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Protein

Hormone-sensitive lipase

Gene

Lipe

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production.

Catalytic activityi

Diacylglycerol + H2O = monoacylglycerol + a carboxylate.
Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Monoacylglycerol + H2O = glycerol + a carboxylate.

Enzyme regulationi

Rapidly activated by cAMP-dependent phosphorylation under the influence of catecholamines. Dephosphorylation and inactivation are controlled by insulin.

Pathwayi: triacylglycerol degradation

This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway triacylglycerol degradation and in Glycerolipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei723PROSITE-ProRule annotation1
Active sitei1003By similarity1
Active sitei1033By similarity1

GO - Molecular functioni

  • acylglycerol lipase activity Source: RGD
  • hormone-sensitive lipase activity Source: UniProtKB-EC
  • hydrolase activity, acting on ester bonds Source: RGD
  • rRNA primary transcript binding Source: UniProtKB

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-KW
  • female pregnancy Source: RGD
  • lipid catabolic process Source: UniProtKB
  • response to drug Source: RGD
  • termination of RNA polymerase I transcription Source: UniProtKB
  • transcription initiation from RNA polymerase I promoter Source: UniProtKB
  • triglyceride catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDAi3.1.1.79. 5301.
ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
UniPathwayiUPA00256.

Protein family/group databases

ESTHERiratno-hslip. Hormone-sensitive_lipase_like_1.
MEROPSiS09.993.

Chemistry databases

SwissLipidsiSLP:000000320.

Names & Taxonomyi

Protein namesi
Recommended name:
Hormone-sensitive lipase (EC:3.1.1.79)
Short name:
HSL
Gene namesi
Name:Lipe
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3010. Lipe.

Subcellular locationi

  • Cell membrane By similarity
  • Membranecaveola By similarity
  • Cytoplasmcytosol By similarity

  • Note: Found in the high-density caveolae. Translocates to the cytoplasm from the caveolae upon insulin stimulation.By similarity

GO - Cellular componenti

  • caveola Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular space Source: RGD
  • lipid particle Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi863S → A or E: No effect on activation by PKA. 1 Publication1
Mutagenesisi865S → A: Increases activation by PKA. 1 Publication1
Mutagenesisi865S → E: No effect on activation by PKA. 1 Publication1
Mutagenesisi959S → A: Slightly decreases activation by PKA. Abolishes activation by PKA; when associated with A-960. 1 Publication1
Mutagenesisi960S → A: No effect on activation by PKA. Abolishes activation by PKA; when associated with A-959. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5582.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000715501 – 1068Hormone-sensitive lipaseAdd BLAST1068

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei863Phosphoserine; by PKA1 Publication1
Modified residuei865PhosphoserineCombined sources1
Modified residuei906PhosphoserineCombined sources1
Modified residuei927PhosphoserineCombined sources1
Modified residuei938PhosphoserineCombined sources1
Modified residuei959Phosphoserine; by PKA1 Publication1
Modified residuei960Phosphoserine; by PKA1 Publication1
Modified residuei1068PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylation by AMPK may block translocation to lipid droplets.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP15304.
PRIDEiP15304.

PTM databases

iPTMnetiP15304.
PhosphoSitePlusiP15304.

Interactioni

Subunit structurei

Interacts with PTRF in the adipocyte cytoplasm (By similarity). Interacts with PLIN5.By similarity1 Publication

Protein-protein interaction databases

BioGridi247369. 2 interactors.
IntActiP15304. 1 interactor.
MINTiMINT-4783535.
STRINGi10116.ENSRNOP00000027911.

Chemistry databases

BindingDBiP15304.

Structurei

3D structure databases

ProteinModelPortaliP15304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi649 – 651Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity3

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Phylogenomic databases

eggNOGiKOG4388. Eukaryota.
COG0657. LUCA.
HOGENOMiHOG000047722.
HOVERGENiHBG000187.
InParanoidiP15304.
KOiK07188.
PhylomeDBiP15304.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR010468. HSL_N.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
PF06350. HSL_N. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P15304-1) [UniParc]FASTAAdd to basket
Also known as: Testicular

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKPRRPISFT REITAMEPSS TSVSRPEWRP EAQQTLTDYP GSRELQEFGI
60 70 80 90 100
PQKQSLPNEA TAQQGAEFQQ EQGVQQSTLL QKLLTPLAFP VPQQSFPSHK
110 120 130 140 150
VHSDQQEATS QNGPGAGKVH TTQKELEHRD EHVGTAESGP AEPPPATEVE
160 170 180 190 200
ATSIAQAVSG PDKKLPTQTD LVSQERAEQS DPTAQQTPLV QGVKSDQGSL
210 220 230 240 250
IESGILARLQ KLAIQQPSQE WKTFLDCVTE SDMEKYLNSS SKSNPPEPSG
260 270 280 290 300
GTVIPGTLPS KQKPDCGKMS GYGGKLPHGK KGILQKHKHY WDTASAFSHS
310 320 330 340 350
MDLRTMTQSL VALAEDNMAF FSSQGPGETA RRLSNVFAGV REQALGLEPT
360 370 380 390 400
LGQLLGVAHH FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRRSI
410 420 430 440 450
FFRASHNLAE LEAYLAALTQ LRALAYYAQR LLTINRPGVL FFEGDEGLSA
460 470 480 490 500
DFLQDYVTLH KGCFYGRCLG FQFTPAIRPF LQTLSIGLVS FGEHYKRNET
510 520 530 540 550
GLSVTASSLF TGGRFAIDPE LRGAEFERII QNLDVHFWKA FWNITEIEVL
560 570 580 590 600
SSLANMASTT VRVSRLLSLP PEAFEMPLTS DPKLTVTISP PLAHTGPGPV
610 620 630 640 650
LARLISYDLR EGQDSKMLNS LAKSEGPRLE LRPRPQQAPR SRALVVHIHG
660 670 680 690 700
GGFVAQTSKS HEPYLKNWAQ ELGVPIISID YSLAPEAPFP RALEECFFAY
710 720 730 740 750
CWAVKHCELL GSTGERICLA GDSAGGNLCI TVSLRAAAYG VRVPDGIMAA
760 770 780 790 800
YPVTTLQSSA SPSRLLSLMD PLLPLSVLSK CVSAYSGTET EDHFDSDQKA
810 820 830 840 850
LGVMGLVQRD TSLFLRDLRL GASSWLNSFL ELSGRKPHKT PLPATETLRP
860 870 880 890 900
TDSGRLTESM RRSVSEAALA QPEGLLGTDS LKKLTIKDLS FKGNSEPSDS
910 920 930 940 950
PEMSQSMETL GPSTPSDVNF FLRSGNSQEE AETRDDISPM DGIPRVRAAF
960 970 980 990 1000
PDGFHPRRSS QGVLHMPLYS SPIVKNPFMS PLLAPDVMLK TLPPVHLVAC
1010 1020 1030 1040 1050
ALDPMLDDSV MFARRLKDLG QPVTLKVVED LPHGFLSLAA LCRETRQAAE
1060
LCVQRIRLIL TPPAAPLT
Length:1,068
Mass (Da):116,812
Last modified:January 24, 2006 - v3
Checksum:i13B10C9315AC87F1
GO
Isoform 2 (identifier: P15304-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-300: Missing.

Show »
Length:768
Mass (Da):84,170
Checksum:i90A1F0432DAC8B4C
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0171171 – 300Missing in isoform 2. 2 PublicationsAdd BLAST300

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51415 mRNA. Translation: CAA35777.1.
U40001 mRNA. Translation: AAC52771.1.
PIRiS03672. LIRTH.
RefSeqiNP_036991.1. NM_012859.1. [P15304-1]
XP_006228456.1. XM_006228394.3. [P15304-2]
UniGeneiRn.10566.

Genome annotation databases

GeneIDi25330.
KEGGirno:25330.
UCSCiRGD:3010. rat. [P15304-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51415 mRNA. Translation: CAA35777.1.
U40001 mRNA. Translation: AAC52771.1.
PIRiS03672. LIRTH.
RefSeqiNP_036991.1. NM_012859.1. [P15304-1]
XP_006228456.1. XM_006228394.3. [P15304-2]
UniGeneiRn.10566.

3D structure databases

ProteinModelPortaliP15304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247369. 2 interactors.
IntActiP15304. 1 interactor.
MINTiMINT-4783535.
STRINGi10116.ENSRNOP00000027911.

Chemistry databases

BindingDBiP15304.
ChEMBLiCHEMBL5582.
SwissLipidsiSLP:000000320.

Protein family/group databases

ESTHERiratno-hslip. Hormone-sensitive_lipase_like_1.
MEROPSiS09.993.

PTM databases

iPTMnetiP15304.
PhosphoSitePlusiP15304.

Proteomic databases

PaxDbiP15304.
PRIDEiP15304.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25330.
KEGGirno:25330.
UCSCiRGD:3010. rat. [P15304-1]

Organism-specific databases

CTDi3991.
RGDi3010. Lipe.

Phylogenomic databases

eggNOGiKOG4388. Eukaryota.
COG0657. LUCA.
HOGENOMiHOG000047722.
HOVERGENiHBG000187.
InParanoidiP15304.
KOiK07188.
PhylomeDBiP15304.

Enzyme and pathway databases

UniPathwayiUPA00256.
BRENDAi3.1.1.79. 5301.
ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

PROiP15304.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR010468. HSL_N.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
PF06350. HSL_N. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIPS_RAT
AccessioniPrimary (citable) accession number: P15304
Secondary accession number(s): Q6LCQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.