ID   GLD2A_XENLA             Reviewed;         509 AA.
AC   Q641A1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Poly(A) RNA polymerase GLD2-A {ECO:0000305};
DE            EC=2.7.7.19;
DE   AltName: Full=PAP-associated domain-containing protein 4-A;
GN   Name=tent2-a; Synonyms=gld2-a, papd4-a;
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 [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH SYMPK.
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   [3]
RP   FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   INTERACTION WITH CPEB1 AND CPSF1, AND MUTAGENESIS OF ASP-242.
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).
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,
CC       ECO:0000269|PubMed:15987818}.
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 and sympk.
CC       {ECO:0000269|PubMed:15550246, ECO:0000269|PubMed:15987818}.
CC   -!- INTERACTION:
CC       Q641A1; Q91808: msi1.L; NbExp=2; IntAct=EBI-11474136, EBI-11474081;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15987818}.
CC   -!- DEVELOPMENTAL STAGE: Present in oocytes. {ECO:0000269|PubMed:15987818}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC082438; AAH82438.1; -; mRNA.
DR   RefSeq; NP_001087892.1; NM_001094423.1.
DR   AlphaFoldDB; Q641A1; -.
DR   SMR; Q641A1; -.
DR   IntAct; Q641A1; 5.
DR   DNASU; 447753; -.
DR   GeneID; 447753; -.
DR   KEGG; xla:447753; -.
DR   AGR; Xenbase:XB-GENE-1217415; -.
DR   Xenbase; XB-GENE-1217415; tent2.S.
DR   OMA; RTYAYAD; -.
DR   OrthoDB; 1080369at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 447753; 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:0031124; P:mRNA 3'-end processing; ISS:UniProtKB.
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   ATP-binding; Cytoplasm; Developmental protein; Differentiation; Magnesium;
KW   Manganese; Metal-binding; mRNA processing; Nucleotide-binding; Oogenesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..509
FT                   /note="Poly(A) RNA polymerase GLD2-A"
FT                   /id="PRO_0000341553"
FT   DOMAIN          409..462
FT                   /note="PAP-associated"
FT   REGION          88..107
FT                   /note="Disordered"
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   MUTAGEN         242
FT                   /note="D->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:15987818"
SQ   SEQUENCE   509 AA;  57982 MW;  F97C98C4BF287EF6 CRC64;
     MYPNSPSLGR IPLPLPCEQQ QQASGYSDKL PVSAAPELLS PEQFIQASLN IQKHANLSRM
     LMNGNVLTVP PVSSPPWAYL NHSPLISPGS PSSSFQNRKR RSDEGNVSYD VKRQRFHSPQ
     EQTVNHQAVP LRGDLRCSYP GSPAFPLLQS PSPPVLKEHV SNSGDCWLYD HIDTTLPVAE
     DKLSQQILDL FQALQQQVCD IKKKDICRAE LQREIQQIFP QSRLYLVGSS LNGFGTRISD
     ADLCLVLKEE PMNQHTEATQ ILGLLHKLFY TRLSYIERLQ FIRAKVPIVK FRDKVSGAEF
     DLNVNNVVGI RNTFLLRTYA YLESRVRPLV LVIKKWANHH GINDASRGTL SSYTLVLMVL
     HYLQTLPEPI LPSLQKKYPE CFDLSMQLNL VHHAPRNIPP YLSKNETPLG DLLLGFLKYF
     AVEFDWSKDI ISVREGKALP RSDDYLWRNK YICVEEPFDG TNTARAVYER QKFDMIRAEF
     LKAWGALRDD RDLYSLLPVT AIVKKMNSL
//