LIPS_BOVIN
ID LIPS_BOVIN Reviewed; 756 AA.
AC P16386; A1YWA8; Q562H4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 128.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Guo Y.Q., Xu S.Z., Gao X., Zhang L.P.;
RT "cDNA cloning of bovine LIPE gene.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-169.
RC TISSUE=Blood;
RA Ma Z.-J., Zhong J.-C., Guan W.-X., Zhao S., He K.;
RT "HSL Gene Sequence and Phylogenetic Evolution of Bovinae (Bos taurus, Bos
RT grunniens, Bubalus bubalis, and Bos frontalis).";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-169.
RC STRAIN=Korean;
RA Chung E.R., Shin S.C., Park J.G., Gwon S.Y.;
RT "Sequencing of hormone-sensitive lipase (LIPE) gene in Korean cattle.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 545-571, AND PHOSPHORYLATION AT SER-552 AND SER-554.
RX PubMed=3345839; DOI=10.1016/0014-5793(88)80799-3;
RA Garton A.J., Campbell D.G., Cohen P., Yeaman S.J.;
RT "Primary structure of the site on bovine hormone-sensitive lipase
RT phosphorylated by cyclic AMP-dependent protein kinase.";
RL FEBS Lett. 229:68-72(1988).
RN [5]
RP PROTEIN SEQUENCE OF 552-556, AND PHOSPHORYLATION AT SER-554.
RC TISSUE=Adipose tissue;
RX PubMed=2537200; DOI=10.1111/j.1432-1033.1989.tb14548.x;
RA Garton A.J., Campbell D.G., Carling D., Hardie D.G., Colbran R.J.,
RA Yeaman S.J.;
RT "Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated
RT protein kinase. A possible antilipolytic mechanism.";
RL Eur. J. Biochem. 179:249-254(1989).
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:P15304};
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; EF140760; ABL84202.1; -; mRNA.
DR EMBL; AY986820; AAX82971.1; -; Genomic_DNA.
DR EMBL; DQ523227; ABG54259.1; -; Genomic_DNA.
DR PIR; S00347; S00347.
DR RefSeq; NP_001073689.1; NM_001080220.1.
DR AlphaFoldDB; P16386; -.
DR SMR; P16386; -.
DR STRING; 9913.ENSBTAP00000041426; -.
DR ESTHER; bovin-hslip; Hormone-sensitive_lipase_like.
DR iPTMnet; P16386; -.
DR PaxDb; P16386; -.
DR GeneID; 286879; -.
DR KEGG; bta:286879; -.
DR CTD; 3991; -.
DR eggNOG; KOG4388; Eukaryota.
DR InParanoid; P16386; -.
DR OrthoDB; 1263520at2759; -.
DR BRENDA; 3.1.1.79; 908.
DR UniPathway; UPA00256; -.
DR Proteomes; UP000009136; 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 1: Evidence at protein level;
KW Cell membrane; Cholesterol metabolism; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Steroid metabolism; Sterol metabolism.
FT CHAIN 1..756
FT /note="Hormone-sensitive lipase"
FT /id="PRO_0000071546"
FT REGION 542..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..600
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 692
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 722
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT MOD_RES 552
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:3345839"
FT MOD_RES 554
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:2537200,
FT ECO:0000269|PubMed:3345839"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15304"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15304"
FT CONFLICT 12
FT /note="T -> S (in Ref. 1; ABL84202)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> P (in Ref. 1; ABL84202)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="S -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 82641 MW; 7E3AACB65DDD68FC CRC64;
MDLRTMTQSL VTLAEDNMAF FSSQGPGETA RRLTGVFAGI REQALGLEPA LGRLLSVAHL
FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRRSI FFRTSHNLAE LEAYLAALTQ
LRALAYYAQR LLTTNQPGRL FFEGDERVIA DFLREYVTLH KGCFYGRCLG FQFTPAIRPF
LQTISIGLVS FGEHYKRNET GISVTASSLF TDGRFAIDPE LRGAEFERII QNLDVHFWKA
FWNITEIQVL SSLANMASTT VRVSRLLSLP PVAFEMPLTS DPELTVTISP PLAHTGPGPV
LVRLISYDLR EGQDSKELSS FVRSEGPRSL ELRLRPQQAP RSRALVVHIH GGGFVAQTSK
SHEPYLKSWA QELGAPILSI DYSLAPEAPF PRALEECFYA YCWAVKHCAL LGSTGERICL
AGDSAGGNLC FTVSLRAAAY GVRVPDGIMA AYPATMLQST ASPSRLLSLM DHLLPLSVLS
KCVSTYAGAE TEDHPDSDQK ALGVMGLVQR DTALLLRDLR LGASSWLNSF LELGGQKSHL
KSVSKTEPMR RSVSEAALTQ PEGSLGTDSL KSLKLHDLGL RNSSDTTDTP ELSLSAETLG
PSAPSTINFL LGSEDGSEMS KAPEELNNKD RVRGVGAAFP EGFHPRRCSQ GAMWMPLYSA
PIVKNPSMSP LLAPDSMLQT LPPVHIVACA LDPMLDDSVM FARRLRGLGQ PVTLRVAEDL
PHGFLSLAAL CRETRQAAAL CVERIRLILN LPGPPV
