PABP2_DROPS
ID PABP2_DROPS Reviewed; 225 AA.
AC Q28ZX3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Polyadenylate-binding protein 2;
DE Short=PABP-2;
DE Short=Poly(A)-binding protein 2;
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;
GN Name=Pabp2 {ECO:0000250|UniProtKB:Q7KNF2}; ORFNames=GA15278;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL25489.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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. Stimulates poly(A) polymerase (PAPOLA) conferring
CC processivity on the poly(A) tail elongation reaction and controls also
CC the poly(A) tail length. Increases the affinity of poly(A) polymerase
CC for RNA. Binds to poly(A) and to poly(G) with high affinity. May
CC protect the poly(A) tail from degradation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Shuttles between the nucleus and the cytoplasm but predominantly
CC found in the nucleus. {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=EAL25489.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000071; EAL25489.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q28ZX3; -.
DR SMR; Q28ZX3; -.
DR STRING; 7237.FBpp0276575; -.
DR eggNOG; KOG4209; Eukaryota.
DR HOGENOM; CLU_012062_23_3_1; -.
DR InParanoid; Q28ZX3; -.
DR OMA; RRGYYMP; -.
DR PhylomeDB; Q28ZX3; -.
DR ChiTaRS; Pabp2; fly.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS: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 3: Inferred from homology;
KW Coiled coil; Cytoplasm; mRNA processing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..225
FT /note="Polyadenylate-binding protein 2"
FT /id="PRO_0000244518"
FT DOMAIN 96..173
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..74
FT /evidence="ECO:0000255"
FT COMPBIAS 1..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 225 AA; 25092 MW; 265AC2DBDEAD858D CRC64;
MADEDISLNE DQLLESMEET NGEQETEIVT ETEEEGSMQI DPELEAIKAR VKEMEEEAEK
IKQMQSEVDK QMAGGSTTGL AAVPLSLEEK QEIDTRSVYV GNVDYGASAE ELEAHFHGCG
TINRVTILCN KADGHPKGFA YIEFGSKEFV ETALAMNETL FRGRQIKVMS KRTNRPGLST
TNRFARGSFR GRGARASRAC CHSTFRGARR AIRGYRGRAN YYAPY
