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Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2) (dPABP2) (Nuclear poly(A)-binding protein 1) (Poly(A)-binding protein II) (PABII) (Polyadenylate-binding nuclear protein 1) (Protein rox2)

 PABP2_DROME             Reviewed;         224 AA.
Q7KNF2; A1Z7B1; Q27926; Q7JQ60;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
16-JAN-2019, entry version 139.
RecName: Full=Polyadenylate-binding protein 2;
Short=Poly(A)-binding protein 2;
AltName: Full=Nuclear poly(A)-binding protein 1;
AltName: Full=Poly(A)-binding protein II;
AltName: Full=Polyadenylate-binding nuclear protein 1;
AltName: Full=Protein rox2;
Name=Pabp2 {ECO:0000312|FlyBase:FBgn0005648};
Synonyms=rox2 {ECO:0000303|PubMed:10481015,
ECO:0000303|PubMed:7890163}; ORFNames=CG2163;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
[1] {ECO:0000305, ECO:0000312|EMBL:AAA73522.1}
TISSUE=Embryo {ECO:0000269|PubMed:7890163};
PubMed=7890163; DOI=10.1016/0378-1119(94)00840-O;
Brand S.F., Pichoff S., Noselli S., Bourbon H.-M.;
"Novel Drosophila melanogaster genes encoding RRM-type RNA-binding
proteins identified by a degenerate PCR strategy.";
Gene 154:187-192(1995).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF00976.1}
STRAIN=Oregon-R {ECO:0000312|EMBL:AAF00976.1};
PubMed=10481015; DOI=10.1093/nar/27.19.3771;
Benoit B., Nemeth A., Aulner N., Kuhn U., Simonelig M., Wahle E.,
Bourbon H.-M.;
"The Drosophila poly(A)-binding protein II is ubiquitous throughout
Drosophila development and has the same function in mRNA
polyadenylation as its bovine homolog in vitro.";
Nucleic Acids Res. 27:3771-3778(1999).
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000305}
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000312|EMBL:AAL48102.1}
STRAIN=Berkeley {ECO:0000312|EMBL:AAL48102.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
PubMed=19364924; DOI=10.1083/jcb.200811072;
Hurt J.A., Obar R.A., Zhai B., Farny N.G., Gygi S.P., Silver P.A.;
"A conserved CCCH-type zinc finger protein regulates mRNA nuclear
adenylation and export.";
J. Cell Biol. 185:265-277(2009).
PubMed=21203496; DOI=10.1371/journal.pgen.1001254;
Yamamoto-Hino M., Kanie Y., Awano W., Aoki-Kinoshita K.F., Yano H.,
Nishihara S., Okano H., Ueda R., Kanie O., Goto S.;
"Identification of genes required for neural-specific glycosylation
using functional genomics.";
PLoS Genet. 6:E1001254-E1001254(2010).
-!- FUNCTION: Involved in the 3'-end formation of mRNA precursors
(pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the
upstream cleavage product (PubMed:10481015). Stimulates poly(A)
polymerase (PAPOLA) conferring processivity on the poly(A) tail
elongation reaction and controls also the poly(A) tail length (By
similarity). Increases the affinity of poly(A) polymerase for RNA
(By similarity). Binds to poly(A) and to poly(G) with high
affinity (PubMed:10481015). May protect the poly(A) tail from
degradation (By similarity). Plays a role in the positive
regulation of alpha-1,3 fucosylation, possibly by cooperating with
swm which regulates nuclear export of fucosyltransferase FucTA
(PubMed:21203496). {ECO:0000250|UniProtKB:Q28165,
ECO:0000269|PubMed:10481015, ECO:0000269|PubMed:21203496}.
-!- SUBUNIT: Interacts with ZC3H3. {ECO:0000269|PubMed:19364924}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10481015}.
Cytoplasm {ECO:0000269|PubMed:10481015}. Note=Shuttles between the
nucleus and the cytoplasm but predominantly found in the nucleus.
Mostly found in the nucleus in the germarium. From egg chamber
formation onwards, expressed in both the nuclei and cytoplasm of
nurse cells and the oocyte. At stage 10, abundant in the nuclei of
nurse cells, oocyte and follicle cells and in the cytoplasm of
nurse cells. Uniformly distributed in the cytoplasm of early
embryos then progressively localizes to nuclei during the pre-
blastoderm and syncytial blastoderm stages. After cellularization,
localizes mainly to the nucleus and remains nuclear in later
embryonic and larval stages. During mitosis, expression levels are
reduced in prophase nuclei and expression is localized to the
cytoplasm during metaphase. Localizes to nuclear speckles.
-!- TISSUE SPECIFICITY: Expressed ubiquitously in all
transcriptionally active cells. {ECO:0000269|PubMed:10481015}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed in all developmental stages; egg, embryo, larva, pupa
and in both adult males and females.
-!- DOMAIN: The RRM domain is essential for specific adenine bases
recognition in the poly(A) tail but not sufficient for poly(A)
binding. {ECO:0000250|UniProtKB:Q28165}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
alpha-1,3-fucosylation of chp. {ECO:0000269|PubMed:21203496}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; L23873; AAA28862.1; -; mRNA.
EMBL; L34934; AAA73522.1; -; mRNA.
EMBL; AF116341; AAF00976.1; -; Genomic_DNA.
EMBL; AE013599; AAF59127.1; -; Genomic_DNA.
EMBL; AY070631; AAL48102.1; -; mRNA.
EMBL; AY075519; AAL68327.1; -; mRNA.
RefSeq; NP_476902.1; NM_057554.4.
RefSeq; NP_724648.1; NM_165589.3.
UniGene; Dm.521; -.
ProteinModelPortal; Q7KNF2; -.
SMR; Q7KNF2; -.
BioGrid; 61644; 15.
IntAct; Q7KNF2; 1.
STRING; 7227.FBpp0087863; -.
PaxDb; Q7KNF2; -.
EnsemblMetazoa; FBtr0088785; FBpp0087863; FBgn0005648.
EnsemblMetazoa; FBtr0088786; FBpp0087864; FBgn0005648.
GeneID; 35788; -.
KEGG; dme:Dmel_CG2163; -.
CTD; 35788; -.
FlyBase; FBgn0005648; Pabp2.
eggNOG; KOG4209; Eukaryota.
GeneTree; ENSGT00940000154606; -.
InParanoid; Q7KNF2; -.
KO; K14396; -.
OrthoDB; 1412946at2759; -.
PhylomeDB; Q7KNF2; -.
Reactome; R-DME-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
Reactome; R-DME-72187; mRNA 3'-end processing.
Reactome; R-DME-77595; Processing of Intronless Pre-mRNAs.
ChiTaRS; Pabp2; fly.
GenomeRNAi; 35788; -.
PRO; PR:Q7KNF2; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0005648; Expressed in 32 organ(s), highest expression level in embryo.
ExpressionAtlas; Q7KNF2; baseline and differential.
Genevisible; Q7KNF2; DM.
GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
GO; GO:1904247; P:positive regulation of polynucleotide adenylyltransferase activity; IEA:InterPro.
GO; GO:0060050; P:positive regulation of protein glycosylation; IMP:UniProtKB.
Gene3D;; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034911; PABP2.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR44316; PTHR44316; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; mRNA processing; Nucleus;
Reference proteome; RNA-binding.
CHAIN 1 224 Polyadenylate-binding protein 2.
DOMAIN 96 173 RRM. {ECO:0000255|PROSITE-
COILED 9 74 {ECO:0000255}.
CONFLICT 73 73 A -> R (in Ref. 1; AAA73522).
SEQUENCE 224 AA; 24978 MW; FD2B99E62DD633A5 CRC64;

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