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Q9VYS4

- GLD2B_DROME

UniProt

Q9VYS4 - GLD2B_DROME

Protein

Poly(A) RNA polymerase gld-2 homolog B

Gene

wisp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific maternal RNAs (bcd, Tl, and tor), forming a poly(A) tail, during late oogenesis and early embryogenesis. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Required for localization of mRNAs to both poles of the egg, to recruit or maintain known centrosomal proteins with two types of microtubule organizing centers (MTOCs): the central MTOC that forms between the meiosis II tandem spindles and the centrosomes of the mitotic spindle. Required at the final stage of oogenesis for meiosis I metaphase arrest and for progression beyond this stage.4 Publications

    Catalytic activityi

    ATP + RNA(n) = diphosphate + RNA(n+1).1 Publication

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1029 – 10291Magnesium or manganese; catalyticBy similarity
    Metal bindingi1031 – 10311Magnesium or manganese; catalyticBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. polynucleotide adenylyltransferase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. egg activation Source: FlyBase
    2. intracellular mRNA localization Source: FlyBase
    3. mitotic spindle organization Source: FlyBase
    4. mRNA polyadenylation Source: FlyBase
    5. oocyte maturation Source: FlyBase
    6. oogenesis Source: UniProtKB
    7. pronuclear fusion Source: FlyBase
    8. pronuclear migration Source: FlyBase
    9. regulation of antimicrobial peptide biosynthetic process Source: FlyBase
    10. RNA polyadenylation Source: UniProtKB
    11. sperm aster formation Source: FlyBase
    12. spindle assembly involved in female meiosis Source: FlyBase

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(A) RNA polymerase gld-2 homolog B (EC:2.7.7.19)
    Alternative name(s):
    Protein wispy
    Gene namesi
    Name:wisp
    ORF Names:CG15737
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0260780. wisp.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Pronuclear migration does not occur in activated eggs. Defects in spindle structures (abnormally shaped spindles, spindle spurs, ectopic spindles associated with lost chromosomes and mispositioning of the meiosis II spindles) correlated with very high frequencies of chromosome non-disjunction and loss. The polar body nuclei do not associate with their normal monastral arrays of microtubules, the sperm aster is reduced in size, and the centrosomes often dissociate from a mitotic spindle that forms in association with the male pronucleus.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13731373Poly(A) RNA polymerase gld-2 homolog BPRO_0000341558Add
    BLAST

    Proteomic databases

    PaxDbiQ9VYS4.
    PRIDEiQ9VYS4.

    Expressioni

    Tissue specificityi

    Expressed in ovaries. Not expressed in adult males.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically.2 Publications

    Gene expression databases

    BgeeiQ9VYS4.

    Interactioni

    Subunit structurei

    Interacts with orb, an RNA-binding protein, generating an ovarian cytoplasmic polyadenylation complex.1 Publication

    Protein-protein interaction databases

    BioGridi58557. 18 interactions.
    IntActiQ9VYS4. 1 interaction.
    MINTiMINT-300598.
    STRINGi7227.FBpp0073417.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VYS4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1211 – 127262PAP-associatedAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi31 – 377Poly-Gln
    Compositional biasi64 – 248185Asn-richAdd
    BLAST
    Compositional biasi130 – 15526Gln-richAdd
    BLAST
    Compositional biasi175 – 278104Ser-richAdd
    BLAST
    Compositional biasi318 – 492175Gln-richAdd
    BLAST
    Compositional biasi357 – 37418Ala-richAdd
    BLAST
    Compositional biasi674 – 6774Poly-Pro
    Compositional biasi691 – 6966Poly-Thr
    Compositional biasi710 – 7134Poly-Ala
    Compositional biasi735 – 7417Poly-Gln
    Compositional biasi755 – 7617Poly-Pro
    Compositional biasi830 – 8334Poly-Ser
    Compositional biasi912 – 9187Poly-Pro
    Compositional biasi1041 – 105414His-richAdd
    BLAST
    Compositional biasi1343 – 13486Poly-Gly

    Sequence similaritiesi

    Contains 1 PAP-associated domain.Curated

    Phylogenomic databases

    eggNOGiCOG5260.
    GeneTreeiENSGT00550000074490.
    InParanoidiQ9VYS4.
    KOiK14079.
    OMAiYRICLVG.
    OrthoDBiEOG7DRJ2S.
    PhylomeDBiQ9VYS4.

    Family and domain databases

    InterProiIPR002058. PAP_assoc.
    [Graphical view]
    PfamiPF03828. PAP_assoc. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VYS4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSTRISGDM KIFAADVAES SVTATCNTSV QQQQSQQLEF RTRMSAGSPS     50
    SKSGQCHLKF GKYNNKTANL LRQVNSCHSS NSSSNTSNNN NEAIKGQQQQ 100
    PLHYCNSNNS HSWARKKYFG NGNSNNSLLQ QQQQPSSFFQ RQQQQHQMQM 150
    QQEKQATNNN DALMKNQNVV NAHVSDCKSS DSNNNSTSSS NNNSTISSNN 200
    NNTSSASNNN TGSSSSCSNR TKPAKWLNEN SSSSSSSNNN NISCRNNNTS 250
    SIDTKRRNSS AGATAAYYRK SESESGSSEG AAESTETEAT RTGGCNSNRT 300
    AESSSADGGT QATMGKSQDQ EQDQTVKQRP RQQPLSFWKT NYPQTSATQL 350
    KDKETVAAVV SAAAVAAAAA AASASEQQQQ QQSLSIEHRR NSGYQQHQQH 400
    NYYPYYYSQP KQLTIASFLQ KEMLPDSTEK SSSNTGGSNM IRSSSNGNSN 450
    FSRHQYGHQS TGSGYQQQQQ RYRNAQNVYQ QYQHQQQHHA QQHTHPHFRR 500
    KHSDNGSGIN KKMHYSPPGK SGDPADRSAS GQQQHHHPHQ QQKTIEILAS 550
    SHFNAMHRRM QGGNNKNGYY QHSYNPMTGE VGSTPTRSEH QNIYNLTYIH 600
    VDTEATGEAA SAAGSTPVVK PSLLSKPNIS ITPASSTTPT TVDRALLPAV 650
    RSVSAPASGS ALPAPANHVR NMFPPPPLAM LGGHGLLSPV TTTTPTKMIS 700
    CAQLDEAITA AAASGDKLST SPSYNQAGHY IMPPQQQQQQ QLSSHPIPTG 750
    TSSHPPPPPP PHMFFHFADG FCNPGQGHQA PPATMWPHSS SPCYPASYGS 800
    SCGSGTGAGT SPHNNDGNAG ALRPASPALS SSSLGSESQW SGTSNRSRLG 850
    HNGHPSISPT PSALGSAQLS PHLAEMRVQH PLHQQHPPSH ASHRPHGQMG 900
    GHAMSSYVPH RPPPPPHPSI SSPNPTPVAT GAGGPWYEMI LPPDRYLAQA 950
    RNIEVTVQPE KLICMCKYDN LSAEIWKRFR GAQQTHNKFK LKMRLWRYLY 1000
    LWMHQPMFER YRICLVGSTI TGFGTDSSDI DMCLLPEQGV HPHQHQYHQH 1050
    HHFHNEKRTE ALIILTLFNA VLKDTEVFQD FNLIEARVPI LRFKDISNGI 1100
    EVDLNFNNCV GIKNTYLLQL YAQMDWRTRP LVVIVKLWAQ YHDINDAKRM 1150
    TISSYSLVLM VLHYLQHACV PHVLPCLHSL YPEKFQLGQQ DCLDLDLIEP 1200
    IEPYQALNTQ TLGEHLLGFF KYYSTFDFRN FAISIRTGGV LPVSTCRMAK 1250
    SPKNDVYQWK ELNIEEPFDL SNTARSVYDG PTFERVKAVF LISARRLDHT 1300
    LDLATIFRPI HHVPEHFPQL QQHQQQFEQQ LHHPISGQQR SAGGGGDGAN 1350
    PVPSTLNPDA ASTFAETTAA HVA 1373
    Length:1,373
    Mass (Da):151,312
    Last modified:May 1, 2000 - v1
    Checksum:i348EC66BF5239BAE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF48114.1.
    RefSeqiNP_572766.1. NM_132538.1.
    UniGeneiDm.6637.

    Genome annotation databases

    EnsemblMetazoaiFBtr0073573; FBpp0073417; FBgn0260780.
    GeneIDi32152.
    KEGGidme:Dmel_CG15737.
    UCSCiCG15737-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF48114.1 .
    RefSeqi NP_572766.1. NM_132538.1.
    UniGenei Dm.6637.

    3D structure databases

    ProteinModelPortali Q9VYS4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58557. 18 interactions.
    IntActi Q9VYS4. 1 interaction.
    MINTi MINT-300598.
    STRINGi 7227.FBpp0073417.

    Proteomic databases

    PaxDbi Q9VYS4.
    PRIDEi Q9VYS4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0073573 ; FBpp0073417 ; FBgn0260780 .
    GeneIDi 32152.
    KEGGi dme:Dmel_CG15737.
    UCSCi CG15737-RA. d. melanogaster.

    Organism-specific databases

    CTDi 32152.
    FlyBasei FBgn0260780. wisp.

    Phylogenomic databases

    eggNOGi COG5260.
    GeneTreei ENSGT00550000074490.
    InParanoidi Q9VYS4.
    KOi K14079.
    OMAi YRICLVG.
    OrthoDBi EOG7DRJ2S.
    PhylomeDBi Q9VYS4.

    Miscellaneous databases

    GenomeRNAii 32152.
    NextBioi 777126.

    Gene expression databases

    Bgeei Q9VYS4.

    Family and domain databases

    InterProi IPR002058. PAP_assoc.
    [Graphical view ]
    Pfami PF03828. PAP_assoc. 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. "The Drosophila wispy gene is required for RNA localization and other microtubule-based events of meiosis and early embryogenesis."
      Brent A.E., MacQueen A., Hazelrigg T.
      Genetics 154:1649-1662(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    4. "Regulation of maternal transcript destabilization during egg activation in Drosophila."
      Tadros W., Houston S.A., Bashirullah A., Cooperstock R.L., Semotok J.L., Reed B.H., Lipshitz H.D.
      Genetics 164:989-1001(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    5. "PAP- and GLD-2-type poly(A) polymerases are required sequentially in cytoplasmic polyadenylation and oogenesis in Drosophila."
      Benoit P., Papin C., Kwak J.E., Wickens M., Simonelig M.
      Development 135:1969-1979(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ORB, TISSUE SPECIFICITY.
    6. "Wispy, the Drosophila homolog of GLD-2, is required during oogenesis and egg activation."
      Cui J., Sackton K.L., Horner V.L., Kumar K.E., Wolfner M.F.
      Genetics 178:2017-2029(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiGLD2B_DROME
    AccessioniPrimary (citable) accession number: Q9VYS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 86 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