PABP2_XENTR
ID PABP2_XENTR Reviewed; 296 AA.
AC Q6NVP7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=pabpn1 {ECO:0000250|UniProtKB:Q28165}; ORFNames=TGas130l12.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ82538.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAJ82538.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR761856; CAJ82538.1; -; mRNA.
DR EMBL; BC067958; AAH67958.1; -; mRNA.
DR RefSeq; NP_001001230.1; NM_001001230.1.
DR AlphaFoldDB; Q6NVP7; -.
DR SMR; Q6NVP7; -.
DR STRING; 8364.ENSXETP00000036077; -.
DR PaxDb; Q6NVP7; -.
DR DNASU; 407911; -.
DR GeneID; 407911; -.
DR KEGG; xtr:407911; -.
DR CTD; 8106; -.
DR Xenbase; XB-GENE-1007049; pabpn1.
DR eggNOG; KOG4209; Eukaryota.
DR HOGENOM; CLU_012062_23_1_1; -.
DR InParanoid; Q6NVP7; -.
DR OMA; PRATSWY; -.
DR OrthoDB; 1412946at2759; -.
DR PhylomeDB; Q6NVP7; -.
DR TreeFam; TF105907; -.
DR Reactome; R-XTR-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-XTR-72187; mRNA 3'-end processing.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR ExpressionAtlas; Q6NVP7; baseline.
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..296
FT /note="Polyadenylate-binding protein 2"
FT /id="PRO_0000252084"
FT DOMAIN 163..240
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 146..296
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT COILED 107..141
FT /evidence="ECO:0000255"
FT COMPBIAS 83..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 32229 MW; AD06CA6F65F19C8D CRC64;
MAAVSSAASL RGADYENGLR GGAGPSGGGQ DPGEDDPMGR GTLDLDLELL GQGRRSRRVG
GRTAPGRRSG GRGGSGGGGA GGLEELEDEE LEEEEPGELT GDQTIEDPEL EAIKARVREM
EEEAEKLKEL QNEVEKQMNM SPPPGNAGPV IMSIEEKMEA DARSIYVGNV DYGATAEELE
AHFHGCGSVN RVTILCDKYT GHPKGFAYIE FSDKESVRTS LALDESLFRG RQIKVVPKRT
NRPGISTTDR GFPRARYRAR ASSYSSRSRF YSGYTPRPRG RVYRGRARVT SWYTPY
