PABP2_DROME
ID PABP2_DROME Reviewed; 224 AA.
AC Q7KNF2; A1Z7B1; Q27926; Q7JQ60;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Polyadenylate-binding protein 2;
DE Short=PABP-2;
DE Short=Poly(A)-binding protein 2;
DE Short=dPABP2;
DE AltName: Full=Nuclear poly(A)-binding protein 1;
DE AltName: Full=Poly(A)-binding protein II;
DE Short=PABII;
DE AltName: Full=Polyadenylate-binding nuclear protein 1;
DE AltName: Full=Protein rox2;
GN Name=Pabp2 {ECO:0000312|FlyBase:FBgn0005648};
GN Synonyms=rox2 {ECO:0000303|PubMed:10481015, ECO:0000303|PubMed:7890163};
GN ORFNames=CG2163;
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] {ECO:0000305, ECO:0000312|EMBL:AAA73522.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo {ECO:0000269|PubMed:7890163};
RX PubMed=7890163; DOI=10.1016/0378-1119(94)00840-o;
RA Brand S.F., Pichoff S., Noselli S., Bourbon H.-M.;
RT "Novel Drosophila melanogaster genes encoding RRM-type RNA-binding proteins
RT identified by a degenerate PCR strategy.";
RL Gene 154:187-192(1995).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF00976.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AAF00976.1};
RX PubMed=10481015; DOI=10.1093/nar/27.19.3771;
RA Benoit B., Nemeth A., Aulner N., Kuhn U., Simonelig M., Wahle E.,
RA Bourbon H.-M.;
RT "The Drosophila poly(A)-binding protein II is ubiquitous throughout
RT Drosophila development and has the same function in mRNA polyadenylation as
RT its bovine homolog in vitro.";
RL Nucleic Acids Res. 27:3771-3778(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305}
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] {ECO:0000312|EMBL:AAL48102.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48102.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 ZC3H3.
RX PubMed=19364924; DOI=10.1083/jcb.200811072;
RA Hurt J.A., Obar R.A., Zhai B., Farny N.G., Gygi S.P., Silver P.A.;
RT "A conserved CCCH-type zinc finger protein regulates mRNA nuclear
RT adenylation and export.";
RL J. Cell Biol. 185:265-277(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21203496; DOI=10.1371/journal.pgen.1001254;
RA Yamamoto-Hino M., Kanie Y., Awano W., Aoki-Kinoshita K.F., Yano H.,
RA Nishihara S., Okano H., Ueda R., Kanie O., Goto S.;
RT "Identification of genes required for neural-specific glycosylation using
RT functional genomics.";
RL PLoS Genet. 6:E1001254-E1001254(2010).
CC -!- FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre-
CC mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream
CC cleavage product (PubMed:10481015). Stimulates poly(A) polymerase
CC (PAPOLA) conferring processivity on the poly(A) tail elongation
CC reaction and controls also the poly(A) tail length (By similarity).
CC Increases the affinity of poly(A) polymerase for RNA (By similarity).
CC Binds to poly(A) and to poly(G) with high affinity (PubMed:10481015).
CC May protect the poly(A) tail from degradation (By similarity). Plays a
CC role in the positive regulation of alpha-1,3 fucosylation, possibly by
CC cooperating with swm which regulates nuclear export of
CC fucosyltransferase FucTA (PubMed:21203496).
CC {ECO:0000250|UniProtKB:Q28165, ECO:0000269|PubMed:10481015,
CC ECO:0000269|PubMed:21203496}.
CC -!- SUBUNIT: Interacts with ZC3H3. {ECO:0000269|PubMed:19364924}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10481015}. Cytoplasm
CC {ECO:0000269|PubMed:10481015}. Note=Shuttles between the nucleus and
CC the cytoplasm but predominantly found in the nucleus. Mostly found in
CC the nucleus in the germarium. From egg chamber formation onwards,
CC expressed in both the nuclei and cytoplasm of nurse cells and the
CC oocyte. At stage 10, abundant in the nuclei of nurse cells, oocyte and
CC follicle cells and in the cytoplasm of nurse cells. Uniformly
CC distributed in the cytoplasm of early embryos then progressively
CC localizes to nuclei during the pre-blastoderm and syncytial blastoderm
CC stages. After cellularization, localizes mainly to the nucleus and
CC remains nuclear in later embryonic and larval stages. During mitosis,
CC expression levels are reduced in prophase nuclei and expression is
CC localized to the cytoplasm during metaphase. Localizes to nuclear
CC speckles.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in all transcriptionally
CC active cells. {ECO:0000269|PubMed:10481015}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in all developmental stages; egg, embryo, larva, pupa and in
CC both adult males and females. {ECO:0000269|PubMed:10481015}.
CC -!- DOMAIN: The RRM domain is essential for specific adenine bases
CC recognition in the poly(A) tail but not sufficient for poly(A) binding.
CC {ECO:0000250|UniProtKB:Q28165}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced alpha-
CC 1,3-fucosylation of chp. {ECO:0000269|PubMed:21203496}.
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DR EMBL; L23873; AAA28862.1; -; mRNA.
DR EMBL; L34934; AAA73522.1; -; mRNA.
DR EMBL; AF116341; AAF00976.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF59127.1; -; Genomic_DNA.
DR EMBL; AY070631; AAL48102.1; -; mRNA.
DR EMBL; AY075519; AAL68327.1; -; mRNA.
DR RefSeq; NP_476902.1; NM_057554.4.
DR RefSeq; NP_724648.1; NM_165589.3.
DR AlphaFoldDB; Q7KNF2; -.
DR SMR; Q7KNF2; -.
DR BioGRID; 61644; 15.
DR IntAct; Q7KNF2; 1.
DR STRING; 7227.FBpp0087863; -.
DR PaxDb; Q7KNF2; -.
DR PRIDE; Q7KNF2; -.
DR ABCD; Q7KNF2; 3 sequenced antibodies.
DR DNASU; 35788; -.
DR EnsemblMetazoa; FBtr0088785; FBpp0087863; FBgn0005648.
DR EnsemblMetazoa; FBtr0088786; FBpp0087864; FBgn0005648.
DR GeneID; 35788; -.
DR KEGG; dme:Dmel_CG2163; -.
DR CTD; 35788; -.
DR FlyBase; FBgn0005648; Pabp2.
DR VEuPathDB; VectorBase:FBgn0005648; -.
DR eggNOG; KOG4209; Eukaryota.
DR GeneTree; ENSGT00940000154606; -.
DR HOGENOM; CLU_012062_23_3_1; -.
DR InParanoid; Q7KNF2; -.
DR OMA; RRGYYMP; -.
DR OrthoDB; 1412946at2759; -.
DR PhylomeDB; Q7KNF2; -.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; Q7KNF2; -.
DR BioGRID-ORCS; 35788; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Pabp2; fly.
DR GenomeRNAi; 35788; -.
DR PRO; PR:Q7KNF2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0005648; Expressed in eye disc (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q7KNF2; baseline and differential.
DR Genevisible; Q7KNF2; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR GO; GO:0060050; P:positive regulation of protein glycosylation; IMP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; mRNA processing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..224
FT /note="Polyadenylate-binding protein 2"
FT /id="PRO_0000252085"
FT DOMAIN 96..173
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..74
FT /evidence="ECO:0000255"
FT CONFLICT 73
FT /note="A -> R (in Ref. 1; AAA73522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24978 MW; FD2B99E62DD633A5 CRC64;
MADEDITLNE DQLLESLEET NGEQETEIAT EVEEEGSMQI DPELEAIKAR VKEMEEEAEK
IKQMQSEVDK QMAGGSTTGL ATVPLSLEEK QEIDTRSVYV GNVDYGASAE ELEAHFHGCG
TINRVTILCN KADGHPKGFA YIEFGSKEFV ETALAMNETL FRGRQIKVMS KRTNRPGLST
TNRFARGSFR GRGARVSRAC CHSTFRGARR AMGYRGRANY YAPY
