ID GLD2_XENTR Reviewed; 528 AA. AC Q0VFA3; A4IIZ6; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=Poly(A) RNA polymerase GLD2; DE EC=2.7.7.19; DE AltName: Full=PAP-associated domain-containing protein 4; GN Name=tent2; Synonyms=gld2, papd4; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. 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 -!- 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 -!- 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 rbm9 and sympk (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q0VFA3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q0VFA3-2; Sequence=VSP_034327; CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC118909; AAI18910.1; -; mRNA. DR EMBL; BC136215; AAI36216.1; -; mRNA. DR RefSeq; NP_001072915.1; NM_001079447.1. [Q0VFA3-1] DR AlphaFoldDB; Q0VFA3; -. DR SMR; Q0VFA3; -. DR STRING; 8364.ENSXETP00000033871; -. DR PaxDb; 8364-ENSXETP00000062194; -. DR DNASU; 780377; -. DR GeneID; 780377; -. DR KEGG; xtr:780377; -. DR AGR; Xenbase:XB-GENE-1217408; -. DR CTD; 167153; -. DR Xenbase; XB-GENE-1217408; tent2. DR eggNOG; KOG2277; Eukaryota. DR InParanoid; Q0VFA3; -. DR OrthoDB; 1080369at2759; -. DR TreeFam; TF315661; -. DR Proteomes; UP000008143; Chromosome 1. 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 2: Evidence at transcript 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..528 FT /note="Poly(A) RNA polymerase GLD2" FT /id="PRO_0000341555" FT DOMAIN 428..481 FT /note="PAP-associated" FT REGION 1..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 99..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..41 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 259 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT VAR_SEQ 35..39 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_034327" SQ SEQUENCE 528 AA; 60540 MW; C7324D94F2546469 CRC64; MYPNSPSQGR IPLPLPCEQQ QPPLEQSQEQ PLQPQPLQPQ QASGYLSKLP VSVAPELLSP EQFIQASINL HNNVNFARML MNANLLAVPP VSPPPWSYRD QSPLISPASP SSSFQNRKRR SDEGNIAYDV KRQKFQSPQE QTVNHQAVPL RGDLGCSYPG SPAFPLLQSP SPPVLKGHVP NSGECWLYDH VDTTLPVAKD KLSKQILELF QALQQQVCDL KKKDICRAEL QREIQQIFPQ SRLYLVGSSL NGFGTRSSDA DLCLVLKDEP MNQHTEARHI LSLLHKHFYT RLSYIERPQF IKAKVPIVKF RDKVSGAEFD LNVNNVVGIR NTFLLRTYAY IENRVRPLVL VIKMWANYHG LNDASRGTLS SYTLVLMALH YLQTLPEPII PSLQKKYPEC FDSTMQLHLV HHAPRNIPKY LSKNETPLGD LLLGFLKYFA IEFDWSKDII SVREAKALPR SDDYEWRNKF ICVEEPYDRT NTARAVYERQ KFDMIRAEFL RAWVALRDNR DLYSLLPWKG IMKKMNSL //