GLD2B_DROME
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 03-AUG-2022, entry version 137.
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).
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 In contrast to the canonical nuclear poly(A) RNA polymerase, it only
CC adds poly(A) to selected cytoplasmic mRNAs. Required for localization
CC of mRNAs to both poles of the egg, to recruit or maintain known
CC centrosomal proteins with two types of microtubule organizing centers
CC (MTOCs): the central MTOC that forms between the meiosis II tandem
CC spindles and the centrosomes of the mitotic spindle. Required at the
CC final stage of oogenesis for meiosis I metaphase arrest and for
CC progression beyond this stage. {ECO:0000269|PubMed:10747060,
CC ECO:0000269|PubMed:12871909, ECO:0000269|PubMed:18430932,
CC ECO:0000269|PubMed:18434412}.
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.
CC {ECO:0000269|PubMed:18434412}.
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: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:10747060, ECO:0000269|PubMed:18430932}.
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}.
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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.FBpp0073417; -.
DR PaxDb; Q9VYS4; -.
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 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; 104275at2759; -.
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 tissues.
DR ExpressionAtlas; Q9VYS4; baseline and differential.
DR Genevisible; Q9VYS4; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase 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:0006378; P:mRNA polyadenylation; IMP:FlyBase.
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:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; IDA: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 Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
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 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
