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Protein

Hormone-sensitive lipase

Gene

LIPE

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

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 (By similarity).By similarity

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 sitei424PROSITE-ProRule annotation1
Active sitei691By similarity1
Active sitei721By similarity1

GO - Molecular functioni

  • hormone-sensitive lipase activity Source: UniProtKB-EC
  • lipase activity Source: InterPro
  • rRNA primary transcript binding Source: UniProtKB

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-KW
  • lipid catabolic process Source: UniProtKB
  • termination of RNA polymerase I transcription Source: UniProtKB
  • transcription initiation from RNA polymerase I promoter Source: UniProtKB
  • triglyceride catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

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

Enzyme and pathway databases

UniPathwayiUPA00256.

Protein family/group databases

ESTHERisussc-hslip. Hormone-sensitive_lipase_like_1.
MEROPSiS09.993.

Names & Taxonomyi

Protein namesi
Recommended name:
Hormone-sensitive lipase (EC:3.1.1.79)
Short name:
HSL
Gene namesi
Name:LIPE
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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: UniProtKB-SubCell
  • lipid particle Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000715491 – 764Hormone-sensitive lipaseAdd BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei552PhosphoserineBy similarity1
Modified residuei554Phosphoserine; by AMPKBy similarity1
Modified residuei593PhosphoserineBy similarity1
Modified residuei625PhosphoserineBy similarity1
Modified residuei647PhosphoserineBy similarity1
Modified residuei648PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ68J42.
PeptideAtlasiQ68J42.
PRIDEiQ68J42.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003269.

Structurei

3D structure databases

ProteinModelPortaliQ68J42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi350 – 352Involved 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.
InParanoidiQ68J42.
KOiK07188.

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]

Sequencei

Sequence statusi: Complete.

Q68J42-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLRTMTQSL VTLAEDNMAF FSGQGPGETA RRLSGVFAGI REQALGLEPA
60 70 80 90 100
LGRLLSVAHL FDLDAETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRRSI
110 120 130 140 150
FFRTSHNLAE LEAYLAALTQ LRALAYYAQR LLAINRPGKL FFEGDEGITA
160 170 180 190 200
DFLREYVTLH KGCFYGRCLG FQFTPAIRPF LQTISIGLVS FGEHYKRNET
210 220 230 240 250
GLSVTASSLF TSGRFAIDPE LRGAEFERII QNLDVHFWKA FWNITEIEVL
260 270 280 290 300
SSLANMASAT VRVSRLLSLP PKAFEMPLTA DPKLTVTISP PLAHTGPGPV
310 320 330 340 350
LVRLISYDLR EGQDSEELSS LVRSEGPRGL ELRPRPQQAP RSRSLVVHIH
360 370 380 390 400
GGGFVAQTSK SHEPYLKSWA QELGVPILSI DYSLAPEAPF PRALEECFYA
410 420 430 440 450
YCWAVKHCGL LGSTGERICL AGDSAGGNLC FTVSLRAAAY GVRVPDGIMA
460 470 480 490 500
AYPATMLQSA ASPSRLLSLM DPLLPLSVLS KCVSAYAGGE MEDHSDSDQK
510 520 530 540 550
ALGMMGLVRR DTALLFRDLR LGASSWLNSF LELSGHKSRP NLVPTEEPMR
560 570 580 590 600
RSVSEAALAQ PEGPLGTDSL KYLTLHDLSL SSETQDTPEL SLSAETLGPT
610 620 630 640 650
TPSAVNFLFR PEDAPEEAEA RDDISTKEEK VYSVRAAFPE GFHPRRSSQG
660 670 680 690 700
AIQMPLYSAP IVKNPFMSPL LAPDSMLQTL PPVHIVACAL DPMLDDSVMF
710 720 730 740 750
ARRLRSLGQP VTLHVVEDLP HGFLSLAALC RETRQAAALC VDRIRFILNP
760
PGPATPAGPT TPPV
Length:764
Mass (Da):83,450
Last modified:October 11, 2004 - v1
Checksum:i68A9BC0C7B401C03
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti129Q → H in strain: Norwegian Landrace. 1
Natural varianti148I → V in strain: Large white and Norwegian Landrace. 1
Natural varianti160H → R in strain: Large white. 1
Natural varianti296G → A in strain: Norwegian Landrace. 1
Natural varianti329G → S in strain: Norwegian Landrace. 1
Natural varianti623D → E in strain: Large white and Norwegian Landrace. 1
Natural varianti644P → S in strain: Large white. 1
Natural varianti705 – 706RS → Q in strain: Norwegian Landrace. 2
Natural varianti722G → R in strain: Norwegian Landrace. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY686758 mRNA. Translation: AAT95416.1.
AY686759 mRNA. Translation: AAT95417.1.
AJ000482 mRNA. Translation: CAA04121.1.
AJ000483, AJ006075, AJ006076 Genomic DNA. Translation: CAA04122.1.
RefSeqiNP_999480.1. NM_214315.1.
UniGeneiSsc.6784.
Ssc.96168.

Genome annotation databases

GeneIDi397583.
KEGGissc:397583.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY686758 mRNA. Translation: AAT95416.1.
AY686759 mRNA. Translation: AAT95417.1.
AJ000482 mRNA. Translation: CAA04121.1.
AJ000483, AJ006075, AJ006076 Genomic DNA. Translation: CAA04122.1.
RefSeqiNP_999480.1. NM_214315.1.
UniGeneiSsc.6784.
Ssc.96168.

3D structure databases

ProteinModelPortaliQ68J42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003269.

Protein family/group databases

ESTHERisussc-hslip. Hormone-sensitive_lipase_like_1.
MEROPSiS09.993.

Proteomic databases

PaxDbiQ68J42.
PeptideAtlasiQ68J42.
PRIDEiQ68J42.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397583.
KEGGissc:397583.

Organism-specific databases

CTDi3991.

Phylogenomic databases

eggNOGiKOG4388. Eukaryota.
COG0657. LUCA.
HOGENOMiHOG000047722.
HOVERGENiHBG000187.
InParanoidiQ68J42.
KOiK07188.

Enzyme and pathway databases

UniPathwayiUPA00256.

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_PIG
AccessioniPrimary (citable) accession number: Q68J42
Secondary accession number(s): Q68J43, Q9TUK0, Q9TUK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 11, 2004
Last modified: October 5, 2016
This is version 79 of the entry and version 1 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.