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P54310

- LIPS_MOUSE

UniProt

P54310 - LIPS_MOUSE

Protein

Hormone-sensitive lipase

Gene

Lipe

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (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.1 Publication

    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. Interacts with PLIN5.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei349 – 3491PROSITE-ProRule annotation
    Active sitei423 – 4231PROSITE-ProRule annotation

    GO - Molecular functioni

    1. hormone-sensitive lipase activity Source: UniProtKB-EC
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB
    4. rRNA primary transcript binding Source: UniProtKB
    5. triglyceride lipase activity Source: MGI

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-KW
    2. diacylglycerol catabolic process Source: MGI
    3. lipid catabolic process Source: UniProtKB
    4. long-chain fatty acid catabolic process Source: MGI
    5. termination of RNA polymerase I transcription Source: UniProtKB
    6. transcription initiation from RNA polymerase I promoter Source: UniProtKB
    7. triglyceride catabolic process Source: MGI

    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. 3474.
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:96790. 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: MGI
    4. lipid particle Source: UniProtKB
    5. mitochondrion Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 759759Hormone-sensitive lipasePRO_0000071548Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei557 – 5571PhosphoserineBy similarity
    Modified residuei559 – 5591Phosphoserine; by AMPK2 Publications
    Modified residuei650 – 6501PhosphoserineBy similarity
    Modified residuei651 – 6511PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by AMPK may block translocation to lipid droplets.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP54310.
    PaxDbiP54310.
    PRIDEiP54310.

    PTM databases

    PhosphoSiteiP54310.

    Expressioni

    Gene expression databases

    ArrayExpressiP54310.
    BgeeiP54310.
    CleanExiMM_LIPE.
    GenevestigatoriP54310.

    Interactioni

    Subunit structurei

    Interacts with PTRF in the adipocyte cytoplasm.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP54310.
    SMRiP54310. Positions 337-524.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi349 – 3513Involved 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.
    GeneTreeiENSGT00730000111056.
    HOGENOMiHOG000047722.
    HOVERGENiHBG000187.
    InParanoidiP54310.
    KOiK07188.
    OrthoDBiEOG7KSX7S.
    TreeFamiTF314423.

    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: P54310-1) [UniParc]FASTAAdd to Basket

    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

    MDLRTMTQSL VTLAEDNMAF FSSQGPGETA RRLSNVFAGV REQALGLEPT    50
    LGQLLGVAHH FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRKSI 100
    FFRASHNLAE LEAYLAALTQ LRAMAYYAQR LLTINRPGVL FFEGDEGLTA 150
    DFLQEYVTLH KGCFYGRCLG FQFTPAIRPF LQTLSIGLVS FGEHYKRNET 200
    GLSVTASSLF TGGRFAIDPE LRGAEFERII QNLDVHFWKA FWNITEIEVL 250
    SSLANMASTT VRVSRLLSLP PEAFEMPLTS DPRLTVTISP PLAHTGPAPV 300
    LARLISYDLR EGQDSKVLNS LAKSEGPRLE LRPRPHQAPR SRALVVHIHG 350
    GGFVAQTSKS HEPYLKNWAQ ELGVPIFSID YSLAPEAPFP RALEECFFAY 400
    CWAVKHCDLL GSTGERICLA GDSAGGNLCI TVSLRAAAYG VRVPDGIMAA 450
    YPVTTLQSSA SPSRLLSLMD PLLPLSVLSK CVSAYSGTEA EDHFDSDQKA 500
    LGVMGLVQRD TSLFLRDLRL GASSWLNSFL ELSGRKPQKT TSPTAESVRP 550
    TESMRRSVSE AALAQPEGLL GTDTLKKLTI KDLSNSEPSD SPEMSQSMET 600
    LGPSTPSDVN FFLRPGNSQE EAEAKDEVRP MDGVPRVRAA FPEGFHPRRS 650
    SQGVLHMPLY TSPIVKNPFM SPLLAPDSML KTLPPVHLVA CALDPMLDDS 700
    VMFARRLRDL GQPVTLKVVE DLPHGFLSLA ALCRETRQAT EFCVQRIRLI 750
    LTPPAAPLN 759
    Length:759
    Mass (Da):83,348
    Last modified:January 24, 2006 - v2
    Checksum:i3419AF52F6C85FF4
    GO
    Isoform 2 (identifier: P54310-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:802
    Mass (Da):88,027
    Checksum:i3D0D4870E898AE5B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1131A → T in BAE41414. (PubMed:16141072)Curated
    Sequence conflicti311 – 3111E → D in BAE41414. (PubMed:16141072)Curated
    Sequence conflicti330 – 3312EL → DV in AAC52163. (PubMed:7698747)Curated
    Sequence conflicti530 – 5301L → P in AAC52163. (PubMed:7698747)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MEPAVESAPVGAQASKQGKE GSKNRSRRRWRKGKIKASAF SHSM in isoform 2. 1 PublicationVSP_053335

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS20981.1. [P54310-2]
    CCDS20982.1. [P54310-1]
    PIRiI49007.
    RefSeqiNP_001034596.1. NM_001039507.2. [P54310-1]
    NP_034849.2. NM_010719.5. [P54310-2]
    XP_006539634.1. XM_006539571.1. [P54310-1]
    XP_006539635.1. XM_006539572.1. [P54310-1]
    UniGeneiMm.158548.
    Mm.333679.

    Genome annotation databases

    EnsembliENSMUST00000003207; ENSMUSP00000003207; ENSMUSG00000003123. [P54310-2]
    ENSMUST00000054301; ENSMUSP00000050935; ENSMUSG00000003123. [P54310-1]
    GeneIDi16890.
    KEGGimmu:16890.
    UCSCiuc009fsp.1. mouse. [P54310-1]
    uc009fsr.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS20981.1. [P54310-2 ]
    CCDS20982.1. [P54310-1 ]
    PIRi I49007.
    RefSeqi NP_001034596.1. NM_001039507.2. [P54310-1 ]
    NP_034849.2. NM_010719.5. [P54310-2 ]
    XP_006539634.1. XM_006539571.1. [P54310-1 ]
    XP_006539635.1. XM_006539572.1. [P54310-1 ]
    UniGenei Mm.158548.
    Mm.333679.

    3D structure databases

    ProteinModelPortali P54310.
    SMRi P54310. Positions 337-524.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL5935.

    Protein family/group databases

    MEROPSi S09.993.

    PTM databases

    PhosphoSitei P54310.

    Proteomic databases

    MaxQBi P54310.
    PaxDbi P54310.
    PRIDEi P54310.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003207 ; ENSMUSP00000003207 ; ENSMUSG00000003123 . [P54310-2 ]
    ENSMUST00000054301 ; ENSMUSP00000050935 ; ENSMUSG00000003123 . [P54310-1 ]
    GeneIDi 16890.
    KEGGi mmu:16890.
    UCSCi uc009fsp.1. mouse. [P54310-1 ]
    uc009fsr.1. mouse.

    Organism-specific databases

    CTDi 3991.
    MGIi MGI:96790. Lipe.

    Phylogenomic databases

    eggNOGi COG0657.
    GeneTreei ENSGT00730000111056.
    HOGENOMi HOG000047722.
    HOVERGENi HBG000187.
    InParanoidi P54310.
    KOi K07188.
    OrthoDBi EOG7KSX7S.
    TreeFami TF314423.

    Enzyme and pathway databases

    UniPathwayi UPA00256 .
    BRENDAi 3.1.1.79. 3474.

    Miscellaneous databases

    NextBioi 290908.
    PROi P54310.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54310.
    Bgeei P54310.
    CleanExi MM_LIPE.
    Genevestigatori P54310.

    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. "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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Activation of hormone-sensitive lipase requires two steps, protein phosphorylation and binding to the PAT-1 domain of lipid droplet coat proteins."
      Wang H., Hu L., Dalen K., Dorward H., Marcinkiewicz A., Russell D., Gong D., Londos C., Yamaguchi T., Holm C., Rizzo M.A., Brasaemle D., Sztalryd C.
      J. Biol. Chem. 284:32116-32125(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLIN5.
    9. "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.
    10. "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.

    Entry informationi

    Entry nameiLIPS_MOUSE
    AccessioniPrimary (citable) accession number: P54310
    Secondary accession number(s): P97866
    , Q3TE34, Q6GU16, Q8CDI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 125 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, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3