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Protein

Hormone-sensitive lipase

Gene

LIPE

Organism
Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus tridecemlineatus)
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei424 – 4241PROSITE-ProRule annotation
Active sitei692 – 6921By similarity
Active sitei722 – 7221By similarity

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

ESTHERispetr-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
OrganismiIctidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus tridecemlineatus)
Taxonomic identifieri43179 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiSciuridaeXerinaeMarmotiniIctidomys
Proteomesi
  • UP000005215 Componenti: Unassembled WGS sequence

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 763763Hormone-sensitive lipasePRO_0000071551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei552 – 5521PhosphoserineBy similarity
Modified residuei554 – 5541Phosphoserine; by AMPKBy similarity
Modified residuei595 – 5951PhosphoserineBy similarity
Modified residuei627 – 6271PhosphoserineBy similarity
Modified residuei649 – 6491PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi43179.ENSSTOP00000010392.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi350 – 3523Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Phylogenomic databases

eggNOGiKOG4388. Eukaryota.
COG0657. LUCA.
HOVERGENiHBG000187.
InParanoidiQ9R101.

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.

Q9R101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLRTMTQSL VTLAEDNMAF FSSQGPGETA RRLSNVFAGV REQALGLEPA
60 70 80 90 100
LGSLLSVAHL FDLDPETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRRSI
110 120 130 140 150
FFRTSHNLAE LEAYLAALTQ LRALAYYAQR LLATNRPGGL FFEGDEGLTA
160 170 180 190 200
DFLREYVTLH KGCFYGRCLG FQFTPSIRPF LQTISIGLVS FGEHYKRNES
210 220 230 240 250
GLGVTASSLF TSGRFAIDPE LRGAEFERIT QNLDVHFWKA FWNITEIEVL
260 270 280 290 300
SSLANMASAT VRVSRLISLP PEAFEMPLTS DPKLTVTISP PLAHTGPGPV
310 320 330 340 350
LIRLISYDLR EGQDSEELNS MVKSEGPRIL ELRPRPQQTS RSRSLVVXFH
360 370 380 390 400
GGGFVAQTSK SHEPYLKSWA QELGAPIISI DYSLAPEAPF PRALEECFFA
410 420 430 440 450
YCWAVKHCAL LGSTGERICL AGDSAGGNLC FTVALRAAAY GVRVPDGIMA
460 470 480 490 500
AYPATMLQSA ASPSRLLSLM DPLLPLSVLS KCVSAYAGAE TEEHPNSDEK
510 520 530 540 550
ALGMMGLVRR DTSLLLRDLR LGASSWLNSF LEFSGQKSQK TSAPTVESMR
560 570 580 590 600
RSVSEAALAQ PEGPVGTDSL KILTLKDLNL KSSSETSETP EMSLSVETLG
610 620 630 640 650
PSTPSDVNFF LRPEDAREEA EAKEGLSAKD GSSRVSNAFP EGFHPRRTSQ
660 670 680 690 700
GATQMPLYSS PIVKNPFMSP LLAPDNMLKT LPPVHIVACA LDPMLDDSXM
710 720 730 740 750
FARRLRALGQ PVTLRVVEDL PHGFLSLASL CRETRQAAEL CVERIRLILT
760
PPAAAAAAAP PPL
Length:763
Mass (Da):83,129
Last modified:May 1, 2000 - v1
Checksum:iE5516B02EFB8BE4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177401 mRNA. Translation: AAD51122.1.
RefSeqiNP_001269179.1. NM_001282250.1.

Genome annotation databases

GeneIDi101976389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177401 mRNA. Translation: AAD51122.1.
RefSeqiNP_001269179.1. NM_001282250.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi43179.ENSSTOP00000010392.

Protein family/group databases

ESTHERispetr-hslip. Hormone-sensitive_lipase_like_1.
MEROPSiS09.993.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101976389.

Organism-specific databases

CTDi3991.

Phylogenomic databases

eggNOGiKOG4388. Eukaryota.
COG0657. LUCA.
HOVERGENiHBG000187.
InParanoidiQ9R101.

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_ICTTR
AccessioniPrimary (citable) accession number: Q9R101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: May 1, 2000
Last modified: March 16, 2016
This is version 77 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.