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Protein

Poly(A) RNA polymerase gld-2 homolog B

Gene

wisp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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

Mg2+By similarity, Mn2+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

GO - Biological processi

  • egg activation Source: FlyBase
  • intracellular mRNA localization Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • mRNA polyadenylation Source: FlyBase
  • oocyte maturation Source: FlyBase
  • oogenesis Source: UniProtKB
  • pronuclear fusion Source: FlyBase
  • pronuclear migration Source: FlyBase
  • regulation of antimicrobial peptide biosynthetic process Source: FlyBase
  • RNA polyadenylation Source: UniProtKB
  • sperm aster formation Source: FlyBase
  • 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 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0260780. wisp.

Subcellular locationi

GO - Cellular componenti

  • 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 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.
OMAiMISCAQL.
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

        10         20         30         40         50
MFSTRISGDM KIFAADVAES SVTATCNTSV QQQQSQQLEF RTRMSAGSPS
60 70 80 90 100
SKSGQCHLKF GKYNNKTANL LRQVNSCHSS NSSSNTSNNN NEAIKGQQQQ
110 120 130 140 150
PLHYCNSNNS HSWARKKYFG NGNSNNSLLQ QQQQPSSFFQ RQQQQHQMQM
160 170 180 190 200
QQEKQATNNN DALMKNQNVV NAHVSDCKSS DSNNNSTSSS NNNSTISSNN
210 220 230 240 250
NNTSSASNNN TGSSSSCSNR TKPAKWLNEN SSSSSSSNNN NISCRNNNTS
260 270 280 290 300
SIDTKRRNSS AGATAAYYRK SESESGSSEG AAESTETEAT RTGGCNSNRT
310 320 330 340 350
AESSSADGGT QATMGKSQDQ EQDQTVKQRP RQQPLSFWKT NYPQTSATQL
360 370 380 390 400
KDKETVAAVV SAAAVAAAAA AASASEQQQQ QQSLSIEHRR NSGYQQHQQH
410 420 430 440 450
NYYPYYYSQP KQLTIASFLQ KEMLPDSTEK SSSNTGGSNM IRSSSNGNSN
460 470 480 490 500
FSRHQYGHQS TGSGYQQQQQ RYRNAQNVYQ QYQHQQQHHA QQHTHPHFRR
510 520 530 540 550
KHSDNGSGIN KKMHYSPPGK SGDPADRSAS GQQQHHHPHQ QQKTIEILAS
560 570 580 590 600
SHFNAMHRRM QGGNNKNGYY QHSYNPMTGE VGSTPTRSEH QNIYNLTYIH
610 620 630 640 650
VDTEATGEAA SAAGSTPVVK PSLLSKPNIS ITPASSTTPT TVDRALLPAV
660 670 680 690 700
RSVSAPASGS ALPAPANHVR NMFPPPPLAM LGGHGLLSPV TTTTPTKMIS
710 720 730 740 750
CAQLDEAITA AAASGDKLST SPSYNQAGHY IMPPQQQQQQ QLSSHPIPTG
760 770 780 790 800
TSSHPPPPPP PHMFFHFADG FCNPGQGHQA PPATMWPHSS SPCYPASYGS
810 820 830 840 850
SCGSGTGAGT SPHNNDGNAG ALRPASPALS SSSLGSESQW SGTSNRSRLG
860 870 880 890 900
HNGHPSISPT PSALGSAQLS PHLAEMRVQH PLHQQHPPSH ASHRPHGQMG
910 920 930 940 950
GHAMSSYVPH RPPPPPHPSI SSPNPTPVAT GAGGPWYEMI LPPDRYLAQA
960 970 980 990 1000
RNIEVTVQPE KLICMCKYDN LSAEIWKRFR GAQQTHNKFK LKMRLWRYLY
1010 1020 1030 1040 1050
LWMHQPMFER YRICLVGSTI TGFGTDSSDI DMCLLPEQGV HPHQHQYHQH
1060 1070 1080 1090 1100
HHFHNEKRTE ALIILTLFNA VLKDTEVFQD FNLIEARVPI LRFKDISNGI
1110 1120 1130 1140 1150
EVDLNFNNCV GIKNTYLLQL YAQMDWRTRP LVVIVKLWAQ YHDINDAKRM
1160 1170 1180 1190 1200
TISSYSLVLM VLHYLQHACV PHVLPCLHSL YPEKFQLGQQ DCLDLDLIEP
1210 1220 1230 1240 1250
IEPYQALNTQ TLGEHLLGFF KYYSTFDFRN FAISIRTGGV LPVSTCRMAK
1260 1270 1280 1290 1300
SPKNDVYQWK ELNIEEPFDL SNTARSVYDG PTFERVKAVF LISARRLDHT
1310 1320 1330 1340 1350
LDLATIFRPI HHVPEHFPQL QQHQQQFEQQ LHHPISGQQR SAGGGGDGAN
1360 1370
PVPSTLNPDA ASTFAETTAA HVA
Length:1,373
Mass (Da):151,312
Last modified:May 1, 2000 - v1
Checksum:i348EC66BF5239BAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF48114.1.
RefSeqiNP_001285144.1. NM_001298215.1.
NP_572766.1. NM_132538.2.
UniGeneiDm.6637.

Genome annotation databases

EnsemblMetazoaiFBtr0073573; FBpp0073417; FBgn0260780.
FBtr0342743; FBpp0309611; FBgn0260780.
GeneIDi32152.
KEGGidme:Dmel_CG15737.
UCSCiCG15737-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF48114.1.
RefSeqiNP_001285144.1. NM_001298215.1.
NP_572766.1. NM_132538.2.
UniGeneiDm.6637.

3D structure databases

ProteinModelPortaliQ9VYS4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiQ9VYS4.
PRIDEiQ9VYS4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073573; FBpp0073417; FBgn0260780.
FBtr0342743; FBpp0309611; FBgn0260780.
GeneIDi32152.
KEGGidme:Dmel_CG15737.
UCSCiCG15737-RA. d. melanogaster.

Organism-specific databases

CTDi32152.
FlyBaseiFBgn0260780. wisp.

Phylogenomic databases

eggNOGiCOG5260.
GeneTreeiENSGT00550000074490.
InParanoidiQ9VYS4.
KOiK14079.
OMAiMISCAQL.
OrthoDBiEOG7DRJ2S.
PhylomeDBiQ9VYS4.

Miscellaneous databases

GenomeRNAii32152.
NextBioi777126.
PROiQ9VYS4.

Gene expression databases

BgeeiQ9VYS4.

Family and domain databases

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

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: April 29, 2015
This is version 92 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.