEY AEANTRLSPD
     DAGFVDVLHT YTRGSPDRSI GIQKPVGHID IYPNGGGFQP GCNLGETIRL LAERGFGDVD
     QLVKCSHERS IHLFIDSLLY EESPSLAYRC STKETFEKGL CLSCRKNRCN SLGYNINKVR
     TKRSTKMYLK TRSQMPYKVF HYQVKIHFFG KLNVTKTNQP FLLSLYGTLD ESENIAFILP
     EISTNKTASF LIYTEVNIGD LLMLKLQWEN DSIFSWSNWW INPEFRIQRV RVKAGETQKK
     LVFCSRDGIS HLKKGKEAVV FVRCTDKFMN V
//