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Q9VYS4 (GLD2B_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) RNA polymerase gld-2 homolog B

EC=2.7.7.19
Alternative name(s):
Protein wispy
Gene names
Name:wisp
ORF Names:CG15737
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1373 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.5 Ref.6

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1). Ref.5

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with orb, an RNA-binding protein, generating an ovarian cytoplasmic polyadenylation complex. Ref.5

Subcellular location

Cytoplasm Ref.3 Ref.6.

Tissue specificity

Expressed in ovaries. Not expressed in adult males. Ref.5

Developmental stage

Expressed both maternally and zygotically. Ref.3 Ref.6

Disruption phenotype

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. Ref.3 Ref.4 Ref.6

Sequence similarities

Belongs to the DNA polymerase type-B-like family. GLD2 subfamily.

Contains 1 PAP-associated domain.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA polyadenylation

Inferred from sequence or structural similarity. Source: UniProtKB

egg activation

Inferred from mutant phenotype Ref.4Ref.6. Source: FlyBase

intracellular mRNA localization

Inferred from mutant phenotype Ref.3. Source: FlyBase

mRNA polyadenylation

Inferred from mutant phenotype Ref.6Ref.5. Source: FlyBase

mitotic spindle organization

Inferred from mutant phenotype Ref.3. Source: FlyBase

oocyte maturation

Inferred from mutant phenotype Ref.6. Source: FlyBase

oogenesis

Inferred from mutant phenotype Ref.6Ref.5. Source: UniProtKB

pronuclear fusion

Inferred from mutant phenotype Ref.3. Source: FlyBase

pronuclear migration

Inferred from mutant phenotype Ref.3Ref.6. Source: FlyBase

regulation of antimicrobial peptide biosynthetic process

Inferred from mutant phenotype PubMed 20421637. Source: FlyBase

sperm aster formation

Inferred from mutant phenotype Ref.3. Source: FlyBase

spindle assembly involved in female meiosis

Inferred from mutant phenotype Ref.3. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

polynucleotide adenylyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13731373Poly(A) RNA polymerase gld-2 homolog B
PRO_0000341558

Regions

Domain1211 – 127262PAP-associated
Compositional bias31 – 377Poly-Gln
Compositional bias64 – 248185Asn-rich
Compositional bias130 – 15526Gln-rich
Compositional bias175 – 278104Ser-rich
Compositional bias318 – 492175Gln-rich
Compositional bias357 – 37418Ala-rich
Compositional bias674 – 6774Poly-Pro
Compositional bias691 – 6966Poly-Thr
Compositional bias710 – 7134Poly-Ala
Compositional bias735 – 7417Poly-Gln
Compositional bias755 – 7617Poly-Pro
Compositional bias830 – 8334Poly-Ser
Compositional bias912 – 9187Poly-Pro
Compositional bias1041 – 105414His-rich
Compositional bias1343 – 13486Poly-Gly

Sites

Metal binding10291Magnesium or manganese; catalytic By similarity
Metal binding10311Magnesium or manganese; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VYS4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 348EC66BF5239BAE

FASTA1,373151,312
        10         20         30         40         50         60 
MFSTRISGDM KIFAADVAES SVTATCNTSV QQQQSQQLEF RTRMSAGSPS SKSGQCHLKF 

        70         80         90        100        110        120 
GKYNNKTANL LRQVNSCHSS NSSSNTSNNN NEAIKGQQQQ PLHYCNSNNS HSWARKKYFG 

       130        140        150        160        170        180 
NGNSNNSLLQ QQQQPSSFFQ RQQQQHQMQM QQEKQATNNN DALMKNQNVV NAHVSDCKSS 

       190        200        210        220        230        240 
DSNNNSTSSS NNNSTISSNN NNTSSASNNN TGSSSSCSNR TKPAKWLNEN SSSSSSSNNN 

       250        260        270        280        290        300 
NISCRNNNTS SIDTKRRNSS AGATAAYYRK SESESGSSEG AAESTETEAT RTGGCNSNRT 

       310        320        330        340        350        360 
AESSSADGGT QATMGKSQDQ EQDQTVKQRP RQQPLSFWKT NYPQTSATQL KDKETVAAVV 

       370        380        390        400        410        420 
SAAAVAAAAA AASASEQQQQ QQSLSIEHRR NSGYQQHQQH NYYPYYYSQP KQLTIASFLQ 

       430        440        450        460        470        480 
KEMLPDSTEK SSSNTGGSNM IRSSSNGNSN FSRHQYGHQS TGSGYQQQQQ RYRNAQNVYQ 

       490        500        510        520        530        540 
QYQHQQQHHA QQHTHPHFRR KHSDNGSGIN KKMHYSPPGK SGDPADRSAS GQQQHHHPHQ 

       550        560        570        580        590        600 
QQKTIEILAS SHFNAMHRRM QGGNNKNGYY QHSYNPMTGE VGSTPTRSEH QNIYNLTYIH 

       610        620        630        640        650        660 
VDTEATGEAA SAAGSTPVVK PSLLSKPNIS ITPASSTTPT TVDRALLPAV RSVSAPASGS 

       670        680        690        700        710        720 
ALPAPANHVR NMFPPPPLAM LGGHGLLSPV TTTTPTKMIS CAQLDEAITA AAASGDKLST 

       730        740        750        760        770        780 
SPSYNQAGHY IMPPQQQQQQ QLSSHPIPTG TSSHPPPPPP PHMFFHFADG FCNPGQGHQA 

       790        800        810        820        830        840 
PPATMWPHSS SPCYPASYGS SCGSGTGAGT SPHNNDGNAG ALRPASPALS SSSLGSESQW 

       850        860        870        880        890        900 
SGTSNRSRLG HNGHPSISPT PSALGSAQLS PHLAEMRVQH PLHQQHPPSH ASHRPHGQMG 

       910        920        930        940        950        960 
GHAMSSYVPH RPPPPPHPSI SSPNPTPVAT GAGGPWYEMI LPPDRYLAQA RNIEVTVQPE 

       970        980        990       1000       1010       1020 
KLICMCKYDN LSAEIWKRFR GAQQTHNKFK LKMRLWRYLY LWMHQPMFER YRICLVGSTI 

      1030       1040       1050       1060       1070       1080 
TGFGTDSSDI DMCLLPEQGV HPHQHQYHQH HHFHNEKRTE ALIILTLFNA VLKDTEVFQD 

      1090       1100       1110       1120       1130       1140 
FNLIEARVPI LRFKDISNGI EVDLNFNNCV GIKNTYLLQL YAQMDWRTRP LVVIVKLWAQ 

      1150       1160       1170       1180       1190       1200 
YHDINDAKRM TISSYSLVLM VLHYLQHACV PHVLPCLHSL YPEKFQLGQQ DCLDLDLIEP 

      1210       1220       1230       1240       1250       1260 
IEPYQALNTQ TLGEHLLGFF KYYSTFDFRN FAISIRTGGV LPVSTCRMAK SPKNDVYQWK 

      1270       1280       1290       1300       1310       1320 
ELNIEEPFDL SNTARSVYDG PTFERVKAVF LISARRLDHT LDLATIFRPI HHVPEHFPQL 

      1330       1340       1350       1360       1370 
QQHQQQFEQQ LHHPISGQQR SAGGGGDGAN PVPSTLNPDA ASTFAETTAA HVA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAF48114.1.
RefSeqNP_572766.1. NM_132538.1.
UniGeneDm.6637.

3D structure databases

ProteinModelPortalQ9VYS4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58557. 18 interactions.
IntActQ9VYS4. 1 interaction.
MINTMINT-300598.
STRING7227.FBpp0073417.

Proteomic databases

PaxDbQ9VYS4.
PRIDEQ9VYS4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073573; FBpp0073417; FBgn0260780.
GeneID32152.
KEGGdme:Dmel_CG15737.
UCSCCG15737-RA. d. melanogaster.

Organism-specific databases

CTD32152.
FlyBaseFBgn0260780. wisp.

Phylogenomic databases

eggNOGCOG5260.
GeneTreeENSGT00550000074490.
InParanoidQ9VYS4.
KOK14079.
OMAYRICLVG.
OrthoDBEOG7DRJ2S.
PhylomeDBQ9VYS4.

Gene expression databases

BgeeQ9VYS4.

Family and domain databases

InterProIPR002058. PAP_assoc.
[Graphical view]
PfamPF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi32152.
NextBio777126.

Entry information

Entry nameGLD2B_DROME
AccessionPrimary (citable) accession number: Q9VYS4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase