GLD2_RAT
ID GLD2_RAT Reviewed; 484 AA.
AC Q5U315;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Poly(A) RNA polymerase GLD2 {ECO:0000305};
DE EC=2.7.7.19;
DE AltName: Full=PAP-associated domain-containing protein 4 {ECO:0000305};
DE AltName: Full=Terminal nucleotidyltransferase 2 {ECO:0000312|RGD:1306438};
GN Name=Tent2 {ECO:0000312|RGD:1306438};
GN Synonyms=Gld2 {ECO:0000312|RGD:1306438}, Palp4 {ECO:0000312|RGD:1306438};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC subfamily. {ECO:0000305}.
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DR EMBL; BC085771; AAH85771.1; -; mRNA.
DR RefSeq; NP_001008373.1; NM_001008372.1.
DR RefSeq; XP_008758861.1; XM_008760639.1.
DR PDB; 6LBK; X-ray; 2.50 A; A/B=131-484.
DR PDBsum; 6LBK; -.
DR AlphaFoldDB; Q5U315; -.
DR SMR; Q5U315; -.
DR STRING; 10116.ENSRNOP00000016135; -.
DR PaxDb; Q5U315; -.
DR GeneID; 361878; -.
DR KEGG; rno:361878; -.
DR UCSC; RGD:1306438; rat.
DR CTD; 167153; -.
DR RGD; 1306438; Tent2.
DR VEuPathDB; HostDB:ENSRNOG00000012099; -.
DR eggNOG; KOG2277; Eukaryota.
DR HOGENOM; CLU_046147_0_0_1; -.
DR InParanoid; Q5U315; -.
DR OMA; LNRKELC; -.
DR OrthoDB; 803033at2759; -.
DR PhylomeDB; Q5U315; -.
DR TreeFam; TF315661; -.
DR PRO; PR:Q5U315; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012099; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5U315; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:1990603; P:dark adaptation; IEP:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
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:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..484
FT /note="Poly(A) RNA polymerase GLD2"
FT /id="PRO_0000341551"
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 HELIX 155..167
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 171..189
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 232..248
FT /evidence="ECO:0007829|PDB:6LBK"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:6LBK"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 387..400
FT /evidence="ECO:0007829|PDB:6LBK"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:6LBK"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6LBK"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:6LBK"
FT TURN 441..444
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 448..467
FT /evidence="ECO:0007829|PDB:6LBK"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6LBK"
FT TURN 477..480
FT /evidence="ECO:0007829|PDB:6LBK"
SQ SEQUENCE 484 AA; 56007 MW; 149E8B0C49142A60 CRC64;
MFPNSILGRP PFTPTHQQHN NFFALSPTLY SHQQLIDAQF NFQNVDLSRA VSLQPLTYGT
VSPIQTSTSP LFRGRKRISD EKAFRLDGKR QRFHSPHQEP TIINQLVPLS GDRRYSMPPL
FHTHYVPEIV RCVPPLREIP LLEPREITLP EAKDKLSQQI LELFETCQQQ ASDLKKKELC
RAQLQREIQL LFPQSRLFLV GSSLNGFGAR SSDGDLCLVV KEEPCFFQVN QKTEARHILT
LVHKHFCTRL SGYIERPQLI RAKVPIVKFR DKVSCVEFDL NVNNTVGIRN TFLLRTYAYL
ENRVRPLVLV IKKWASHHEI NDASRGTLSS YSLVLMVLHY LQTLPEPILP SLQKIYPESF
STSVQLHLVH HAPCNVPPYL SKNESSLGDL LLGFLKYYAT EFDWNTQMIS VREAKAIPRP
DDMEWRNKYI CVEEPFDGTN TARAVHEKQK FDMIKDQFLK SWQRLKNKRD LNSVLPLRAA
TLKR
