GLD2A_XENLA
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 03-AUG-2022, entry version 64.
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 CTD; 447753; -.
DR Xenbase; XB-GENE-1217415; tent2.S.
DR OMA; LNRKELC; -.
DR OrthoDB; 803033at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 447753; 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; 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 GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB.
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 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
