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Q9VRG7

- CNEP1_DROME

UniProt

Q9VRG7 - CNEP1_DROME

Protein

CTD nuclear envelope phosphatase 1 homolog

Gene

Dd

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Serine/threonine protein phosphatase that may dephosphorylate and activate lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol By similarity.By similarity

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    GO - Molecular functioni

    1. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. imaginal disc-derived wing vein specification Source: FlyBase
    2. negative regulation of BMP signaling pathway Source: FlyBase
    3. nuclear envelope organization Source: UniProtKB
    4. positive regulation of triglyceride biosynthetic process Source: UniProtKB
    5. protein dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_219169. Depolymerisation of the Nuclear Lamina.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTD nuclear envelope phosphatase 1 homolog (EC:3.1.3.16)
    Alternative name(s):
    Serine/threonine-protein phosphatase dullard homolog
    Gene namesi
    Name:Dd
    Synonyms:l(1)G0269
    ORF Names:CG1696
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0029067. Dd.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. Nem1-Spo7 phosphatase complex Source: UniProtKB
    5. nuclear envelope Source: UniProtKB
    6. nuclear membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 243243CTD nuclear envelope phosphatase 1 homologPRO_0000297976Add
    BLAST

    Proteomic databases

    PaxDbiQ9VRG7.
    PRIDEiQ9VRG7.

    Expressioni

    Gene expression databases

    BgeeiQ9VRG7.

    Interactioni

    Protein-protein interaction databases

    BioGridi59385. 7 interactions.
    MINTiMINT-899760.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VRG7.
    SMRiQ9VRG7. Positions 60-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 2717HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 223168FCP1 homologyPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the dullard family.Curated
    Contains 1 FCP1 homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5190.
    GeneTreeiENSGT00550000075053.
    HOGENOMiHOG000002447.
    InParanoidiQ9VRG7.
    KOiK17617.
    OMAiLLGIRTF.
    OrthoDBiEOG7MKW6W.
    PhylomeDBiQ9VRG7.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR011948. Dullard_phosphatase.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view]
    PfamiPF03031. NIF. 1 hit.
    [Graphical view]
    SMARTiSM00577. CPDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02251. HIF-SF_euk. 1 hit.
    PROSITEiPS50969. FCP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VRG7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MISLLQMKFR ALLLLLSKVW TCICFMFNRQ VRAFIQYQPV KYELFPLSPV    50
    SRHRLSLVQR KTLVLDLDET LIHSHHNAMP RNTVKPGTPH DFTVKVTIDR 100
    NPVRFFVHKR PHVDYFLDVV SQWYDLVVFT ASMEIYGAAV ADKLDNGRNI 150
    LRRRYYRQHC TPDYGSYTKD LSAICSDLNR IFIIDNSPGA YRCFPNNAIP 200
    IKSWFSDPMD TALLSLLPML DALRFTNDVR SVLSRNLHLH RLW 243
    Length:243
    Mass (Da):28,486
    Last modified:May 1, 2000 - v1
    Checksum:i1E278DD1D8DF60C6
    GO

    Sequence cautioni

    The sequence AAM48350.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF50833.1.
    AY094776 mRNA. Translation: AAM11129.1.
    AY118321 mRNA. Translation: AAM48350.1. Different initiation.
    RefSeqiNP_608449.1. NM_134605.2.
    UniGeneiDm.7059.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077226; FBpp0076921; FBgn0029067.
    GeneIDi33107.
    KEGGidme:Dmel_CG1696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF50833.1 .
    AY094776 mRNA. Translation: AAM11129.1 .
    AY118321 mRNA. Translation: AAM48350.1 . Different initiation.
    RefSeqi NP_608449.1. NM_134605.2.
    UniGenei Dm.7059.

    3D structure databases

    ProteinModelPortali Q9VRG7.
    SMRi Q9VRG7. Positions 60-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59385. 7 interactions.
    MINTi MINT-899760.

    Proteomic databases

    PaxDbi Q9VRG7.
    PRIDEi Q9VRG7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077226 ; FBpp0076921 ; FBgn0029067 .
    GeneIDi 33107.
    KEGGi dme:Dmel_CG1696.

    Organism-specific databases

    CTDi 33107.
    FlyBasei FBgn0029067. Dd.

    Phylogenomic databases

    eggNOGi COG5190.
    GeneTreei ENSGT00550000075053.
    HOGENOMi HOG000002447.
    InParanoidi Q9VRG7.
    KOi K17617.
    OMAi LLGIRTF.
    OrthoDBi EOG7MKW6W.
    PhylomeDBi Q9VRG7.

    Enzyme and pathway databases

    Reactomei REACT_219169. Depolymerisation of the Nuclear Lamina.

    Miscellaneous databases

    GenomeRNAii 33107.
    NextBioi 781938.
    PROi Q9VRG7.

    Gene expression databases

    Bgeei Q9VRG7.

    Family and domain databases

    Gene3Di 3.40.50.1000. 1 hit.
    InterProi IPR011948. Dullard_phosphatase.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view ]
    Pfami PF03031. NIF. 1 hit.
    [Graphical view ]
    SMARTi SM00577. CPDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02251. HIF-SF_euk. 1 hit.
    PROSITEi PS50969. FCP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiCNEP1_DROME
    AccessioniPrimary (citable) accession number: Q9VRG7
    Secondary accession number(s): Q8MT79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3