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Q8BJ56

- PLPL2_MOUSE

UniProt

Q8BJ56 - PLPL2_MOUSE

Protein

Patatin-like phospholipase domain-containing protein 2

Gene

Pnpla2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion.6 Publications

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

    Enzyme regulationi

    Stimulated by PKA-dependent PLIN phosphorylation.3 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei47 – 471

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. triglyceride lipase activity Source: UniProtKB

    GO - Biological processi

    1. lipid particle organization Source: MGI
    2. lipid storage Source: UniProtKB
    3. negative regulation of sequestering of triglyceride Source: UniProtKB
    4. positive regulation of triglyceride catabolic process Source: UniProtKB
    5. triglyceride catabolic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_199036. Acyl chain remodeling of DAG and TAG.
    UniPathwayiUPA00256.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Patatin-like phospholipase domain-containing protein 2 (EC:3.1.1.3)
    Alternative name(s):
    Adipose triglyceride lipase
    Desnutrin
    Gene namesi
    Name:Pnpla2
    Synonyms:Atgl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1914103. Pnpla2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: MGI
    2. integral component of membrane Source: UniProtKB-KW
    3. lipid particle Source: UniProtKB
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Lipid droplet, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice show increased adipose mass and triacylglycerol deposition in multiple tissues. They accumulate large amounts of lipid in the heart, causing cardiac dysfunction and premature death.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471S → A: Loss of triacylglycerol hydrolysis activity. 1 Publication
    Mutagenesisi396 – 3961S → A: Slightly reduced TG hydrolase activity. 1 Publication
    Mutagenesisi406 – 4061S → A: Reduced TG hydrolase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Patatin-like phospholipase domain-containing protein 2PRO_0000292528Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
    Modified residuei374 – 3741Phosphoserine; in vitro2 Publications
    Modified residuei396 – 3961Phosphoserine; by PKA2 Publications
    Modified residuei406 – 4061Phosphoserine; by PKA2 Publications
    Modified residuei430 – 4301Phosphoserine; in vitro2 Publications
    Modified residuei468 – 4681Phosphoserine; in vitro2 Publications

    Post-translational modificationi

    Phosphorylation at Ser-406 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity.2 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ8BJ56.
    PaxDbiQ8BJ56.
    PRIDEiQ8BJ56.

    PTM databases

    PhosphoSiteiQ8BJ56.

    Expressioni

    Tissue specificityi

    Expressed at high levels in white and brown adipose tissue, and to a lesser degree in testis and cardiac muscle. Barely detected in liver, spleen, thymus, kidney, skeletal muscle, and brain. Among the white adipose depots, gonadal fat showed the highest level of expression compared with inguinal and renal white adipose tissues.4 Publications

    Developmental stagei

    Increased expression when preadipocytes are induced to differentiate to adipocytes. Not detected in proliferating or confluent preadipocytes.4 Publications

    Inductioni

    Transiently induced during fasting. cAMP and glucagon may not be involved in the induction during fasting. Induced by dexamethasone. Down-regulated by insulin, isoprotenerol and TNF-alfa. Expression is not affected by glucose and by growth hormone. Expression is reduced in fasted leptin deficient mouse (ob/ob), an obese mouse model. Expression is not affected in fed ob/ob mouse.5 Publications

    Gene expression databases

    ArrayExpressiQ8BJ56.
    BgeeiQ8BJ56.
    CleanExiMM_PNPLA2.
    GenevestigatoriQ8BJ56.

    Interactioni

    Subunit structurei

    Interacts with ABHD5; this association stimulates PNPLA2 triglyceride hydrolase activity. Interacts with SERPINF1; interacts at one site of interaction By similarity. Despite a colocalization in lipid droplets, it probably does not interact with PLIN. Interacts with PLIN5; prevents interaction with ABHD5.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi211763. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BJ56.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini30 – 486457LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 179170PatatinAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi45 – 495GXSXG

    Sequence similaritiesi

    Contains 1 patatin domain.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG261571.
    GeneTreeiENSGT00390000005295.
    HOVERGENiHBG007046.
    InParanoidiQ8BJ56.
    KOiK16816.
    OMAiLVLREMC.
    OrthoDBiEOG7J9VQR.
    PhylomeDBiQ8BJ56.
    TreeFamiTF314272.

    Family and domain databases

    InterProiIPR016035. Acyl_Trfase/lysoPLipase.
    IPR002641. Patatin/PLipase_A2-rel.
    [Graphical view]
    PfamiPF01734. Patatin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52151. SSF52151. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BJ56-1) [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

    MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA    50
    LTATALVTGA CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK 100
    TLPADCHERA NGRLGISLTR VSDGENVIIS HFSSKDELIQ ANVCSTFIPV 150
    YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN TITVSPFSGE SDICPQDSST 200
    NIHELRVTNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ GYRDGLRFLR 250
    RNGLLNQPNP LLALPPVVPQ EEDAEEAAVV EERAGEEDQL QPYRKDRILE 300
    HLPARLNEAL LEACVEPKDL MTTLSNMLPV RLATAMMVPY TLPLESAVSF 350
    TIRLLEWLPD VPEDIRWMKE QTGSICQYLV MRAKRKLGDH LPSRLSEQVE 400
    LRRAQSLPSV PLSCATYSEA LPNWVRNNLS LGDALAKWEE CQRQLLLGLF 450
    CTNVAFPPDA LRMRAPASPT AADPATPQDP PGLPPC 486
    Length:486
    Mass (Da):53,657
    Last modified:March 1, 2003 - v1
    Checksum:i512FE1931B72FC9C
    GO
    Isoform 2 (identifier: Q8BJ56-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         253-308: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:430
    Mass (Da):47,364
    Checksum:i16F03A3A9B559E6A
    GO
    Isoform 3 (identifier: Q8BJ56-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.
         57-62: VTGACL → MSHACQ

    Note: No experimental confirmation available.

    Show »
    Length:430
    Mass (Da):47,877
    Checksum:i1A66AF92E3D62A4F
    GO

    Sequence cautioni

    The sequence BAB22643.1 differs from that shown. Reason: Frameshift at positions 301, 317 and 460.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31P → T in BAB22387. (PubMed:16141072)Curated
    Sequence conflicti30 – 301R → H in AAU33824. (PubMed:15337759)Curated
    Sequence conflicti193 – 1931I → V in BAE29364. (PubMed:16141072)Curated
    Sequence conflicti319 – 3202DL → VG in BAB22643. (PubMed:16141072)Curated
    Sequence conflicti362 – 3621P → T in BAE29364. (PubMed:16141072)Curated
    Sequence conflicti385 – 3851R → G in AAC36536. (PubMed:9798653)Curated
    Sequence conflicti389 – 3891D → G in AAH64747. (PubMed:15489334)Curated
    Sequence conflicti412 – 4121L → P in AAC36536. (PubMed:9798653)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 3. 1 PublicationVSP_026422Add
    BLAST
    Alternative sequencei57 – 626VTGACL → MSHACQ in isoform 3. 1 PublicationVSP_026423
    Alternative sequencei253 – 30856Missing in isoform 2. 1 PublicationVSP_026424Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY731699 mRNA. Translation: AAU33824.1.
    AY894805 mRNA. Translation: AAW81963.1.
    AY510273 mRNA. Translation: AAS48458.1.
    AK002826 mRNA. Translation: BAB22387.1.
    AK003207 mRNA. Translation: BAB22643.1. Frameshift.
    AK031609 mRNA. Translation: BAC27476.1.
    AK150184 mRNA. Translation: BAE29364.1.
    BC019188 mRNA. Translation: AAH19188.1.
    BC044781 mRNA. Translation: AAH44781.1.
    BC064747 mRNA. Translation: AAH64747.1.
    U89431 mRNA. Translation: AAC36536.1.
    CCDSiCCDS22015.1. [Q8BJ56-2]
    CCDS52445.1. [Q8BJ56-1]
    RefSeqiNP_001157161.1. NM_001163689.1. [Q8BJ56-1]
    NP_080078.2. NM_025802.3. [Q8BJ56-2]
    UniGeneiMm.29998.

    Genome annotation databases

    EnsembliENSMUST00000064151; ENSMUSP00000065116; ENSMUSG00000025509. [Q8BJ56-2]
    ENSMUST00000164016; ENSMUSP00000127149; ENSMUSG00000025509. [Q8BJ56-1]
    GeneIDi66853.
    KEGGimmu:66853.
    UCSCiuc009klg.2. mouse. [Q8BJ56-2]
    uc009klh.2. mouse. [Q8BJ56-3]
    uc009kli.2. mouse. [Q8BJ56-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY731699 mRNA. Translation: AAU33824.1 .
    AY894805 mRNA. Translation: AAW81963.1 .
    AY510273 mRNA. Translation: AAS48458.1 .
    AK002826 mRNA. Translation: BAB22387.1 .
    AK003207 mRNA. Translation: BAB22643.1 . Frameshift.
    AK031609 mRNA. Translation: BAC27476.1 .
    AK150184 mRNA. Translation: BAE29364.1 .
    BC019188 mRNA. Translation: AAH19188.1 .
    BC044781 mRNA. Translation: AAH44781.1 .
    BC064747 mRNA. Translation: AAH64747.1 .
    U89431 mRNA. Translation: AAC36536.1 .
    CCDSi CCDS22015.1. [Q8BJ56-2 ]
    CCDS52445.1. [Q8BJ56-1 ]
    RefSeqi NP_001157161.1. NM_001163689.1. [Q8BJ56-1 ]
    NP_080078.2. NM_025802.3. [Q8BJ56-2 ]
    UniGenei Mm.29998.

    3D structure databases

    ProteinModelPortali Q8BJ56.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211763. 4 interactions.

    PTM databases

    PhosphoSitei Q8BJ56.

    Proteomic databases

    MaxQBi Q8BJ56.
    PaxDbi Q8BJ56.
    PRIDEi Q8BJ56.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064151 ; ENSMUSP00000065116 ; ENSMUSG00000025509 . [Q8BJ56-2 ]
    ENSMUST00000164016 ; ENSMUSP00000127149 ; ENSMUSG00000025509 . [Q8BJ56-1 ]
    GeneIDi 66853.
    KEGGi mmu:66853.
    UCSCi uc009klg.2. mouse. [Q8BJ56-2 ]
    uc009klh.2. mouse. [Q8BJ56-3 ]
    uc009kli.2. mouse. [Q8BJ56-1 ]

    Organism-specific databases

    CTDi 57104.
    MGIi MGI:1914103. Pnpla2.

    Phylogenomic databases

    eggNOGi NOG261571.
    GeneTreei ENSGT00390000005295.
    HOVERGENi HBG007046.
    InParanoidi Q8BJ56.
    KOi K16816.
    OMAi LVLREMC.
    OrthoDBi EOG7J9VQR.
    PhylomeDBi Q8BJ56.
    TreeFami TF314272.

    Enzyme and pathway databases

    UniPathwayi UPA00256 .
    Reactomei REACT_199036. Acyl chain remodeling of DAG and TAG.

    Miscellaneous databases

    ChiTaRSi PNPLA2. mouse.
    NextBioi 322819.
    PROi Q8BJ56.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BJ56.
    Bgeei Q8BJ56.
    CleanExi MM_PNPLA2.
    Genevestigatori Q8BJ56.

    Family and domain databases

    InterProi IPR016035. Acyl_Trfase/lysoPLipase.
    IPR002641. Patatin/PLipase_A2-rel.
    [Graphical view ]
    Pfami PF01734. Patatin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52151. SSF52151. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: ectopic expression of desnutrin increases triglyceride hydrolysis."
      Villena J.A., Roy S., Sarkadi-Nagy E., Kim K.-H., Sul H.S.
      J. Biol. Chem. 279:47066-47075(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: C57BL/6.
      Tissue: White adipose tissue.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
      Strain: C57BL/6.
    3. "The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated by insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for transactivation by PPARgamma."
      Kim J.Y., Tillison K., Lee J.-H., Rearick D.A., Smas C.M.
      Am. J. Physiol. 291:E115-E127(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: C57BL/6.
    4. "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: Bone marrow, Kidney and Testis.
    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] (ISOFORMS 1 AND 3).
      Strain: FVB/N.
      Tissue: Trophoblast stem cell.
    6. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
      Chu C.C., Paul W.E.
      Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-473.
      Strain: BALB/c.
      Tissue: Spleen.
    7. "Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members."
      Lake A.C., Sun Y., Li J.-L., Kim J.E., Johnson J.W., Li D., Revett T., Shih H.H., Liu W., Paulsen J.E., Gimeno R.E.
      J. Lipid Res. 46:2477-2487(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    8. "Isoproterenol, TNFalpha, and insulin downregulate adipose triglyceride lipase in 3T3-L1 adipocytes."
      Kralisch S., Klein J., Lossner U., Bluher M., Paschke R., Stumvoll M., Fasshauer M.
      Mol. Cell. Endocrinol. 240:43-49(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome."
      Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G., Schweiger M., Kienesberger P., Strauss J.G., Gorkiewicz G., Zechner R.
      Cell Metab. 3:309-319(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ABHD5, MUTAGENESIS OF SER-47.
    10. "Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin."
      Kershaw E.E., Hamm J.K., Verhagen L.A.W., Peroni O., Katic M., Flier J.S.
      Diabetes 55:148-157(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism."
      Schweiger M., Schreiber R., Haemmerle G., Lass A., Fledelius C., Jacobsen P., Tornqvist H., Zechner R., Zimmermann R.
      J. Biol. Chem. 281:40236-40241(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    12. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    13. "Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes."
      Miyoshi H., Perfield J.W. II, Souza S.C., Shen W.-J., Zhang H.-H., Stancheva Z.S., Kraemer F.B., Obin M.S., Greenberg A.S.
      J. Biol. Chem. 282:996-1002(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    14. "Analysis of lipolytic protein trafficking and interactions in adipocytes."
      Granneman J.G., Moore H.-P.H., Granneman R.L., Greenberg A.S., Obin M.S., Zhu Z.
      J. Biol. Chem. 282:5726-5735(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABHD5, LACK OF INTERACTION WITH PLIN.
    15. "Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase."
      Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z., Zhou L.
      J. Biol. Chem. 286:5126-5135(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLIN5, EXCLUSION OF INTERACTION WITH ABHD5.
    16. "Unique regulation of adipose triglyceride lipase (ATGL) by perilipin 5, a lipid droplet-associated protein."
      Wang H., Bell M., Sreenivasan U., Sreenevasan U., Hu H., Liu J., Dalen K., Londos C., Yamaguchi T., Rizzo M.A., Coleman R., Gong D., Brasaemle D., Sztalryd C.
      J. Biol. Chem. 286:15707-15715(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLIN5.
    17. "Identification and functional characterization of protein kinase A phosphorylation sites in the major lipolytic protein, adipose triglyceride lipase."
      Pagnon J., Matzaris M., Stark R., Meex R.C., Macaulay S.L., Brown W., O'Brien P.E., Tiganis T., Watt M.J.
      Endocrinology 153:4278-4289(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-374; SER-396; SER-406; SER-430 AND SER-468, MUTAGENESIS OF SER-396 AND SER-406.

    Entry informationi

    Entry nameiPLPL2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BJ56
    Secondary accession number(s): O89080
    , Q05BJ0, Q3UD97, Q643S0, Q6P234, Q9D1Q9, Q9DCF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 89 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. 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