ID Q71UV2_HUMAN Unreviewed; 332 AA.
AC Q71UV2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Lipoprotein lipase {ECO:0000256|ARBA:ARBA00018617};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.34 {ECO:0000256|ARBA:ARBA00013181};
DE AltName: Full=Phospholipase A1 {ECO:0000256|ARBA:ARBA00031180};
DE Flags: Fragment;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAC61679.1};
RN [1] {ECO:0000313|EMBL:AAC61679.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9662394; DOI=10.1038/907;
RA Nickerson D.A., Taylor S.L., Weiss K.M., Clark A.G., Hutchinson R.G.,
RA Stengaerd J., Salomaa V., Vartiainen E., Boerwinkle E., Sing C.F.;
RT "DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase
RT gene.";
RL Nat. Genet. 19:233-240(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000256|ARBA:ARBA00000652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000256|ARBA:ARBA00000652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000256|ARBA:ARBA00001601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000256|ARBA:ARBA00001601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000256|ARBA:ARBA00001885};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC Evidence={ECO:0000256|ARBA:ARBA00001885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000256|ARBA:ARBA00000879};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000256|ARBA:ARBA00000879};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000256|ARBA:ARBA00000111};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004296};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296};
CC Extracellular side {ECO:0000256|ARBA:ARBA00004296}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000256|ARBA:ARBA00004498}.
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 EMBL; AF050163; AAC61679.1; -; Genomic_DNA.
DR AlphaFoldDB; Q71UV2; -.
DR ESTHER; human-LPL; Lipoprotein_Lipase.
DR PeptideAtlas; Q71UV2; -.
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:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004465; F:lipoprotein lipase activity; ISS:AgBase.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009749; P:response to glucose; ISS:AgBase.
DR CDD; cd01758; PLAT_LPL; 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; IPR002330; Lipo_Lipase.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF3; LIPOPROTEIN LIPASE; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chylomicron {ECO:0000256|ARBA:ARBA00022513};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Lipoprotein {ECO:0000313|EMBL:AAC61679.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nitration {ECO:0000256|ARBA:ARBA00023074};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW VLDL {ECO:0000256|ARBA:ARBA00023313}.
FT DOMAIN 198..321
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC61679.1"
FT NON_TER 332
FT /evidence="ECO:0000313|EMBL:AAC61679.1"
SQ SEQUENCE 332 AA; 37182 MW; 448D1A7A042A64AA CRC64;
EEFNYPLDNV HLLGYSLGAH AAGIAGSLTN KKVNRITGLD PAGPNFEYAE APSRLSPDDA
DFVDVLHTFT RGSPGRSIGI QKPVGHVDIY PNGGTFQPGC NIGEAIRVIA ERGLGDVDQL
VKCSHERSIH LFIDSLLNEE NPSKAYRCSS KEAFEKGLCL SCRKNRCNNL GYEINKVRAK
RSSKMYLKTR SQMPYKVFHY QVKIHFSGTE SETHTNQAFE ISLYGTVAES ENIPFTLPEV
STNKTYSFLI YTEVDIGELL MLKLKWKSDS YFSWSDWWSS PGFAIQKIRV KAGETQKKVI
FCSREKVSHL QKGKAPAVFV KCHDKSLNKK SG
//
