PAB2A_XENLA
ID PAB2A_XENLA Reviewed; 296 AA.
AC Q9DDY9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Polyadenylate-binding protein 2-A;
DE Short=PABP-2-A;
DE Short=Poly(A)-binding protein 2-A;
DE AltName: Full=Nuclear poly(A)-binding protein 1-A;
DE AltName: Full=Poly(A)-binding protein II-A;
DE Short=PABII-A;
DE AltName: Full=Polyadenylate-binding nuclear protein 1-A;
DE AltName: Full=XLnPABP2-A;
DE AltName: Full=nPABP2-A;
DE AltName: Full=xPABPII-A;
GN Name=pabpn1-a; Synonyms=pabpii;
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:0000305, ECO:0000312|EMBL:AAG36902.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:11677061};
RX PubMed=11677061; DOI=10.1016/s0925-4773(01)00514-7;
RA Kim J., Choi S.C., Chang J.Y., Han J.K.;
RT "Poly(A) binding protein II in Xenopus laevis is expressed in developing
RT brain and pancreas.";
RL Mech. Dev. 109:111-114(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAR26262.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Tail bud {ECO:0000269|PubMed:15083517};
RX PubMed=15083517; DOI=10.1002/gene.20015;
RA Good P.J., Abler L., Herring D., Sheets M.D.;
RT "Xenopus embryonic poly(A) binding protein 2 (ePABP2) defines a new family
RT of cytoplasmic poly(A) binding proteins expressed during the early stages
RT of vertebrate development.";
RL Genesis 38:166-175(2004).
RN [3] {ECO:0000312|EMBL:AAH73657.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH73657.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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:0000269|PubMed:11677061,
CC ECO:0000269|PubMed:15083517}. Cytoplasm {ECO:0000250|UniProtKB:Q86U42}.
CC Note=Shuttles between the nucleus and the cytoplasm but predominantly
CC found in the nucleus. {ECO:0000250|UniProtKB:Q86U42}.
CC -!- TISSUE SPECIFICITY: Shows dynamic spatial expression throughout
CC development. First expressed in the animal pole region of the egg and
CC this pattern persists through to the blastula stage. In gastrula and
CC neurula embryos, expressed mainly in ectodermal, neural and epidermal
CC regions. Neural tissue-specific expression pattern persists into
CC tailbud stage when expression is localized to the brain and spinal
CC cord. At early tadpole stage, expression becomes gradually confined to
CC the specific vesicle regions of the developing brain. At stage 39,
CC expressed in the telencephalon and mesencephalon regions of the brain.
CC Also detected in the eye and olfactory pit at the tadpole stage.
CC Expressed during gut endoderm development. At stage 35, expressed
CC exclusively in the anterior portion of the gut endoderm, which includes
CC the prospective liver, stomach and pancreas. As development proceeds,
CC expression becomes restricted to the pancreas, and by stage 46/47 (the
CC seventh day of development) expression is localized exclusively to the
CC pancreas. Expressed in most adult tissues.
CC {ECO:0000269|PubMed:11677061, ECO:0000269|PubMed:15083517}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at relatively constant levels throughout development.
CC {ECO:0000269|PubMed:11677061, ECO:0000269|PubMed:15083517}.
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; AF257236; AAG36902.1; -; mRNA.
DR EMBL; AY382836; AAR26262.1; -; mRNA.
DR EMBL; BC073657; AAH73657.1; -; mRNA.
DR RefSeq; NP_001082057.1; NM_001088588.1.
DR AlphaFoldDB; Q9DDY9; -.
DR SMR; Q9DDY9; -.
DR BioGRID; 99536; 1.
DR IntAct; Q9DDY9; 1.
DR DNASU; 398201; -.
DR GeneID; 398201; -.
DR KEGG; xla:398201; -.
DR CTD; 398201; -.
DR Xenbase; XB-GENE-6251817; pabpn1.S.
DR OMA; ISAEDQF; -.
DR OrthoDB; 1412946at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 398201; Expressed in gastrula 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; IDA: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-A"
FT /id="PRO_0000252082"
FT DOMAIN 163..240
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..106
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 33..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 32449 MW; 319E1235DF4B33E3 CRC64;
MAAVSSVASL RGADYENGLR GVAGPSDGGQ DPGEDDPMGR GTLDLEMELL EQGRRSRRVG
GRTTPGRRSG GRGGSGGGGA GGLEELEDEE LEEEEPGELT GDQTIEDPEL EAIKARVREM
EEEAEKLKEL QNEVEKQMNM SPPPGNAGPV IMSVEEKMEA DARSIYVGNV DYGATAEELE
AHFHGCGSVN RVTILCDKFT GHPKGFAYIE FCDKESVRTS LALDESLFRG RQIKVVPKRT
NRPGISTTDR GFPRARYRAR ASSYSSRSRF YSGYTPRPRG RVYRGRARAT SWYTPY
