ID GLD2B_DROME Reviewed; 1373 AA. AC Q9VYS4; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Poly(A) RNA polymerase gld-2 homolog B; DE EC=2.7.7.19; DE AltName: Full=Protein wispy; GN Name=wisp; ORFNames=CG15737; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION RP PHENOTYPE. RX PubMed=10747060; DOI=10.1093/genetics/154.4.1649; RA Brent A.E., MacQueen A., Hazelrigg T.; RT "The Drosophila wispy gene is required for RNA localization and other RT microtubule-based events of meiosis and early embryogenesis."; RL Genetics 154:1649-1662(2000). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12871909; DOI=10.1093/genetics/164.3.989; RA Tadros W., Houston S.A., Bashirullah A., Cooperstock R.L., Semotok J.L., RA Reed B.H., Lipshitz H.D.; RT "Regulation of maternal transcript destabilization during egg activation in RT Drosophila."; RL Genetics 164:989-1001(2003). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ORB, AND TISSUE SPECIFICITY. RX PubMed=18434412; DOI=10.1242/dev.021444; RA Benoit P., Papin C., Kwak J.E., Wickens M., Simonelig M.; RT "PAP- and GLD-2-type poly(A) polymerases are required sequentially in RT cytoplasmic polyadenylation and oogenesis in Drosophila."; RL Development 135:1969-1979(2008). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION RP PHENOTYPE. RX PubMed=18430932; DOI=10.1534/genetics.107.084558; RA Cui J., Sackton K.L., Horner V.L., Kumar K.E., Wolfner M.F.; RT "Wispy, the Drosophila homolog of GLD-2, is required during oogenesis and RT egg activation."; RL Genetics 178:2017-2029(2008). RN [7] RP FUNCTION, INTERACTION WITH DCR-2, DEVELOPMENTAL STAGE, AND REGION. RX PubMed=29317541; DOI=10.1261/rna.065417.117; RA Coll O., Guitart T., Villalba A., Papin C., Simonelig M., Gebauer F.; RT "Dicer-2 promotes mRNA activation through cytoplasmic polyadenylation."; RL RNA 24:529-539(2018). CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP CC monomers to the 3'-end of specific maternal RNAs (bcd, Tl, and tor), CC forming a poly(A) tail, during late oogenesis and early embryogenesis CC (PubMed:29317541, PubMed:18434412, PubMed:18430932). In contrast to the CC canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to CC selected cytoplasmic mRNAs (PubMed:18434412, PubMed:18430932). Required CC for localization of mRNAs to both poles of the egg, to recruit or CC maintain known centrosomal proteins with two types of microtubule CC organizing centers (MTOCs): the central MTOC that forms between the CC meiosis II tandem spindles and the centrosomes of the mitotic spindle CC (PubMed:10747060). Required at the final stage of oogenesis for meiosis CC I metaphase arrest and for progression beyond this stage CC (PubMed:10747060, PubMed:12871909, PubMed:18434412). Functions with the CC RNA-binding protein Dcr-2 to promote cytoplasmic polyadenylation and CC translational activation of certain mRNAs such as Tl and r2d2 CC (PubMed:29317541). As a consequence, is involved in regulating Toll CC immune signaling and promoting resistance to fungal infection CC (PubMed:29317541). {ECO:0000269|PubMed:10747060, CC ECO:0000269|PubMed:12871909, ECO:0000269|PubMed:18430932, CC ECO:0000269|PubMed:18434412, ECO:0000269|PubMed:29317541}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, CC ChEBI:CHEBI:173115; EC=2.7.7.19; CC Evidence={ECO:0000269|PubMed:18434412}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with orb, an RNA-binding protein, generating an CC ovarian cytoplasmic polyadenylation complex (PubMed:18434412). CC Interacts (via C-terminus) with Dcr-2 (PubMed:29317541). CC {ECO:0000269|PubMed:18434412, ECO:0000269|PubMed:29317541}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10747060, CC ECO:0000269|PubMed:18430932}. CC -!- TISSUE SPECIFICITY: Expressed in ovaries. Not expressed in adult males. CC {ECO:0000269|PubMed:18434412}. CC -!- DEVELOPMENTAL STAGE: In embryos (at protein level) (PubMed:29317541). CC Expressed both maternally and zygotically (PubMed:10747060, CC PubMed:18430932). {ECO:0000269|PubMed:10747060, CC ECO:0000269|PubMed:18430932, ECO:0000269|PubMed:29317541}. CC -!- DISRUPTION PHENOTYPE: Pronuclear migration does not occur in activated CC eggs. Defects in spindle structures (abnormally shaped spindles, CC spindle spurs, ectopic spindles associated with lost chromosomes and CC mispositioning of the meiosis II spindles) correlated with very high CC frequencies of chromosome non-disjunction and loss. The polar body CC nuclei do not associate with their normal monastral arrays of CC microtubules, the sperm aster is reduced in size, and the centrosomes CC often dissociate from a mitotic spindle that forms in association with CC the male pronucleus. {ECO:0000269|PubMed:10747060, CC ECO:0000269|PubMed:12871909, ECO:0000269|PubMed:18430932}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014298; AAF48114.1; -; Genomic_DNA. DR RefSeq; NP_001285144.1; NM_001298215.1. DR RefSeq; NP_572766.1; NM_132538.2. DR AlphaFoldDB; Q9VYS4; -. DR SMR; Q9VYS4; -. DR BioGRID; 58557; 34. DR IntAct; Q9VYS4; 1. DR STRING; 7227.FBpp0309611; -. DR PaxDb; 7227-FBpp0073417; -. DR EnsemblMetazoa; FBtr0073573; FBpp0073417; FBgn0260780. DR EnsemblMetazoa; FBtr0342743; FBpp0309611; FBgn0260780. DR GeneID; 32152; -. DR KEGG; dme:Dmel_CG15737; -. DR UCSC; CG15737-RA; d. melanogaster. DR AGR; FB:FBgn0260780; -. DR CTD; 32152; -. DR FlyBase; FBgn0260780; wisp. DR VEuPathDB; VectorBase:FBgn0260780; -. DR eggNOG; KOG2277; Eukaryota. DR GeneTree; ENSGT00940000156640; -. DR InParanoid; Q9VYS4; -. DR OMA; SHANSPC; -. DR OrthoDB; 1080369at2759; -. DR PhylomeDB; Q9VYS4; -. DR SignaLink; Q9VYS4; -. DR BioGRID-ORCS; 32152; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 32152; -. DR PRO; PR:Q9VYS4; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0260780; Expressed in egg cell and 16 other cell types or tissues. DR ExpressionAtlas; Q9VYS4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IDA:FlyBase. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0007343; P:egg activation; IMP:FlyBase. DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase. DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase. DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:FlyBase. DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central. DR GO; GO:0001556; P:oocyte maturation; IMP:FlyBase. DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB. DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase. DR GO; GO:0007344; P:pronuclear fusion; IMP:FlyBase. DR GO; GO:0035046; P:pronuclear migration; IMP:FlyBase. DR GO; GO:0035044; P:sperm aster formation; IMP:FlyBase. DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IMP:FlyBase. DR CDD; cd05402; NT_PAP_TUTase; 1. DR Gene3D; 1.10.1410.10; -; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR002058; PAP_assoc. DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1. DR PANTHER; PTHR12271:SF40; POLY(A) RNA POLYMERASE GLD2; 1. DR Pfam; PF03828; PAP_assoc; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1. DR Genevisible; Q9VYS4; DM. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding; KW mRNA processing; Nucleotide-binding; Reference proteome; RNA-binding; KW Transferase. FT CHAIN 1..1373 FT /note="Poly(A) RNA polymerase gld-2 homolog B" FT /id="PRO_0000341558" FT DOMAIN 1211..1272 FT /note="PAP-associated" FT REGION 75..155 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 175..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 425..543 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 734..770 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 802..866 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 880..928 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 945..1373 FT /note="Sufficent for interaction with Dcr-2" FT /evidence="ECO:0000269|PubMed:29317541" FT REGION 1320..1359 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..489 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 526..543 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 734..749 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 750..764 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 802..817 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 825..866 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 908..923 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1320..1337 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1029 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 1031 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" SQ SEQUENCE 1373 AA; 151312 MW; 348EC66BF5239BAE CRC64; MFSTRISGDM KIFAADVAES SVTATCNTSV QQQQSQQLEF RTRMSAGSPS SKSGQCHLKF GKYNNKTANL LRQVNSCHSS NSSSNTSNNN NEAIKGQQQQ PLHYCNSNNS HSWARKKYFG NGNSNNSLLQ QQQQPSSFFQ RQQQQHQMQM QQEKQATNNN DALMKNQNVV NAHVSDCKSS DSNNNSTSSS NNNSTISSNN NNTSSASNNN TGSSSSCSNR TKPAKWLNEN SSSSSSSNNN NISCRNNNTS SIDTKRRNSS AGATAAYYRK SESESGSSEG AAESTETEAT RTGGCNSNRT AESSSADGGT QATMGKSQDQ EQDQTVKQRP RQQPLSFWKT NYPQTSATQL KDKETVAAVV SAAAVAAAAA AASASEQQQQ QQSLSIEHRR NSGYQQHQQH NYYPYYYSQP KQLTIASFLQ KEMLPDSTEK SSSNTGGSNM IRSSSNGNSN FSRHQYGHQS TGSGYQQQQQ RYRNAQNVYQ QYQHQQQHHA QQHTHPHFRR KHSDNGSGIN KKMHYSPPGK SGDPADRSAS GQQQHHHPHQ QQKTIEILAS SHFNAMHRRM QGGNNKNGYY QHSYNPMTGE VGSTPTRSEH QNIYNLTYIH VDTEATGEAA SAAGSTPVVK PSLLSKPNIS ITPASSTTPT TVDRALLPAV RSVSAPASGS ALPAPANHVR NMFPPPPLAM LGGHGLLSPV TTTTPTKMIS CAQLDEAITA AAASGDKLST SPSYNQAGHY IMPPQQQQQQ QLSSHPIPTG TSSHPPPPPP PHMFFHFADG FCNPGQGHQA PPATMWPHSS SPCYPASYGS SCGSGTGAGT SPHNNDGNAG ALRPASPALS SSSLGSESQW SGTSNRSRLG HNGHPSISPT PSALGSAQLS PHLAEMRVQH PLHQQHPPSH ASHRPHGQMG GHAMSSYVPH RPPPPPHPSI SSPNPTPVAT GAGGPWYEMI LPPDRYLAQA RNIEVTVQPE KLICMCKYDN LSAEIWKRFR GAQQTHNKFK LKMRLWRYLY LWMHQPMFER YRICLVGSTI TGFGTDSSDI DMCLLPEQGV HPHQHQYHQH HHFHNEKRTE ALIILTLFNA VLKDTEVFQD FNLIEARVPI LRFKDISNGI EVDLNFNNCV GIKNTYLLQL YAQMDWRTRP LVVIVKLWAQ YHDINDAKRM TISSYSLVLM VLHYLQHACV PHVLPCLHSL YPEKFQLGQQ DCLDLDLIEP IEPYQALNTQ TLGEHLLGFF KYYSTFDFRN FAISIRTGGV LPVSTCRMAK SPKNDVYQWK ELNIEEPFDL SNTARSVYDG PTFERVKAVF LISARRLDHT LDLATIFRPI HHVPEHFPQL QQHQQQFEQQ LHHPISGQQR SAGGGGDGAN PVPSTLNPDA ASTFAETTAA HVA //