GLD2B_XENLA
ID GLD2B_XENLA Reviewed; 509 AA.
AC Q6DFA8; A4F5G9; Q68PF4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Poly(A) RNA polymerase GLD2-B {ECO:0000305};
DE Short=xGLD-2;
DE EC=2.7.7.19;
DE AltName: Full=PAP-associated domain-containing protein 4-B;
GN Name=tent2-b {ECO:0000250|UniProtKB:Q6PIY7}; Synonyms=gld2-b, papd4-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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH CPEB1; CPSF1 AND SYMPK, AND MUTAGENESIS OF ASP-242.
RC TISSUE=Oocyte;
RX PubMed=15550246; DOI=10.1016/j.cell.2004.10.029;
RA Barnard D.C., Ryan K., Manley J.L., Richter J.D.;
RT "Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic
RT polyadenylation.";
RL Cell 119:641-651(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH RBFOX2.
RC TISSUE=Oocyte;
RX PubMed=18177378; DOI=10.1111/j.1742-4658.2007.06216.x;
RA Papin C., Rouget C., Mandart E.;
RT "Xenopus Rbm9 is a novel interactor of XGld2 in the cytoplasmic
RT polyadenylation complex.";
RL FEBS J. 275:490-503(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15987818; DOI=10.1261/rna.2630205;
RA Rouhana L., Wang L., Buter N., Kwak J.E., Schiltz C.A., Gonzalez T.,
RA Kelley A.E., Landry C.F., Wickens M.;
RT "Vertebrate GLD2 poly(A) polymerases in the germline and the brain.";
RL RNA 11:1117-1130(2005).
RN [5]
RP FUNCTION, AND INTERACTION WITH PARN.
RX PubMed=17052452; DOI=10.1016/j.molcel.2006.08.016;
RA Kim J.H., Richter J.D.;
RT "Opposing polymerase-deadenylase activities regulate cytoplasmic
RT polyadenylation.";
RL Mol. Cell 24:173-183(2006).
RN [6]
RP INTERACTION WITH PABPC1.
RX PubMed=17938241; DOI=10.1101/gad.1593007;
RA Kim J.H., Richter J.D.;
RT "RINGO/cdk1 and CPEB mediate poly(A) tail stabilization and translational
RT regulation by ePAB.";
RL Genes Dev. 21:2571-2579(2007).
RN [7]
RP INDUCTION.
RX PubMed=17164476; DOI=10.1261/rna.333507;
RA Rouhana L., Wickens M.;
RT "Autoregulation of GLD-2 cytoplasmic poly(A) polymerase.";
RL RNA 13:188-199(2007).
CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP
CC monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In
CC contrast to the canonical nuclear poly(A) RNA polymerase, it only adds
CC poly(A) to selected cytoplasmic mRNAs during oocyte maturation. Plays a
CC central role during oocyte maturation by mediating polyadenylation of
CC dormant mRNAs, which contain 5'AAUAAA-3' sequence in their 3'-UTR. In
CC immature oocytes, polyadenylation of poly(A) tails is counteracted by
CC the ribonuclease parn. During maturation parn is excluded from the
CC ribonucleoprotein complex, allowing poly(A) elongation and activation
CC of mRNAs. May not play a role in replication-dependent histone mRNA
CC degradation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15550246,
CC ECO:0000269|PubMed:15987818, ECO:0000269|PubMed:17052452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:15987818};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of a complex at least composed of cpeb1, cpsf1,
CC tent2/gld2, pabpc1/ePAB, parn and sympk. Following oocyte maturation,
CC parn is expelled from the complex. Interacts with rbfox2. Interacts
CC with sympk (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15550246,
CC ECO:0000269|PubMed:15987818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6DFA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DFA8-2; Sequence=VSP_034326;
CC -!- DEVELOPMENTAL STAGE: Present in oocytes. {ECO:0000269|PubMed:15987818}.
CC -!- INDUCTION: Autoregulated; mediates its own polyadenylation and
CC translational activation during frog oocyte maturation.
CC {ECO:0000269|PubMed:17164476}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC subfamily. {ECO:0000305}.
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DR EMBL; AY655140; AAT98005.1; -; mRNA.
DR EMBL; AM419010; CAL91353.1; -; mRNA.
DR EMBL; BC076832; AAH76832.1; -; mRNA.
DR RefSeq; NP_001086580.1; NM_001093111.1. [Q6DFA8-1]
DR RefSeq; NP_001087078.1; NM_001093609.1.
DR AlphaFoldDB; Q6DFA8; -.
DR SMR; Q6DFA8; -.
DR IntAct; Q6DFA8; 1.
DR MINT; Q6DFA8; -.
DR MaxQB; Q6DFA8; -.
DR DNASU; 446415; -.
DR GeneID; 446415; -.
DR GeneID; 446914; -.
DR KEGG; xla:446415; -.
DR CTD; 446415; -.
DR CTD; 446914; -.
DR Xenbase; XB-GENE-6256236; tent2.L.
DR OMA; YATEFXP; -.
DR OrthoDB; 803033at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446415; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034062; F:5'-3' RNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0070566; F:adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000626; P:negative regulation of miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0043489; P:RNA stabilization; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Differentiation; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Oogenesis; Reference proteome; Transferase.
FT CHAIN 1..509
FT /note="Poly(A) RNA polymerase GLD2-B"
FT /id="PRO_0000341554"
FT DOMAIN 409..462
FT /note="PAP-associated"
FT REGION 88..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 56..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18177378"
FT /id="VSP_034326"
FT MUTAGEN 242
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15550246"
FT CONFLICT 28
FT /note="S -> T (in Ref. 1; AAT98005)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="G -> S (in Ref. 1; AAT98005)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="K -> R (in Ref. 1; AAT98005)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="I -> V (in Ref. 1; AAT98005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 58235 MW; 8FB3569E258252D7 CRC64;
MYPNSPSLGR IPLPLPCARQ QQTSAYLSKV PVSVAPDLLS PEQFFQASLN IHKNANLPRL
LMNGNVLTVP PLSSPPWSYL NHSPLISPGS PPSSFQNRKR RSDEGNSPYD VKRQRFQSPQ
EQTVNHQAVP LRGDIRCSYP GSPAFPLLQS PSPPVLKGHS SNSGDCWLYD HIDTTLPVAK
DKLSKQILDL FQALQQQVCD LKKKDICRAE LQREIQQIFP QSRLYLVGSS LNGFGIRSSD
ADLCLVLKEE PMNQNTEARH ILSLLHKHFY TRLSYIERPQ FIRAKVPIVK FRDKVSGAEF
DLNVNNVVGI RNTFLLRTYA YLDKRVRPLV LVIKKWANHH GINDASRGTL SSYTIVLMVL
HYLQTLPEPI LPSLQKKYPE CFDRTMQLHL VHQAPRNIPQ FLSKNETPLG DLLLGFLKYF
AVEFDWSKDI ISLREAKALP RTDDYEWRNK YICVEEPFDG SNTARAVYEK QKFDLIRAEF
LKAWVALRDN RDLYSLLPVK GIMKKMHSL
