PAPD7_MOUSE
ID PAPD7_MOUSE Reviewed; 542 AA.
AC Q6PB75; G3X948;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Terminal nucleotidyltransferase 4A {ECO:0000305};
DE AltName: Full=DNA polymerase sigma;
DE AltName: Full=Non-canonical poly(A) RNA polymerase PAPD7;
DE EC=2.7.7.19;
DE AltName: Full=PAP-associated domain-containing protein 7;
DE AltName: Full=TRAMP-like complex polyadenylate polymerase;
DE AltName: Full=Terminal guanylyltransferase {ECO:0000305};
DE EC=2.7.7.- {ECO:0000250|UniProtKB:Q5XG87};
GN Name=Tent4a {ECO:0000250|UniProtKB:Q5XG87};
GN Synonyms=Papd7 {ECO:0000312|MGI:MGI:2682295}, Pols;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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: Terminal nucleotidyltransferase that catalyzes preferentially
CC the transfert of ATP and GTP on RNA 3' poly(A) tail creating a
CC heterogeneous 3' poly(A) tail leading to mRNAs stabilization by
CC protecting mRNAs from active deadenylation (By similarity). Also
CC functions as a catalytic subunit of a TRAMP-like complex which has a
CC poly(A) RNA polymerase activity and is involved in a post-
CC transcriptional quality control mechanism. Polyadenylation with short
CC oligo(A) tails is required for the degradative activity of the exosome
CC on several of its nuclear RNA substrates. Has no terminal
CC uridylyltransferase activity, and does not play a role in replication-
CC dependent histone mRNA degradation via uridylation (By similarity).
CC {ECO:0000250|UniProtKB:Q5XG87}.
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 nuclear TRAMP-like complex, an ATP-dependent
CC exosome regulatory complex consisting of a helicase (MTREX), an
CC oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific
CC RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes
CC exist with specific compositions and are associated with nuclear, or
CC nucleolar RNA exosomes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC {ECO:0000250}. Note=Excluded from nucleolus, weak staining detected in
CC the cytoplasm. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have DNA polymerase activity.
CC {ECO:0000305}.
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DR EMBL; AC122484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466563; EDL37014.1; -; Genomic_DNA.
DR EMBL; BC059846; AAH59846.1; -; mRNA.
DR RefSeq; NP_941002.2; NM_198600.2.
DR AlphaFoldDB; Q6PB75; -.
DR SMR; Q6PB75; -.
DR BioGRID; 229130; 1.
DR STRING; 10090.ENSMUSP00000040757; -.
DR iPTMnet; Q6PB75; -.
DR PhosphoSitePlus; Q6PB75; -.
DR PaxDb; Q6PB75; -.
DR PRIDE; Q6PB75; -.
DR ProteomicsDB; 294328; -.
DR Antibodypedia; 22404; 156 antibodies from 22 providers.
DR DNASU; 210106; -.
DR Ensembl; ENSMUST00000044081; ENSMUSP00000040757; ENSMUSG00000034575.
DR Ensembl; ENSMUST00000223344; ENSMUSP00000152244; ENSMUSG00000034575.
DR GeneID; 210106; -.
DR KEGG; mmu:210106; -.
DR UCSC; uc007rch.2; mouse.
DR CTD; 11044; -.
DR MGI; MGI:2682295; Tent4a.
DR VEuPathDB; HostDB:ENSMUSG00000034575; -.
DR eggNOG; KOG1906; Eukaryota.
DR GeneTree; ENSGT00940000157811; -.
DR HOGENOM; CLU_013572_3_0_1; -.
DR InParanoid; Q6PB75; -.
DR OMA; KWGSRVH; -.
DR PhylomeDB; Q6PB75; -.
DR TreeFam; TF313939; -.
DR BioGRID-ORCS; 210106; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Papd7; mouse.
DR PRO; PR:Q6PB75; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6PB75; protein.
DR Bgee; ENSMUSG00000034575; Expressed in animal zygote and 227 other tissues.
DR ExpressionAtlas; Q6PB75; baseline and differential.
DR Genevisible; Q6PB75; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031499; C:TRAMP complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070568; F:guanylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0071076; P:RNA 3' uridylation; ISS:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; IEA:InterPro.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR040137; TENT4A.
DR InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; PTHR23092; 1.
DR PANTHER; PTHR23092:SF24; PTHR23092:SF24; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..542
FT /note="Terminal nucleotidyltransferase 4A"
FT /id="PRO_0000120309"
FT DOMAIN 178..238
FT /note="PAP-associated"
FT REGION 350..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 297
FT /note="W -> R (in Ref. 3; AAH59846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 60027 MW; 9B9DC7D11F886045 CRC64;
MSPCPEEAAM RREVVKRIET VVKDLWPTAD VQIFGSFSTG LYLPTSDIDL VVFGKWERPP
LQLLEQALRK HNVAEPCSIK VLDKATVPII KLTDQETEVK VDISFNMETG VRAAEFIKNY
MKKYSLLPYL ILVLKQFLLQ RDLNEVFTGG ISSYSLILMA ISFLQLHPRI DARRADENLG
MLLVEFFELY GRNFNYLKTG IRIKEGGAYI AKEEIMKAMT SGYRPSMLCI EDPLLPGNDV
GRSSYGAMQV KQVFDYAYIV LSHAVSPLAR SYPNRDSEST LGRIIKVTQE VIDYRRWIKE
KWGSRILPSP DLDNRIKIKE RITTCNGEQM QSREPSSPYT QRLTLSLSSP QLLSSGSSAS
SVSSLSGSDI DSDTPPCTTP SVYQFSLQAP TTLMASLPTA LPMPSSKPQP AASRTLIMTT
NNQTRVTIPP PTLGVAPVPC RQAGVDGTTS LKAVHSVTSP AIPSASPNPL SSPHLYHKQH
NGMKLSMKGS HNHTQGGGYS SVGSGAVRPP VGNRGHHQYN RTGWRRKKHA HTRDSLPVSL
SR
