LIPS_PIG
ID LIPS_PIG Reviewed; 764 AA.
AC Q68J42; Q68J43; Q9TUK0; Q9TUK1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Hormone-sensitive lipase;
DE Short=HSL;
DE EC=3.1.1.79 {ECO:0000250|UniProtKB:P15304};
DE AltName: Full=Monoacylglycerol lipase LIPE;
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:P54310};
DE AltName: Full=Retinyl ester hydrolase {ECO:0000250|UniProtKB:P54310};
DE Short=REH;
GN Name=LIPE;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Large white, and Meishan;
RA Lei M.G., Xiong Y.Z., Deng C.Y., Li F.E., Zhang Z.B., Zheng R.;
RT "Sequences of porcine HSL gene of different pig breeds.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Norwegian Landrace; TISSUE=Adipose tissue;
RX PubMed=10050278; DOI=10.1046/j.1365-2052.1999.00412.x;
RA Harbitz I., Langset M., Ege A.G., Hoyheim B., Davies W.;
RT "The porcine hormone-sensitive lipase gene: sequence, structure,
RT polymorphisms and linkage mapping.";
RL Anim. Genet. 30:10-15(1999).
CC -!- FUNCTION: Lipase with broad substrate specificity, catalyzing the
CC hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs),
CC monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (By
CC similarity). Shows a preferential hydrolysis of DAGs over TAGs and MAGs
CC (By similarity). Preferentially hydrolyzes fatty acid (FA) esters at
CC the sn-3 position of the glycerol backbone in DAGs and FA esters at the
CC sn-1 and sn-2 positions of the glycerol backbone in TAGs (By
CC similarity). Catalyzes the hydrolysis of 2-arachidonoylglycerol, an
CC endocannabinoid and of 2-acetyl monoalkylglycerol ether, the
CC penultimate precursor of the pathway for de novo synthesis of platelet-
CC activating factor (By similarity). In adipose tissue and heart, it
CC primarily hydrolyzes stored triglycerides to free fatty acids, while in
CC steroidogenic tissues, it principally converts cholesteryl esters to
CC free cholesterol for steroid hormone production (By similarity).
CC {ECO:0000250|UniProtKB:P15304, ECO:0000250|UniProtKB:P54310,
CC ECO:0000250|UniProtKB:Q05469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.79;
CC Evidence={ECO:0000250|UniProtKB:P15304};
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=3.1.1.79;
CC Evidence={ECO:0000250|UniProtKB:P15304};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868; EC=3.1.1.79;
CC Evidence={ECO:0000250|UniProtKB:P15304};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+)
CC = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000250|UniProtKB:Q05469};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38381;
CC Evidence={ECO:0000250|UniProtKB:Q05469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:38383, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:73990, ChEBI:CHEBI:75824;
CC Evidence={ECO:0000250|UniProtKB:Q05469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38384;
CC Evidence={ECO:0000250|UniProtKB:Q05469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate +
CC cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:Q05469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000250|UniProtKB:Q05469};
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:0000250|UniProtKB:Q05469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:Q05469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:75937;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + H2O = 1-O-hexadecyl-sn-
CC glycerol + acetate + H(+); Xref=Rhea:RHEA:38563, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:34115,
CC ChEBI:CHEBI:75936; Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC octadecenoate + (9Z-octadecenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:39935, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75937;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39936;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75735, ChEBI:CHEBI:75937;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940;
CC Evidence={ECO:0000250|UniProtKB:P54310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38659,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:73990;
CC Evidence={ECO:0000250|UniProtKB:P15304};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38660;
CC Evidence={ECO:0000250|UniProtKB:P15304};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with CAVIN1
CC in the adipocyte cytoplasm (By similarity). Interacts with PLIN5 (By
CC similarity). {ECO:0000250|UniProtKB:P15304,
CC ECO:0000250|UniProtKB:P54310, ECO:0000250|UniProtKB:Q05469}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05469}.
CC Membrane, caveola {ECO:0000250|UniProtKB:Q05469}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q05469}. Lipid droplet
CC {ECO:0000250|UniProtKB:P54310}. Note=Found in the high-density
CC caveolae. Translocates to the cytoplasm from the caveolae upon insulin
CC stimulation. Phosphorylation by AMPK reduces its translocation towards
CC the lipid droplets. {ECO:0000250|UniProtKB:P54310,
CC ECO:0000250|UniProtKB:Q05469}.
CC -!- PTM: Phosphorylation by AMPK reduces its translocation towards the
CC lipid droplets. {ECO:0000250|UniProtKB:P54310}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY686758; AAT95416.1; -; mRNA.
DR EMBL; AY686759; AAT95417.1; -; mRNA.
DR EMBL; AJ000482; CAA04121.1; -; mRNA.
DR EMBL; AJ000483; CAA04122.1; -; Genomic_DNA.
DR EMBL; AJ006075; CAA04122.1; JOINED; Genomic_DNA.
DR EMBL; AJ006076; CAA04122.1; JOINED; Genomic_DNA.
DR RefSeq; NP_999480.1; NM_214315.1.
DR AlphaFoldDB; Q68J42; -.
DR SMR; Q68J42; -.
DR STRING; 9823.ENSSSCP00000003269; -.
DR ESTHER; pig-hslip; Hormone-sensitive_lipase_like.
DR MEROPS; S09.993; -.
DR PaxDb; Q68J42; -.
DR PeptideAtlas; Q68J42; -.
DR GeneID; 397583; -.
DR KEGG; ssc:397583; -.
DR CTD; 3991; -.
DR eggNOG; KOG4388; Eukaryota.
DR InParanoid; Q68J42; -.
DR UniPathway; UPA00256; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0102259; F:1,2-diacylglycerol acylhydrolase activity; ISS:UniProtKB.
DR GO; GO:0102258; F:1,3-diacylglycerol acylhydrolase activity; ISS:UniProtKB.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0033878; F:hormone-sensitive lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; ISS:UniProtKB.
DR GO; GO:0042134; F:rRNA primary transcript binding; ISS:UniProtKB.
DR GO; GO:0004771; F:sterol esterase activity; ISS:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046340; P:diacylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; ISS:UniProtKB.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; ISS:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR010468; HSL_N.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR Pfam; PF06350; HSL_N; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cholesterol metabolism; Cytoplasm; Hydrolase;
KW Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Steroid metabolism; Sterol metabolism.
FT CHAIN 1..764
FT /note="Hormone-sensitive lipase"
FT /id="PRO_0000071549"
FT REGION 316..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 350..352
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 691
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 721
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16386"
FT MOD_RES 554
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:P16386"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15304"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15304"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15304"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15304"
FT VARIANT 129
FT /note="Q -> H (in strain: Norwegian Landrace)"
FT VARIANT 148
FT /note="I -> V (in strain: Large white and Norwegian
FT Landrace)"
FT VARIANT 160
FT /note="H -> R (in strain: Large white)"
FT VARIANT 296
FT /note="G -> A (in strain: Norwegian Landrace)"
FT VARIANT 329
FT /note="G -> S (in strain: Norwegian Landrace)"
FT VARIANT 623
FT /note="D -> E (in strain: Large white and Norwegian
FT Landrace)"
FT VARIANT 644
FT /note="P -> S (in strain: Large white)"
FT VARIANT 705..706
FT /note="RS -> Q (in strain: Norwegian Landrace)"
FT VARIANT 722
FT /note="G -> R (in strain: Norwegian Landrace)"
SQ SEQUENCE 764 AA; 83450 MW; 68A9BC0C7B401C03 CRC64;
MDLRTMTQSL VTLAEDNMAF FSGQGPGETA RRLSGVFAGI REQALGLEPA LGRLLSVAHL
FDLDAETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRRSI FFRTSHNLAE LEAYLAALTQ
LRALAYYAQR LLAINRPGKL FFEGDEGITA DFLREYVTLH KGCFYGRCLG FQFTPAIRPF
LQTISIGLVS FGEHYKRNET GLSVTASSLF TSGRFAIDPE LRGAEFERII QNLDVHFWKA
FWNITEIEVL SSLANMASAT VRVSRLLSLP PKAFEMPLTA DPKLTVTISP PLAHTGPGPV
LVRLISYDLR EGQDSEELSS LVRSEGPRGL ELRPRPQQAP RSRSLVVHIH GGGFVAQTSK
SHEPYLKSWA QELGVPILSI DYSLAPEAPF PRALEECFYA YCWAVKHCGL LGSTGERICL
AGDSAGGNLC FTVSLRAAAY GVRVPDGIMA AYPATMLQSA ASPSRLLSLM DPLLPLSVLS
KCVSAYAGGE MEDHSDSDQK ALGMMGLVRR DTALLFRDLR LGASSWLNSF LELSGHKSRP
NLVPTEEPMR RSVSEAALAQ PEGPLGTDSL KYLTLHDLSL SSETQDTPEL SLSAETLGPT
TPSAVNFLFR PEDAPEEAEA RDDISTKEEK VYSVRAAFPE GFHPRRSSQG AIQMPLYSAP
IVKNPFMSPL LAPDSMLQTL PPVHIVACAL DPMLDDSVMF ARRLRSLGQP VTLHVVEDLP
HGFLSLAALC RETRQAAALC VDRIRFILNP PGPATPAGPT TPPV
