PABP_DROME
ID PABP_DROME Reviewed; 634 AA.
AC P21187; A4UZM5; Q0E932; Q9V8C3;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Polyadenylate-binding protein;
DE Short=PABP;
DE Short=Poly(A)-binding protein;
GN Name=pAbp; ORFNames=CG5119;
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 [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=2125288; DOI=10.1016/0378-1119(90)90256-q;
RA Lefrere V., Vincent A., Amalric F.;
RT "Drosophila melanogaster poly(A)-binding protein: cDNA cloning reveals an
RT unusually long 3'-untranslated region of the mRNA, also present in other
RT eukaryotic species.";
RL Gene 96:219-225(1990).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8482550; DOI=10.1016/0378-1119(93)90387-i;
RA Lefrere V., Vincent A., Amalric F.;
RT "Drosophila melanogaster poly(A)-binding protein: cDNA cloning reveals an
RT unusually long 3'-untranslated region of the mRNA, also present in other
RT eukaryotic species.";
RL Gene 126:295-296(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP INTERACTION WITH GW.
RX PubMed=19797087; DOI=10.1128/mcb.01081-09;
RA Zekri L., Huntzinger E., Heimstadt S., Izaurralde E.;
RT "The silencing domain of GW182 interacts with PABPC1 to promote
RT translational repression and degradation of microRNA targets and is
RT required for target release.";
RL Mol. Cell. Biol. 29:6220-6231(2009).
RN [7]
RP INTERACTION WITH LARP.
RX PubMed=19631203; DOI=10.1016/j.ydbio.2009.07.016;
RA Blagden S.P., Gatt M.K., Archambault V., Lada K., Ichihara K., Lilley K.S.,
RA Inoue Y.H., Glover D.M.;
RT "Drosophila Larp associates with poly(A)-binding protein and is required
RT for male fertility and syncytial embryo development.";
RL Dev. Biol. 334:186-197(2009).
RN [8]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH EIF4E1; CUP; TRAL AND ME31B, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=28875934; DOI=10.7554/elife.27891;
RA Wang M., Ly M., Lugowski A., Laver J.D., Lipshitz H.D., Smibert C.A.,
RA Rissland O.S.;
RT "ME31B globally represses maternal mRNAs by two distinct mechanisms during
RT the Drosophila maternal-to-zygotic transition.";
RL Elife 6:0-0(2017).
RN [9]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH TYF; ATX2 AND LSM12A,
RP IDENTIFICATION IN A COMPLEX WITH TYF; ATX2 AND ME31B, AND INTERACTION WITH
RP ME31B; TYF AND ATX2.
RX PubMed=28388438; DOI=10.1016/j.molcel.2017.03.004;
RA Lee J., Yoo E., Lee H., Park K., Hur J.H., Lim C.;
RT "LSM12 and ME31B/DDX6 Define Distinct Modes of Posttranscriptional
RT Regulation by ATAXIN-2 Protein Complex in Drosophila Circadian Pacemaker
RT Neurons.";
RL Mol. Cell 66:129-140(2017).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA (PubMed:2125288). Since it
CC interacts with the cap-associating translation initiation factor eIF4G,
CC it is likely that it functions by linking Atx2 to the cap-binding
CC complex (PubMed:28388438). Forms a complex with tyf and Atx2 which
CC functions in adult circadian pacemaker neurons to sustain circadian
CC rhythms likely by switching between activator and repressor modes of
CC post-transcriptional regulation via interaction with Lsm12a or me31B,
CC respectively (PubMed:28388438). The activator complex (Atx2-tyf
CC activator complex) activates the TYF-dependent translation of per to
CC maintain 24 hour periodicity in circadian locomotor behaviors, whereas
CC the repressor complex (Atx2-Not1 repressor complex) promotes Not1-
CC dependent post-transcriptional gene silencing and supports high-
CC amplitude circadian rhythms in a per-independent manner
CC (PubMed:28388438). In 0-1 hour embryos, forms a ribonucleoprotein
CC complex (RNP) with me31B, eIF4E1, tral and cup which binds to various
CC mRNAs including maternal mRNAs, and down-regulates their expression
CC during the maternal-to-zygotic transition (PubMed:28875934).
CC {ECO:0000269|PubMed:2125288, ECO:0000269|PubMed:28388438,
CC ECO:0000269|PubMed:28875934}.
CC -!- SUBUNIT: Core component of the neuromuscular Atx2 complex, composed of
CC at least Atx2, tyf, pAbp, Lsm12a (PubMed:28388438). Interacts with Atx2
CC (via PAM2 motif) (PubMed:28388438). Atx2 and pAbp form a subcomplex
CC that can associate with the 5' cap of pre-mRNAs independently of tyf,
CC Lsm12a or me31B (PubMed:28388438). Forms a ribonucleoprotein complex
CC (RNP) containing at least me31B, eIF4E1, cup, tral and pAbp; this
CC interaction is required for the translational silencing of maternal
CC mRNAs during the maternal-to-zygotic transition (PubMed:28875934). In
CC 1-5 hour embryos, interaction with me31B is severely reduced and there
CC is no detected interaction with cup and tral, however interaction with
CC eIF4E1 and eIF4G1 remains unchanged (PubMed:28875934). Interacts with
CC gw; this interaction interferes with the binding of pAbp to eIF4G and
CC is required for miRNA-mediated silencing (PubMed:19797087). Interacts
CC with larp (PubMed:19631203). {ECO:0000269|PubMed:19631203,
CC ECO:0000269|PubMed:19797087, ECO:0000269|PubMed:28388438,
CC ECO:0000269|PubMed:28875934}.
CC -!- INTERACTION:
CC P21187; P48598: eIF4E1; NbExp=2; IntAct=EBI-103658, EBI-198574;
CC P21187; Q8SY33: gw; NbExp=11; IntAct=EBI-103658, EBI-160693;
CC P21187; Q9W4M7: tyf; NbExp=3; IntAct=EBI-103658, EBI-194676;
CC P21187; Q9UPQ9: TNRC6B; Xeno; NbExp=6; IntAct=EBI-103658, EBI-947158;
CC P21187; Q9HCJ0: TNRC6C; Xeno; NbExp=5; IntAct=EBI-103658, EBI-6507625;
CC -!- DEVELOPMENTAL STAGE: Expressed during the first 5 hrs of embryogenesis
CC (at protein level) (PubMed:28875934). Expressed both maternally and
CC zygotically throughout development (PubMed:2125288).
CC {ECO:0000269|PubMed:2125288, ECO:0000269|PubMed:28875934}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; L05109; AAA70421.1; -; mRNA.
DR EMBL; AE013599; AAF57746.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68175.1; -; Genomic_DNA.
DR EMBL; AY118528; AAM49897.1; -; mRNA.
DR PIR; S30887; S30887.
DR RefSeq; NP_476667.1; NM_057319.5.
DR RefSeq; NP_725749.1; NM_166264.4.
DR RefSeq; NP_725750.1; NM_166265.2.
DR AlphaFoldDB; P21187; -.
DR SMR; P21187; -.
DR BioGRID; 62753; 66.
DR DIP; DIP-52140N; -.
DR ELM; P21187; -.
DR IntAct; P21187; 18.
DR MINT; P21187; -.
DR STRING; 7227.FBpp0085915; -.
DR PaxDb; P21187; -.
DR PRIDE; P21187; -.
DR ABCD; P21187; 15 sequenced antibodies.
DR DNASU; 37070; -.
DR EnsemblMetazoa; FBtr0086736; FBpp0085915; FBgn0265297.
DR EnsemblMetazoa; FBtr0086738; FBpp0085917; FBgn0265297.
DR EnsemblMetazoa; FBtr0086740; FBpp0085919; FBgn0265297.
DR GeneID; 37070; -.
DR KEGG; dme:Dmel_CG5119; -.
DR CTD; 37070; -.
DR FlyBase; FBgn0265297; pAbp.
DR VEuPathDB; VectorBase:FBgn0265297; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000169027; -.
DR HOGENOM; CLU_012062_22_2_1; -.
DR InParanoid; P21187; -.
DR OMA; ASPMEQK; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; P21187; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-429947; Deadenylation of mRNA.
DR Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P21187; -.
DR BioGRID-ORCS; 37070; 1 hit in 3 CRISPR screens.
DR ChiTaRS; pAbp; fly.
DR GenomeRNAi; 37070; -.
DR PRO; PR:P21187; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0265297; Expressed in cleaving embryo and 30 other tissues.
DR Genevisible; P21187; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0008143; F:poly(A) binding; ISS:FlyBase.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:FlyBase.
DR GO; GO:0048599; P:oocyte development; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0045727; P:positive regulation of translation; IGI:FlyBase.
DR GO; GO:0045314; P:regulation of compound eye photoreceptor development; IGI:FlyBase.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..634
FT /note="Polyadenylate-binding protein"
FT /id="PRO_0000081713"
FT DOMAIN 2..80
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 90..167
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 181..259
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 285..362
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 552..629
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT CONFLICT 171..173
FT /note="REK -> Q (in Ref. 1; AAA70421)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..337
FT /note="AA -> PE (in Ref. 1; AAA70421)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="H -> D (in Ref. 1; AAA70421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 69925 MW; A76B204ED206392E CRC64;
MASLYVGDLP QDVNESGLFD KFSSAGPVLS IRVCRDVITR RSLGYAYVNF QQPADAERAL
DTMNFDLVRN KPIRIMWSQR DPSLRRSGVG NVFIKNLDRA IDNKAIYDTF SAFGNILSCK
VATDEKGNSK GYGFVHFETE EAANTSIDKV NGMLLNGKKV YVGKFIPRKE REKELGEKAK
LFTNVYVKNF TEDFDDEKLK EFFEPYGKIT SYKVMSKEDG KSKGFGFVAF ETTEAAEAAV
QALNGKDMGE GKSLYVARAQ KKAERQQELK RKFEELKQKR HESVFGVNLY VKNLDDTIDD
DRLRIAFSPY GNITSAKVMT DEEGRSKGFG FVCFNAASEA TCAVTELNGR VVGSKPLYVA
LAQRKEERKA HLASQYMRHM TGMRMQQLGQ IYQPNAASGF FVPTLPSNQR FFGSQVATQM
RNTPRWVPQV RPPAAIQGVQ AGAAAAGGFQ GTAGAVPTQF RSAAAGARGA QPQVQGTHAA
AAAANNMRNT GARAITGQQT AAPNMQIPGA QIAGGAQQRT SNYKYTSNMR NPPVPQLHQT
QPIPQQLQGK NSEKLIASLL ANAKPQEQKQ ILGERLYPMI EHMHANLAGK ITGMLLEIEN
SELLHMIEDQ EALKAKVEEA VAVLQVHRVT EPAN
