ID A0A3Q2WL60_HAPBU Unreviewed; 515 AA.
AC A0A3Q2WL60;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
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 Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000026526.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000026526.1}
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 RefSeq; XP_005920852.1; XM_005920790.1.
DR AlphaFoldDB; A0A3Q2WL60; -.
DR STRING; 8153.ENSHBUP00000026526; -.
DR Ensembl; ENSHBUT00000003116.1; ENSHBUP00000026526.1; ENSHBUG00000009247.1.
DR GeneID; 102302710; -.
DR CTD; 30354; -.
DR GeneTree; ENSGT00940000157178; -.
DR OMA; IRAQQHY; -.
DR OrthoDB; 3428256at2759; -.
DR Proteomes; UP000264840; 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:UP000264840};
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..515
FT /note="Lipoprotein lipase"
FT /evidence="ECO:0000256|RuleBase:RU362020"
FT /id="PRO_5018382634"
FT DOMAIN 363..486
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT REGION 487..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 515 AA; 58086 MW; E2107CC6BF313319 CRC64;
MGKQNICFLT AWIILGKIFA TFSSDLESNT TAFANTTVTI DQLLNTTEWL TDFTDIVSKF
SLRTADTPDD DMCYIVPGRP ETIKECNFNP ETQTFIVIHG WTVTGMFESW VPKLVSALYD
RVPTANVIVV DWLSRANQHY PTSAAYTKLV GRDVAKFVTW IQNELQLPWD RVHLLGYSLG
AHVAGIAGDL TNHKISRITG LDPAGPTFEH ADEQSTLSRG DAQFVDVLHT NTRGSPDRSI
GIQRPVGHID IYPNGGTFQP GCDIQNTLMG IALEGIKGLQ NMDQLVKCSH ERSIHLFIDS
LLNIEQQSVA FRCNSKDTFN KGMCLSCRKN RCNKIGYNVK KVRTARSTTM YLKTRGTMPF
KVFHYQVKAH FFSQNKQSFT EQPMKISLYG TNGEKEDIPF VLPALNSNTT QSFLITTDTD
IGDLMIVKLR WERDAYISWS NWWGSTKFNI RKLRIKCGET QSKVIFNAKD GEFVDLTRGG
ENAVFVKSKE DKQSRKEKLA HKLKTKGSLF GQQEA
//
