GLD2_XENTR
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 03-AUG-2022, entry version 84.
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}.
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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; Q0VFA3; -.
DR PRIDE; Q0VFA3; -.
DR DNASU; 780377; -.
DR GeneID; 780377; -.
DR KEGG; xtr:780377; -.
DR CTD; 167153; -.
DR Xenbase; XB-GENE-1217408; tent2.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; Q0VFA3; -.
DR OMA; YATEFXP; -.
DR OrthoDB; 803033at2759; -.
DR TreeFam; TF315661; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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:0031123; P:RNA 3'-end processing; IBA:GO_Central.
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 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
