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Protein

Hormone-sensitive lipase

Gene

LIPE

Organism
Bos taurus (Bovine)
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)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

BRENDAi3.1.1.79. 908.
UniPathwayiUPA00256.

Protein family/group databases

ESTHERibovin-hslip. Hormone-sensitive_lipase_like_1.

Names & Taxonomyi

Protein namesi
Recommended name:
Hormone-sensitive lipase (EC:3.1.1.79)
Short name:
HSL
Gene namesi
Name:LIPE
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 756756Hormone-sensitive lipasePRO_0000071546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei552 – 5521Phosphoserine; by PKA1 Publication
Modified residuei554 – 5541Phosphoserine; by AMPK2 Publications
Modified residuei595 – 5951PhosphoserineBy similarity
Modified residuei649 – 6491PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP16386.
PRIDEiP16386.

PTM databases

iPTMnetiP16386.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000041426.

Structurei

3D structure databases

ProteinModelPortaliP16386.
ModBaseiSearch...
MobiDBiSearch...

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.
HOGENOMiHOG000047722.
HOVERGENiHBG000187.
InParanoidiP16386.
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.

P16386-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLRTMTQSL VTLAEDNMAF FSSQGPGETA RRLTGVFAGI REQALGLEPA
60 70 80 90 100
LGRLLSVAHL FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRRSI
110 120 130 140 150
FFRTSHNLAE LEAYLAALTQ LRALAYYAQR LLTTNQPGRL FFEGDERVIA
160 170 180 190 200
DFLREYVTLH KGCFYGRCLG FQFTPAIRPF LQTISIGLVS FGEHYKRNET
210 220 230 240 250
GISVTASSLF TDGRFAIDPE LRGAEFERII QNLDVHFWKA FWNITEIQVL
260 270 280 290 300
SSLANMASTT VRVSRLLSLP PVAFEMPLTS DPELTVTISP PLAHTGPGPV
310 320 330 340 350
LVRLISYDLR EGQDSKELSS FVRSEGPRSL ELRLRPQQAP RSRALVVHIH
360 370 380 390 400
GGGFVAQTSK SHEPYLKSWA QELGAPILSI DYSLAPEAPF PRALEECFYA
410 420 430 440 450
YCWAVKHCAL LGSTGERICL AGDSAGGNLC FTVSLRAAAY GVRVPDGIMA
460 470 480 490 500
AYPATMLQST ASPSRLLSLM DHLLPLSVLS KCVSTYAGAE TEDHPDSDQK
510 520 530 540 550
ALGVMGLVQR DTALLLRDLR LGASSWLNSF LELGGQKSHL KSVSKTEPMR
560 570 580 590 600
RSVSEAALTQ PEGSLGTDSL KSLKLHDLGL RNSSDTTDTP ELSLSAETLG
610 620 630 640 650
PSAPSTINFL LGSEDGSEMS KAPEELNNKD RVRGVGAAFP EGFHPRRCSQ
660 670 680 690 700
GAMWMPLYSA PIVKNPSMSP LLAPDSMLQT LPPVHIVACA LDPMLDDSVM
710 720 730 740 750
FARRLRGLGQ PVTLRVAEDL PHGFLSLAAL CRETRQAAAL CVERIRLILN

LPGPPV
Length:756
Mass (Da):82,641
Last modified:February 5, 2008 - v2
Checksum:i7E3AACB65DDD68FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121T → S in ABL84202 (Ref. 1) Curated
Sequence conflicti87 – 871L → P in ABL84202 (Ref. 1) Curated
Sequence conflicti564 – 5641S → P AA sequence (PubMed:3345839).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF140760 mRNA. Translation: ABL84202.1.
AY986820 Genomic DNA. Translation: AAX82971.1.
DQ523227 Genomic DNA. Translation: ABG54259.1.
PIRiS00347.
RefSeqiNP_001073689.1. NM_001080220.1.
UniGeneiBt.28410.

Genome annotation databases

GeneIDi286879.
KEGGibta:286879.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF140760 mRNA. Translation: ABL84202.1.
AY986820 Genomic DNA. Translation: AAX82971.1.
DQ523227 Genomic DNA. Translation: ABG54259.1.
PIRiS00347.
RefSeqiNP_001073689.1. NM_001080220.1.
UniGeneiBt.28410.

3D structure databases

ProteinModelPortaliP16386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000041426.

Protein family/group databases

ESTHERibovin-hslip. Hormone-sensitive_lipase_like_1.

PTM databases

iPTMnetiP16386.

Proteomic databases

PaxDbiP16386.
PRIDEiP16386.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286879.
KEGGibta:286879.

Organism-specific databases

CTDi3991.

Phylogenomic databases

eggNOGiKOG4388. Eukaryota.
COG0657. LUCA.
HOGENOMiHOG000047722.
HOVERGENiHBG000187.
InParanoidiP16386.
KOiK07188.

Enzyme and pathway databases

UniPathwayiUPA00256.
BRENDAi3.1.1.79. 908.

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...

Publicationsi

  1. "cDNA cloning of bovine LIPE gene."
    Guo Y.Q., Xu S.Z., Gao X., Zhang L.P.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "HSL Gene Sequence and Phylogenetic Evolution of Bovinae (Bos taurus, Bos grunniens, Bubalus bubalis, and Bos frontalis)."
    Ma Z.-J., Zhong J.-C., Guan W.-X., Zhao S., He K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-169.
    Tissue: Blood.
  3. "Sequencing of hormone-sensitive lipase (LIPE) gene in Korean cattle."
    Chung E.R., Shin S.C., Park J.G., Gwon S.Y.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-169.
    Strain: Korean.
  4. "Primary structure of the site on bovine hormone-sensitive lipase phosphorylated by cyclic AMP-dependent protein kinase."
    Garton A.J., Campbell D.G., Cohen P., Yeaman S.J.
    FEBS Lett. 229:68-72(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 545-571, PHOSPHORYLATION AT SER-552 AND SER-554.
  5. "Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism."
    Garton A.J., Campbell D.G., Carling D., Hardie D.G., Colbran R.J., Yeaman S.J.
    Eur. J. Biochem. 179:249-254(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 552-556, PHOSPHORYLATION AT SER-554.
    Tissue: Adipose tissue.

Entry informationi

Entry nameiLIPS_BOVIN
AccessioniPrimary (citable) accession number: P16386
Secondary accession number(s): A1YWA8, Q562H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.