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P54310 (LIPS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hormone-sensitive lipase

Short name=HSL
EC=3.1.1.79
Gene names
Name:Lipe
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

Diacylglycerol + H2O = monoacylglycerol + a carboxylate.

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Monoacylglycerol + H2O = glycerol + a carboxylate.

Enzyme regulation

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

Pathway

Glycerolipid metabolism; triacylglycerol degradation.

Subunit structure

Interacts with PTRF in the adipocyte cytoplasm By similarity.

Subcellular location

Cell membrane By similarity. Membranecaveola By similarity. Cytoplasmcytosol By similarity. Note: Found in the high-density caveolae By similarity. Translocates to the cytoplasm from the caveolae upon insulin stimulation By similarity.

Post-translational modification

Phosphorylation by AMPK may block translocation to lipid droplets.

Sequence similarities

Belongs to the 'GDXG' lipolytic enzyme family.

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid degradation
Lipid metabolism
Steroid metabolism
Sterol metabolism
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

diacylglycerol catabolic process

Inferred from direct assay PubMed 16804080. Source: MGI

lipid catabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

long-chain fatty acid catabolic process

Inferred from direct assay PubMed 16804080. Source: MGI

termination of RNA polymerase I transcription

Inferred from sequence or structural similarity PubMed 9582279. Source: UniProtKB

transcription initiation from RNA polymerase I promoter

Inferred from sequence or structural similarity PubMed 9582279. Source: UniProtKB

triglyceride catabolic process

Inferred from direct assay PubMed 16804080. Source: MGI

   Cellular_componentcaveola

Inferred from sequence or structural similarity PubMed 17026959. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity PubMed 17026959. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 16804080PubMed 17074755. Source: MGI

lipid particle

Inferred from direct assay Ref.6. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity PubMed 15242332. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity PubMed 15242332. Source: UniProtKB

   Molecular_functionhormone-sensitive lipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase binding

Inferred from physical interaction Ref.6. Source: UniProtKB

rRNA primary transcript binding

Inferred from sequence or structural similarity PubMed 9582279. Source: UniProtKB

triglyceride lipase activity

Inferred from mutant phenotype PubMed 17074755. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54310-1)

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.
Isoform 2 (identifier: P54310-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPAVESAPVGAQASKQGKEGSKNRSRRRWRKGKIKASAFSHSM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759Hormone-sensitive lipase
PRO_0000071548

Regions

Motif349 – 3513Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole By similarity

Sites

Active site3491 Potential
Active site4231 Potential

Amino acid modifications

Modified residue5571Phosphoserine By similarity
Modified residue5591Phosphoserine; by AMPK Probable
Modified residue6501Phosphoserine By similarity
Modified residue6511Phosphoserine By similarity

Natural variations

Alternative sequence11M → MEPAVESAPVGAQASKQGKE GSKNRSRRRWRKGKIKASAF SHSM in isoform 2.
VSP_053335

Experimental info

Sequence conflict1131A → T in BAE41414. Ref.3
Sequence conflict3111E → D in BAE41414. Ref.3
Sequence conflict330 – 3312EL → DV in AAC52163. Ref.1
Sequence conflict5301L → P in AAC52163. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 3419AF52F6C85FF4

FASTA75983,348
        10         20         30         40         50         60 
MDLRTMTQSL VTLAEDNMAF FSSQGPGETA RRLSNVFAGV REQALGLEPT LGQLLGVAHH 

        70         80         90        100        110        120 
FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRKSI FFRASHNLAE LEAYLAALTQ 

       130        140        150        160        170        180 
LRAMAYYAQR LLTINRPGVL FFEGDEGLTA DFLQEYVTLH KGCFYGRCLG FQFTPAIRPF 

       190        200        210        220        230        240 
LQTLSIGLVS FGEHYKRNET GLSVTASSLF TGGRFAIDPE LRGAEFERII QNLDVHFWKA 

       250        260        270        280        290        300 
FWNITEIEVL SSLANMASTT VRVSRLLSLP PEAFEMPLTS DPRLTVTISP PLAHTGPAPV 

       310        320        330        340        350        360 
LARLISYDLR EGQDSKVLNS LAKSEGPRLE LRPRPHQAPR SRALVVHIHG GGFVAQTSKS 

       370        380        390        400        410        420 
HEPYLKNWAQ ELGVPIFSID YSLAPEAPFP RALEECFFAY CWAVKHCDLL GSTGERICLA 

       430        440        450        460        470        480 
GDSAGGNLCI TVSLRAAAYG VRVPDGIMAA YPVTTLQSSA SPSRLLSLMD PLLPLSVLSK 

       490        500        510        520        530        540 
CVSAYSGTEA EDHFDSDQKA LGVMGLVQRD TSLFLRDLRL GASSWLNSFL ELSGRKPQKT 

       550        560        570        580        590        600 
TSPTAESVRP TESMRRSVSE AALAQPEGLL GTDTLKKLTI KDLSNSEPSD SPEMSQSMET 

       610        620        630        640        650        660 
LGPSTPSDVN FFLRPGNSQE EAEAKDEVRP MDGVPRVRAA FPEGFHPRRS SQGVLHMPLY 

       670        680        690        700        710        720 
TSPIVKNPFM SPLLAPDSML KTLPPVHLVA CALDPMLDDS VMFARRLRDL GQPVTLKVVE 

       730        740        750 
DLPHGFLSLA ALCRETRQAT EFCVQRIRLI LTPPAAPLN 

« Hide

Isoform 2 [UniParc].

Checksum: 3D0D4870E898AE5B
Show »

FASTA80288,027

References

« Hide 'large scale' references
[1]"Isolation and characterization of the gene for mouse hormone-sensitive lipase."
Li Z., Sumida M., Birchbauer A., Schotz M.C., Reue K.
Genomics 24:259-265(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Hormone-sensitive lipase (Lipe): sequence analysis of the 129Sv mouse Lipe gene."
Sztrolovics R., Wang S.P., Lapierre P., Chen H.S., Robert M.-F., Mitchell G.A.
Mamm. Genome 8:86-89(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Testis.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFOM 1).
Strain: FVB/N.
Tissue: Salivary gland.
[6]"Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes."
Daval M., Diot-Dupuy F., Bazin R., Hainault I., Viollet B., Vaulont S., Hajduch E., Ferre P., Foufelle F.
J. Biol. Chem. 280:25250-25257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY AMPK.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"The stoichiometry of protein phosphorylation in adipocyte lipid droplets: analysis by N-terminal isotope tagging and enzymatic dephosphorylation."
Kanshin E., Wang S., Ashmarina L., Fedjaev M., Nifant'ev I., Mitchell G.A., Pshezhetsky A.V.
Proteomics 9:5067-5077(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-559.
[9]"Ablation of TRIP-Br2, a regulator of fat lipolysis, thermogenesis and oxidative metabolism, prevents diet-induced obesity and insulin resistance."
Liew C.W., Boucher J., Cheong J.K., Vernochet C., Koh H.J., Mallol C., Townsend K., Langin D., Kawamori D., Hu J., Tseng Y.H., Hellerstein M.K., Farmer S.R., Goodyear L., Doria A., Blueher M., Hsu S.I., Kulkarni R.N.
Nat. Med. 19:217-226(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS LIPOLYTIC ENZYME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08188 mRNA. Translation: AAC52163.1.
AF179427 Genomic DNA. Translation: AAC53069.1.
AC162443 Genomic DNA. No translation available.
AC169209 Genomic DNA. No translation available.
AK029984 mRNA. Translation: BAC26716.1.
AK169858 mRNA. Translation: BAE41414.1.
BC021642 mRNA. Translation: AAH21642.1.
PIRI49007.
RefSeqNP_001034596.1. NM_001039507.2.
NP_034849.2. NM_010719.5.
XP_006539634.1. XM_006539571.1.
XP_006539635.1. XM_006539572.1.
UniGeneMm.158548.
Mm.333679.

3D structure databases

ProteinModelPortalP54310.
SMRP54310. Positions 337-524, 670-757.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL5935.

Protein family/group databases

MEROPSS09.993.

PTM databases

PhosphoSiteP54310.

Proteomic databases

PaxDbP54310.
PRIDEP54310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003207; ENSMUSP00000003207; ENSMUSG00000003123. [P54310-2]
ENSMUST00000054301; ENSMUSP00000050935; ENSMUSG00000003123. [P54310-1]
GeneID16890.
KEGGmmu:16890.
UCSCuc009fsp.1. mouse. [P54310-1]
uc009fsr.1. mouse.

Organism-specific databases

CTD3991.
MGIMGI:96790. Lipe.

Phylogenomic databases

eggNOGCOG0657.
GeneTreeENSGT00730000111056.
HOGENOMHOG000047722.
HOVERGENHBG000187.
InParanoidP54310.
KOK07188.
OrthoDBEOG7KSX7S.
TreeFamTF314423.

Enzyme and pathway databases

BRENDA3.1.1.79. 3474.
UniPathwayUPA00256.

Gene expression databases

ArrayExpressP54310.
BgeeP54310.
CleanExMM_LIPE.
GenevestigatorP54310.

Family and domain databases

InterProIPR013094. AB_hydrolase_3.
IPR010468. HSL_N.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamPF07859. Abhydrolase_3. 2 hits.
PF06350. HSL_N. 1 hit.
[Graphical view]
PROSITEPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio290908.
PROP54310.
SOURCESearch...

Entry information

Entry nameLIPS_MOUSE
AccessionPrimary (citable) accession number: P54310
Secondary accession number(s): P97866 expand/collapse secondary AC list , Q3TE34, Q6GU16, Q8CDI9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot