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   27-MAR-2024, entry version 79.
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   AGR; Xenbase:XB-GENE-6256236; -.
DR   CTD; 446914; -.
DR   OMA; YATEFXP; -.
DR   OrthoDB; 1080369at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 446415; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; ISS:UniProtKB.
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   CDD; cd05402; NT_PAP_TUTase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF40; POLY(A) RNA POLYMERASE GLD2; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 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
//