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P15304

- LIPS_RAT

UniProt

P15304 - LIPS_RAT

Protein

Hormone-sensitive lipase

Gene

Lipe

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (24 Jan 2006)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei649 – 6491PROSITE-ProRule annotation
    Active sitei723 – 7231PROSITE-ProRule annotation

    GO - Molecular functioni

    1. acylglycerol lipase activity Source: RGD
    2. hormone-sensitive lipase activity Source: UniProtKB-EC
    3. hydrolase activity, acting on ester bonds Source: RGD
    4. protein binding Source: UniProtKB
    5. rRNA primary transcript binding Source: UniProtKB

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-KW
    2. female pregnancy Source: RGD
    3. lipid catabolic process Source: UniProtKB
    4. response to drug Source: RGD
    5. termination of RNA polymerase I transcription Source: UniProtKB
    6. transcription initiation from RNA polymerase I promoter Source: UniProtKB
    7. triglyceride catabolic process Source: RGD

    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

    MEROPSiS09.993.

    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
    ProteomesiUP000002494: 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

    1. caveola Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular space Source: RGD
    5. lipid particle Source: UniProtKB
    6. mitochondrion Source: UniProtKB
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi863 – 8631S → A or E: No effect on activation by PKA. 1 Publication
    Mutagenesisi865 – 8651S → A: Increases activation by PKA. 1 Publication
    Mutagenesisi865 – 8651S → E: No effect on activation by PKA. 1 Publication
    Mutagenesisi959 – 9591S → A: Slightly decreases activation by PKA. Abolishes activation by PKA; when associated with A-960. 1 Publication
    Mutagenesisi960 – 9601S → A: No effect on activation by PKA. Abolishes activation by PKA; when associated with A-959. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10681068Hormone-sensitive lipasePRO_0000071550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei863 – 8631Phosphoserine; by PKA2 Publications
    Modified residuei865 – 8651Phosphoserine; by AMPKBy similarity
    Modified residuei959 – 9591Phosphoserine; by PKA2 Publications
    Modified residuei960 – 9601Phosphoserine; by PKA2 Publications

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP15304.
    PRIDEiP15304.

    PTM databases

    PhosphoSiteiP15304.

    Expressioni

    Gene expression databases

    GenevestigatoriP15304.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi247369. 2 interactions.
    IntActiP15304. 1 interaction.
    MINTiMINT-4783535.

    Structurei

    3D structure databases

    ProteinModelPortaliP15304.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi649 – 6513Involved 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

    eggNOGiCOG0657.
    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_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. Align

    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

    MKPRRPISFT REITAMEPSS TSVSRPEWRP EAQQTLTDYP GSRELQEFGI     50
    PQKQSLPNEA TAQQGAEFQQ EQGVQQSTLL QKLLTPLAFP VPQQSFPSHK 100
    VHSDQQEATS QNGPGAGKVH TTQKELEHRD EHVGTAESGP AEPPPATEVE 150
    ATSIAQAVSG PDKKLPTQTD LVSQERAEQS DPTAQQTPLV QGVKSDQGSL 200
    IESGILARLQ KLAIQQPSQE WKTFLDCVTE SDMEKYLNSS SKSNPPEPSG 250
    GTVIPGTLPS KQKPDCGKMS GYGGKLPHGK KGILQKHKHY WDTASAFSHS 300
    MDLRTMTQSL VALAEDNMAF FSSQGPGETA RRLSNVFAGV REQALGLEPT 350
    LGQLLGVAHH FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRRSI 400
    FFRASHNLAE LEAYLAALTQ LRALAYYAQR LLTINRPGVL FFEGDEGLSA 450
    DFLQDYVTLH KGCFYGRCLG FQFTPAIRPF LQTLSIGLVS FGEHYKRNET 500
    GLSVTASSLF TGGRFAIDPE LRGAEFERII QNLDVHFWKA FWNITEIEVL 550
    SSLANMASTT VRVSRLLSLP PEAFEMPLTS DPKLTVTISP PLAHTGPGPV 600
    LARLISYDLR EGQDSKMLNS LAKSEGPRLE LRPRPQQAPR SRALVVHIHG 650
    GGFVAQTSKS HEPYLKNWAQ ELGVPIISID YSLAPEAPFP RALEECFFAY 700
    CWAVKHCELL GSTGERICLA GDSAGGNLCI TVSLRAAAYG VRVPDGIMAA 750
    YPVTTLQSSA SPSRLLSLMD PLLPLSVLSK CVSAYSGTET EDHFDSDQKA 800
    LGVMGLVQRD TSLFLRDLRL GASSWLNSFL ELSGRKPHKT PLPATETLRP 850
    TDSGRLTESM RRSVSEAALA QPEGLLGTDS LKKLTIKDLS FKGNSEPSDS 900
    PEMSQSMETL GPSTPSDVNF FLRSGNSQEE AETRDDISPM DGIPRVRAAF 950
    PDGFHPRRSS QGVLHMPLYS SPIVKNPFMS PLLAPDVMLK TLPPVHLVAC 1000
    ALDPMLDDSV MFARRLKDLG QPVTLKVVED LPHGFLSLAA LCRETRQAAE 1050
    LCVQRIRLIL TPPAAPLT 1068
    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)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 300300Missing in isoform 2. 2 PublicationsVSP_017117Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006228394.1. [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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51415 mRNA. Translation: CAA35777.1 .
    U40001 mRNA. Translation: AAC52771.1 .
    PIRi S03672. LIRTH.
    RefSeqi NP_036991.1. NM_012859.1. [P15304-1 ]
    XP_006228456.1. XM_006228394.1. [P15304-2 ]
    UniGenei Rn.10566.

    3D structure databases

    ProteinModelPortali P15304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247369. 2 interactions.
    IntActi P15304. 1 interaction.
    MINTi MINT-4783535.

    Chemistry

    BindingDBi P15304.
    ChEMBLi CHEMBL5582.

    Protein family/group databases

    MEROPSi S09.993.

    PTM databases

    PhosphoSitei P15304.

    Proteomic databases

    PaxDbi P15304.
    PRIDEi P15304.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25330.
    KEGGi rno:25330.
    UCSCi RGD:3010. rat. [P15304-1 ]

    Organism-specific databases

    CTDi 3991.
    RGDi 3010. Lipe.

    Phylogenomic databases

    eggNOGi COG0657.
    HOGENOMi HOG000047722.
    HOVERGENi HBG000187.
    InParanoidi P15304.
    KOi K07188.
    PhylomeDBi P15304.

    Enzyme and pathway databases

    UniPathwayi UPA00256 .

    Miscellaneous databases

    NextBioi 606207.
    PROi P15304.

    Gene expression databases

    Genevestigatori P15304.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR010468. HSL_N.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view ]
    Pfami PF07859. Abhydrolase_3. 2 hits.
    PF06350. HSL_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 2 hits.
    PROSITEi PS01173. LIPASE_GDXG_HIS. 1 hit.
    PS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of rat adipose hormone sensitive lipase cDNA."
      Holm C., Kirchgessner T.G., Svenson K.L., Lusis A.J., Belfrage P., Schotz M.C.
      Nucleic Acids Res. 16:9879-9879(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Adipose tissue.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Adipose tissue.
    3. Holm C.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 842-855 AND 1046-1068.
    4. "Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase."
      Holst L.S., Langin D., Mulder H., Laurell H., Grober J., Bergh A., Mohrenweiser H.W., Edgren G., Holm C.
      Genomics 35:441-447(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Sprague-Dawley.
      Tissue: Testis.
    5. "Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro."
      Anthonsen M.W., Roennstrand L., Wernstedt C., Degerman E., Holm C.
      J. Biol. Chem. 273:215-221(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-863; SER-959 AND SER-960, MUTAGENESIS OF SER-863; SER-865; SER-959 AND SER-960.
    6. "Skeletal muscle PLIN3 and PLIN5 are serine phosphorylated at rest and following lipolysis during adrenergic or contractile stimulation."
      Macpherson R.E., Vandenboom R., Roy B.D., Peters S.J.
      Physiol. Rep. 1:E00084-E00084(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIPE AND PNPLA2, PHOSPHORYLATION.

    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: October 1, 2014
    This is version 126 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

    External Data

    Dasty 3