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Q9DBL9

- ABHD5_MOUSE

UniProt

Q9DBL9 - ABHD5_MOUSE

Protein

1-acylglycerol-3-phosphate O-acyltransferase ABHD5

Gene

Abhd5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2. Involved in keratinocyte differentiation.1 Publication

    Catalytic activityi

    Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

    GO - Molecular functioni

    1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. fatty acid metabolic process Source: UniProtKB-KW
    3. lipid metabolic process Source: MGI
    4. negative regulation of sequestering of triglyceride Source: UniProtKB
    5. phosphatidic acid biosynthetic process Source: UniProtKB
    6. positive regulation of lipoprotein lipase activity Source: MGI
    7. positive regulation of triglyceride catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Differentiation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Protein family/group databases

    MEROPSiS33.975.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (EC:2.3.1.51)
    Alternative name(s):
    Abhydrolase domain-containing protein 5
    Lipid droplet-binding protein CGI-58
    Short name:
    Protein CGI-58
    Gene namesi
    Name:Abhd5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1914719. Abhd5.

    Subcellular locationi

    Cytoplasm. Lipid droplet
    Note: Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. lipid particle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Lipid droplet

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3513511-acylglycerol-3-phosphate O-acyltransferase ABHD5PRO_0000080867Add
    BLAST

    Proteomic databases

    MaxQBiQ9DBL9.
    PaxDbiQ9DBL9.
    PRIDEiQ9DBL9.

    PTM databases

    PhosphoSiteiQ9DBL9.

    Expressioni

    Tissue specificityi

    Highly expressed in the adipose tissue and testes. Weakly expressed in the liver, muscle, kidney, and heart. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and hypothalamus in brain (at protein level).3 Publications

    Gene expression databases

    ArrayExpressiQ9DBL9.
    BgeeiQ9DBL9.
    CleanExiMM_ABHD5.
    GenevestigatoriQ9DBL9.

    Interactioni

    Subunit structurei

    Interacts with ADRP By similarity. Interacts with PLIN. Interacts with and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi212211. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBL9.
    SMRiQ9DBL9. Positions 72-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi329 – 3346HXXXXD motif

    Domaini

    The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0596.
    GeneTreeiENSGT00390000016277.
    HOVERGENiHBG054445.
    InParanoidiQ9DBL9.
    KOiK13699.
    OMAiERPIPIW.
    OrthoDBiEOG751NG1.
    PhylomeDBiQ9DBL9.
    TreeFamiTF314196.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PRINTSiPR00111. ABHYDROLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9DBL9-1) [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

    MKAMAAEEEV DSADAGGGSG WLTGWLPTWC PTSTSHLKEA EEKMLKCVPC    50
    TYKKEPVRIS NGNRIWTLMF SHNISSKTPL VLLHGFGGGL GLWALNFEDL 100
    STDRPVYAFD LLGFGRSSRP RFDSDAEEVE NQFVESIEEW RCALRLDKMI 150
    LLGHNLGGFL AAAYSLKYPS RVSHLILVEP WGFPERPDLA DQERPIPVWI 200
    RALGAALTPF NPLAGLRIAG PFGLSLVQRL RPDFKRKYSS MFEDDTVTEY 250
    IYHCNVQTPS GETAFKNMTI PYGWAKRPML QRIGGLHPDI PVSVIFGARS 300
    CIDGNSGTSI QSLRPKSYVK TIAILGAGHY VYADQPEEFN QKVKEICHTV 350
    D 351
    Length:351
    Mass (Da):39,155
    Last modified:June 1, 2001 - v1
    Checksum:i04068BFB77D33E67
    GO
    Isoform 2 (identifier: Q9DBL9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-171: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:198
    Mass (Da):21,846
    Checksum:i724796B08B1653D0
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei19 – 171153Missing in isoform 2. 1 PublicationVSP_015345Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004873 mRNA. Translation: BAB23632.1.
    AK019488 mRNA. Translation: BAB31755.2.
    AK050377 mRNA. Translation: BAC34220.1.
    BC037063 mRNA. Translation: AAH37063.1.
    CCDSiCCDS23646.1. [Q9DBL9-1]
    RefSeqiNP_080455.1. NM_026179.2. [Q9DBL9-1]
    XP_006512308.1. XM_006512245.1. [Q9DBL9-2]
    UniGeneiMm.280254.

    Genome annotation databases

    EnsembliENSMUST00000111497; ENSMUSP00000107123; ENSMUSG00000032540. [Q9DBL9-2]
    ENSMUST00000156520; ENSMUSP00000122274; ENSMUSG00000032540. [Q9DBL9-1]
    GeneIDi67469.
    KEGGimmu:67469.
    UCSCiuc009sew.1. mouse. [Q9DBL9-1]
    uc009sey.1. mouse. [Q9DBL9-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004873 mRNA. Translation: BAB23632.1 .
    AK019488 mRNA. Translation: BAB31755.2 .
    AK050377 mRNA. Translation: BAC34220.1 .
    BC037063 mRNA. Translation: AAH37063.1 .
    CCDSi CCDS23646.1. [Q9DBL9-1 ]
    RefSeqi NP_080455.1. NM_026179.2. [Q9DBL9-1 ]
    XP_006512308.1. XM_006512245.1. [Q9DBL9-2 ]
    UniGenei Mm.280254.

    3D structure databases

    ProteinModelPortali Q9DBL9.
    SMRi Q9DBL9. Positions 72-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212211. 4 interactions.

    Protein family/group databases

    MEROPSi S33.975.

    PTM databases

    PhosphoSitei Q9DBL9.

    Proteomic databases

    MaxQBi Q9DBL9.
    PaxDbi Q9DBL9.
    PRIDEi Q9DBL9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000111497 ; ENSMUSP00000107123 ; ENSMUSG00000032540 . [Q9DBL9-2 ]
    ENSMUST00000156520 ; ENSMUSP00000122274 ; ENSMUSG00000032540 . [Q9DBL9-1 ]
    GeneIDi 67469.
    KEGGi mmu:67469.
    UCSCi uc009sew.1. mouse. [Q9DBL9-1 ]
    uc009sey.1. mouse. [Q9DBL9-2 ]

    Organism-specific databases

    CTDi 51099.
    MGIi MGI:1914719. Abhd5.

    Phylogenomic databases

    eggNOGi COG0596.
    GeneTreei ENSGT00390000016277.
    HOVERGENi HBG054445.
    InParanoidi Q9DBL9.
    KOi K13699.
    OMAi ERPIPIW.
    OrthoDBi EOG751NG1.
    PhylomeDBi Q9DBL9.
    TreeFami TF314196.

    Miscellaneous databases

    ChiTaRSi ABHD5. mouse.
    NextBioi 324670.
    PROi Q9DBL9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DBL9.
    Bgeei Q9DBL9.
    CleanExi MM_ABHD5.
    Genevestigatori Q9DBL9.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view ]
    PRINTSi PR00111. ABHYDROLASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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: Liver.
    2. "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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Colon and Mammary gland.
    3. "Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes."
      Subramanian V., Rothenberg A., Gomez C., Cohen A.W., Garcia A., Bhattacharyya S., Shapiro L., Dolios G., Wang R., Lisanti M.P., Brasaemle D.L.
      J. Biol. Chem. 279:42062-42071(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "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, TISSUE SPECIFICITY, INTERACTION WITH PLIN AND PNPLA2.
    5. "CGI-58 is an alpha/beta-hydrolase within lipid transporting lamellar granules of differentiated keratinocytes."
      Akiyama M., Sakai K., Takayama C., Yanagi T., Yamanaka Y., McMillan J.R., Shimizu H.
      Am. J. Pathol. 173:1349-1360(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "CGI-58, the causative gene for Chanarin-Dorfman syndrome, mediates acylation of lysophosphatidic acid."
      Ghosh A.K., Ramakrishnan G., Chandramohan C., Rajasekharan R.
      J. Biol. Chem. 283:24525-24533(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    7. "Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation."
      Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z.
      J. Biol. Chem. 284:3049-3057(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLIN5.
    8. "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.

    Entry informationi

    Entry nameiABHD5_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBL9
    Secondary accession number(s): Q9CTY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 104 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. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3