PAB2B_XENLA
ID PAB2B_XENLA Reviewed; 295 AA.
AC Q7ZXB8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Polyadenylate-binding protein 2-B;
DE Short=PABP-2-B;
DE Short=Poly(A)-binding protein 2-B;
DE AltName: Full=Nuclear poly(A)-binding protein 1-B;
DE AltName: Full=Poly(A)-binding protein II-B;
DE Short=PABII-B;
DE AltName: Full=Polyadenylate-binding nuclear protein 1-B;
DE AltName: Full=XLnPABP2-B;
DE AltName: Full=nPABP2-B;
DE AltName: Full=xPABPII-B;
GN Name=pabpn1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH45063.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH45063.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000250|UniProtKB:Q28165}.
CC -!- SUBUNIT: Monomer and homooligomer. Binds RNA as a monomer and
CC oligomerizes when bound to poly(A) (By similarity).
CC {ECO:0000250|UniProtKB:Q86U42}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9DDY9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q86U42}. Note=Shuttles between the nucleus and
CC the cytoplasm but predominantly found in the nucleus.
CC {ECO:0000250|UniProtKB:Q86U42}.
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}.
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DR EMBL; BC045063; AAH45063.1; -; mRNA.
DR RefSeq; NP_001080719.1; NM_001087250.1.
DR RefSeq; XP_018080447.1; XM_018224958.1.
DR AlphaFoldDB; Q7ZXB8; -.
DR SMR; Q7ZXB8; -.
DR DNASU; 380411; -.
DR GeneID; 380411; -.
DR KEGG; xla:380411; -.
DR CTD; 380411; -.
DR Xenbase; XB-GENE-1007055; pabpn1.L.
DR OrthoDB; 1412946at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 380411; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:1904247; P:positive regulation of polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034911; PABP2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23236:SF16; PTHR23236:SF16; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; mRNA processing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..295
FT /note="Polyadenylate-binding protein 2-B"
FT /id="PRO_0000252083"
FT DOMAIN 162..239
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..295
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT COILED 106..140
FT /evidence="ECO:0000255"
FT COMPBIAS 82..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 295 AA; 32213 MW; 0E221DE8B50B678B CRC64;
MAAVSSVASL RGADYENGLR GGAGPSGGGQ DPGEDDPMGR GTLDLDLELL TQGRRNRRVG
GRTAPGRRSG GRGGSGGGAG GLEELEDEEL EEEEPGELTG DQTIEDPELE AIKARVREME
EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSVEEKMEAD ARSIYVGNVD YGATAEELEA
HFHGCGSVNR VTILCDKFTG HPKGFAYIEF SDKESVRTSL ALDESLFRGR QIKVVPKRTN
RPGISTTDRG FPRARYRARA SSYSSRSRFY SGYTPRPRGR VYRGRARATS WYTPY
