Q9VYS4 (GLD2B_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1373 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	mRNA processing
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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_component	cytoplasm Inferred from direct assay Ref.3Ref.6. Source: UniProtKB
Molecular_function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1373	1373	Poly(A) RNA polymerase gld-2 homolog B		PRO_0000341558
Regions
	Domain	1211 – 1272	62	PAP-associated
	Compositional bias	31 – 37	7	Poly-Gln
	Compositional bias	64 – 248	185	Asn-rich
	Compositional bias	130 – 155	26	Gln-rich
	Compositional bias	175 – 278	104	Ser-rich
	Compositional bias	318 – 492	175	Gln-rich
	Compositional bias	357 – 374	18	Ala-rich
	Compositional bias	674 – 677	4	Poly-Pro
	Compositional bias	691 – 696	6	Poly-Thr
	Compositional bias	710 – 713	4	Poly-Ala
	Compositional bias	735 – 741	7	Poly-Gln
	Compositional bias	755 – 761	7	Poly-Pro
	Compositional bias	830 – 833	4	Poly-Ser
	Compositional bias	912 – 918	7	Poly-Pro
	Compositional bias	1041 – 1054	14	His-rich
	Compositional bias	1343 – 1348	6	Poly-Gly
Sites
	Metal binding	1029	1	Magnesium or manganese; catalytic By similarity
	Metal binding	1031	1	Magnesium or manganese; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9VYS4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 348EC66BF5239BAE	FASTA	1,373	151,312
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
RefSeq	NP_572766.1. NM_132538.1.
UniGene	Dm.6637.
3D structure databases
ProteinModelPortal	Q9VYS4.
SMR	Q9VYS4. Positions 965-1298.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VYS4. 1 interaction.
MINT	MINT-300598.
STRING	7227.FBpp0073417.
Proteomic databases
PaxDb	Q9VYS4.
PRIDE	Q9VYS4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0073573; FBpp0073417; FBgn0260780.
GeneID	32152.
KEGG	dme:Dmel_CG15737.
UCSC	CG15737-RA. d. melanogaster.
Organism-specific databases
CTD	32152.
FlyBase	FBgn0260780. wisp.
Phylogenomic databases
eggNOG	COG5260.
GeneTree	ENSGT00550000074490.
InParanoid	Q9VYS4.
KO	K14079.
OMA	DSSDIDM.
OrthoDB	EOG4S7H5K.
PhylomeDB	Q9VYS4.
Gene expression databases
Bgee	Q9VYS4.
Family and domain databases
InterPro	IPR002058. PAP_assoc. [Graphical view]
Pfam	PF03828. PAP_assoc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	32152.
NextBio	777126.

Entry information

Entry name

GLD2B_DROME

Accession

Primary (citable) accession number: Q9VYS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project