SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9VYS4

- GLD2B_DROME

UniProt

Q9VYS4 - GLD2B_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Poly(A) RNA polymerase gld-2 homolog B
Gene
wisp, CG15737
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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; catalytic By similarity
Metal bindingi1031 – 10311Magnesium or manganese; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

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 B
PRO_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.

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 377Poly-Gln
Compositional biasi64 – 248185Asn-rich
Add
BLAST
Compositional biasi130 – 15526Gln-rich
Add
BLAST
Compositional biasi175 – 278104Ser-rich
Add
BLAST
Compositional biasi318 – 492175Gln-rich
Add
BLAST
Compositional biasi357 – 37418Ala-rich
Add
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-rich
Add
BLAST
Compositional biasi1343 – 13486Poly-Gly

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 85 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

Similar proteinsi