ID A0A3Q1HF25_ANATE Unreviewed; 520 AA.
AC A0A3Q1HF25;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
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 Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000007252.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000007252.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR AlphaFoldDB; A0A3Q1HF25; -.
DR Ensembl; ENSATET00000007375.2; ENSATEP00000007252.2; ENSATEG00000005074.2.
DR GeneTree; ENSGT00940000157178; -.
DR InParanoid; A0A3Q1HF25; -.
DR Proteomes; UP000265040; 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 Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362020};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362020};
KW VLDL {ECO:0000256|ARBA:ARBA00023313, ECO:0000256|RuleBase:RU362020}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU362020"
FT CHAIN 24..520
FT /note="Lipoprotein lipase"
FT /evidence="ECO:0000256|RuleBase:RU362020"
FT /id="PRO_5031609046"
FT DOMAIN 369..492
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT REGION 494..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 520 AA; 58273 MW; 77CC1F23E45CCCF4 CRC64;
MGNENICIFS LWIILGNIFA TFSSDPEAAA GVSLLGILTN FLNATATPPP ATTEWITDYT
DIVSKFSLRS SDIPDDDMCY IVAGSPETIK ECEFNSETQT FVVIHGWTVT GMFESWVPKL
VTALYEREPS ANVIVVDWLT RANQHYPTSA AYTKLVGRDV AKFVTWLQKE LQLPWERIHL
LGYSLGAHVA GIAGDLTDHK ISRITGLDPA GPTFEHADDQ STLSRGDAQF VDVLHTNTRG
SPDRSIGIQR PVGHIDIYPN GGTFQPGCDI QNTLLGIALE GIKGLQNMDQ LVKCSHERSI
HLFIDSLLNT QQQSMAYRCN SKEAFNKGLC LSCRKNRCNK LGYNINKVRS PRSAKMYLKT
REMMPYKVFH YQVKLHFFSK DQLSFTEQPM KISLYGTHGE KQDIPFVLPV MNGNSTVSFL
ITTDTDVGDL MIVKLRWEKD TIISWSNWWG SSQFYIRKLR VKSGETQSKV IFSAKEGEFA
YLVRGGENAE FVKSKESSAS RRGKLQKLKT QGSLFGQNDA
//
