GLD2A_DROME
ID GLD2A_DROME Reviewed; 1364 AA.
AC Q9VD44; B5RJK9; Q8MR77;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Poly(A) RNA polymerase gld-2 homolog A;
DE Short=DmGLD2;
DE EC=2.7.7.19 {ECO:0000269|PubMed:18780789};
GN Name=Gld2; ORFNames=CG5732;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FMR1 AND EIF-4E, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ASP-995.
RX PubMed=18780789; DOI=10.1073/pnas.0803185105;
RA Kwak J.E., Drier E., Barbee S.A., Ramaswami M., Yin J.C.P., Wickens M.;
RT "GLD2 poly(A) polymerase is required for long-term memory.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14644-14649(2008).
CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP
CC monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In
CC contrast to the canonical nuclear poly(A) RNA polymerase, it only adds
CC poly(A) to selected cytoplasmic mRNAs. Required for formation of long
CC term memory. {ECO:0000269|PubMed:18780789}.
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:18780789};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000269|PubMed:18780789};
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 Fmr1 and eIF-4E. {ECO:0000269|PubMed:18780789}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18780789}. Nucleus
CC {ECO:0000269|PubMed:18780789}. Note=Found in neuronal cytoplasm,
CC present in discrete neuronal particles associated with mRNA control,
CC and in nuclear puncta.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9VD44-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VD44-2; Sequence=VSP_034331;
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:18780789}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae, pupae and adults.
CC {ECO:0000269|PubMed:18780789}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC subfamily. {ECO:0000305}.
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DR EMBL; AE014297; AAF55959.3; -; Genomic_DNA.
DR EMBL; AY122076; AAM52588.1; -; mRNA.
DR EMBL; BT044483; ACH95257.1; -; mRNA.
DR RefSeq; NP_001262829.1; NM_001275900.1. [Q9VD44-1]
DR RefSeq; NP_651012.2; NM_142755.4. [Q9VD44-1]
DR AlphaFoldDB; Q9VD44; -.
DR SMR; Q9VD44; -.
DR BioGRID; 67563; 4.
DR IntAct; Q9VD44; 3.
DR STRING; 7227.FBpp0301888; -.
DR PaxDb; Q9VD44; -.
DR PRIDE; Q9VD44; -.
DR EnsemblMetazoa; FBtr0305038; FBpp0293575; FBgn0038934. [Q9VD44-1]
DR EnsemblMetazoa; FBtr0310204; FBpp0301888; FBgn0038934. [Q9VD44-1]
DR GeneID; 42602; -.
DR KEGG; dme:Dmel_CG5732; -.
DR UCSC; CG5732-RA; d. melanogaster. [Q9VD44-1]
DR CTD; 42602; -.
DR FlyBase; FBgn0038934; Gld2.
DR VEuPathDB; VectorBase:FBgn0038934; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156640; -.
DR HOGENOM; CLU_258575_0_0_1; -.
DR InParanoid; Q9VD44; -.
DR OMA; TVVHTCP; -.
DR PhylomeDB; Q9VD44; -.
DR BRENDA; 2.7.7.19; 1994.
DR BioGRID-ORCS; 42602; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42602; -.
DR PRO; PR:Q9VD44; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038934; Expressed in testis and 11 other tissues.
DR ExpressionAtlas; Q9VD44; baseline and differential.
DR Genevisible; Q9VD44; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
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:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB.
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 Alternative splicing; ATP-binding; Cytoplasm; Magnesium; Manganese;
KW Metal-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..1364
FT /note="Poly(A) RNA polymerase gld-2 homolog A"
FT /id="PRO_0000341557"
FT DOMAIN 1163..1224
FT /note="PAP-associated"
FT REGION 27..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 993
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 995
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 881..1364
FT /note="PEENNDDDELPLVVHNRYWREFFGYTPADRFLLRAKFVEMRRPPKVMGCKNK
FT WDPLSLSVWKKFLESQQTRHVYKIKMRLWRAIYTVAMKNYPRYGLYLVGSSISYFGSKC
FT SDMDICMLACTNPNIDSRMEAVYHLHVMKELLGRTNMFQDFNLIEARVPILRFTDRCHK
FT VEVDINFNNSVGIRNTHLLYCYSQLDWRVRPMALTVKQWAQYHNINNAKNMTISSYSLM
FT LMVIHFLQVGASPPVLPCLHNLYPEKFGLLQPNDFGYVDMNEVMAPYQSDNSQTLGDLL
FT LSFLHYYSVFDYGKYAISIRVGGVLPIEVCRAATAPKNDIHQWNELCIEEPFDQTNTAR
FT SVYDTDTFERIKTIFVASYRRLDSTRNLSAIFEDYDGPTILMQQPSVDSEIELYEGQHH
FT RLLPNRGSSRSNSAIPSPRPSILMVDKATTAIWDDINNKPDHPVLSHSNNYDATNECTG
FT NGSLMGLKDNSVADKPPIA -> VGELKNVLLNGQITKFISSKSYFFLSSVCLIVHFIR
FT FTK (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_034331"
FT MUTAGEN 995
FT /note="D->A: Destroys active site."
FT /evidence="ECO:0000269|PubMed:18780789"
FT CONFLICT 523
FT /note="I -> V (in Ref. 3; AAM52588 and 4; ACH95257)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="P -> A (in Ref. 3; AAM52588 and 4; ACH95257)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="T -> TAA (in Ref. 3; AAM52588 and 4; ACH95257)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="A -> T (in Ref. 3; AAM52588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1364 AA; 147592 MW; 9BAFCAE8D75083CA CRC64;
MSTAMAMAAA ASSSAAAATA TTTAISNSTN TTASPATTNT INTTTKTITT SEVPLEPASN
MAPKALEIED SGRNEPEDLE HGAAKPLEQR KTTVVHTCPR PPGGYKYSME FLYGIGSGMA
GIPLNIPTPS SITPRTVRST APLLTTHMPL LTNMGVAPSR PSGIRYPGSA GGSNGTTVAA
STTPSTTVTT SSGSPGSGAE AITSSVSSSG LPAAGLQAAQ FICQGYMPTG PQRRLWHAEN
AVWQFDRNYP YNQAYSPPYG IPMMPVGFEH PYGQRIIYPG YYNQTPPGIN PAAVAGLTRT
NRPVTQQPHI LTQPAVGTTE SSEEAPATLG NAPQVSSTWR YGRPGTHRGR HAVPTAAAPA
LLHRDSKSFY NSIGSGMANG PRFKAPFVAN VRNFQAGAVA TVAAGGAATT AVVGTSAPAT
GAASSSDQNV ATKRNHQGAA TQNNHRNRHN AKKGGKNSVG KELTSNSSES LSNSSSKSQL
NKRPSSSSSI SPIKHPHRNY RNRMRYTATE PTEQKAATTT VPISNYQPPQ QSTSTVRRTS
KFQGSNAYQA HTAAGRQQSR FYQSRHMDGY VFQSGHYMVY AAGAPPVGLR PGKSPVSEAT
GAPPGAAAAT AAAATAVAAT AAAAEGGGAA EGGGAAAAPV TASSATLEGE QPLDSDFDQR
QEFADLGLDP ANGGFSSDLE PNGIKQDTSE LDTHSCLISH PNSEVDGDDN QSLASFAPSV
ESDDSDSELS DASVESVARD ILVSCLAVAT GAEEPDFSGP NLVPYGDMHY LKELDKKNPP
TNGYRSHRPY HQSHYAYHSQ MSPRGLSCCG DMLNQHSEDL VFKLDQNQPD GIESGKNIFL
REITEQPDNI SVASNLSCSP SASSSKSVLA PMASKSNITM PEENNDDDEL PLVVHNRYWR
EFFGYTPADR FLLRAKFVEM RRPPKVMGCK NKWDPLSLSV WKKFLESQQT RHVYKIKMRL
WRAIYTVAMK NYPRYGLYLV GSSISYFGSK CSDMDICMLA CTNPNIDSRM EAVYHLHVMK
ELLGRTNMFQ DFNLIEARVP ILRFTDRCHK VEVDINFNNS VGIRNTHLLY CYSQLDWRVR
PMALTVKQWA QYHNINNAKN MTISSYSLML MVIHFLQVGA SPPVLPCLHN LYPEKFGLLQ
PNDFGYVDMN EVMAPYQSDN SQTLGDLLLS FLHYYSVFDY GKYAISIRVG GVLPIEVCRA
ATAPKNDIHQ WNELCIEEPF DQTNTARSVY DTDTFERIKT IFVASYRRLD STRNLSAIFE
DYDGPTILMQ QPSVDSEIEL YEGQHHRLLP NRGSSRSNSA IPSPRPSILM VDKATTAIWD
DINNKPDHPV LSHSNNYDAT NECTGNGSLM GLKDNSVADK PPIA
