GLD2_BOVIN
ID GLD2_BOVIN Reviewed; 484 AA.
AC Q2HJ44; Q1JPF9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Poly(A) RNA polymerase GLD2 {ECO:0000250|UniProtKB:Q6PIY7};
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:Q6PIY7};
DE AltName: Full=PAP-associated domain-containing protein 4 {ECO:0000250|UniProtKB:Q6PIY7};
GN Name=TENT2 {ECO:0000250|UniProtKB:Q6PIY7};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-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. Does not play a role in
CC replication-dependent histone mRNA degradation. Adds a single
CC nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes
CC and prolongs the activity of some but not all miRNAs.
CC {ECO:0000250|UniProtKB:Q6PIY7}.
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:0000250|UniProtKB:Q6PIY7};
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: Interacts with CPEB1, CPEB2, CPSF1 and PABPC1.
CC {ECO:0000250|UniProtKB:Q91YI6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91YI6}. Nucleus
CC {ECO:0000250|UniProtKB:Q91YI6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2HJ44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2HJ44-2; Sequence=VSP_034322, VSP_034323;
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC subfamily. {ECO:0000305}.
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DR EMBL; BT025394; ABF57350.1; -; mRNA.
DR EMBL; BC113319; AAI13320.1; -; mRNA.
DR RefSeq; NP_001039826.1; NM_001046361.1. [Q2HJ44-1]
DR RefSeq; XP_005211397.1; XM_005211340.2. [Q2HJ44-1]
DR RefSeq; XP_005211398.1; XM_005211341.3. [Q2HJ44-1]
DR RefSeq; XP_005211399.1; XM_005211342.3. [Q2HJ44-1]
DR RefSeq; XP_015328524.1; XM_015473038.1. [Q2HJ44-1]
DR AlphaFoldDB; Q2HJ44; -.
DR SMR; Q2HJ44; -.
DR STRING; 9913.ENSBTAP00000008885; -.
DR PaxDb; Q2HJ44; -.
DR PRIDE; Q2HJ44; -.
DR Ensembl; ENSBTAT00000008885; ENSBTAP00000008885; ENSBTAG00000006751. [Q2HJ44-1]
DR Ensembl; ENSBTAT00000048886; ENSBTAP00000045850; ENSBTAG00000006751. [Q2HJ44-2]
DR GeneID; 533862; -.
DR KEGG; bta:533862; -.
DR CTD; 167153; -.
DR VEuPathDB; HostDB:ENSBTAG00000006751; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156640; -.
DR HOGENOM; CLU_046147_0_0_1; -.
DR InParanoid; Q2HJ44; -.
DR OMA; LNRKELC; -.
DR OrthoDB; 803033at2759; -.
DR TreeFam; TF315661; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000006751; Expressed in neutrophil and 110 other tissues.
DR ExpressionAtlas; Q2HJ44; differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
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:0031123; P:RNA 3'-end processing; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Magnesium; Manganese;
KW Metal-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..484
FT /note="Poly(A) RNA polymerase GLD2"
FT /id="PRO_0000341548"
FT DOMAIN 386..440
FT /note="PAP-associated"
FT MOTIF 76..92
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIY7"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIY7"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIY7"
FT VAR_SEQ 157..163
FT /note="SQQILEL -> NKRTLTW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_034322"
FT VAR_SEQ 164..484
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_034323"
SQ SEQUENCE 484 AA; 56051 MW; EA2345615C844818 CRC64;
MFPNSILGRP PFTPNHQQHN NFFALSPSLY SHQQLIDAQF SFHNADLSRA VSLQQLTYGN
VSPIQTSTSP LFRGRKRLSD EKNLPLDGKR QRFHSPHQEP TIVNHIVPLS DERRYSMSPL
FHTHYVPDIV RCVPPFREIS ILEPREITLP EAKDKLSQQI LELFEACQQQ VSDLKKKELC
RTELQREIQL LFPQSRLFLV GSSLNGFGTR SSDGDLCLVV KEEPCFFQVN QKTEARHILT
LVHKHFCTRL SGYIERPQLI RAKVPIVKFR DKVSCVEFDL NVNNIVGIRN TFLLRTYAYL
ENRVRPLVLV IKKWASHHDI NDASRGTLSS YSLVLMVLHY LQTLPEPILP SIQKIYPESF
SPSIQLHLVH QAPCNVPPYL SKNESNLGDL LLGFLKYYAT EFDWNSQMIS VREAKAIPRP
DGIEWRNKYI CVEEPFDGTN TARAVHEKQK FDMIKDQFLK SWHRLKNRKD LNSILPLRAA
ILKR
