ID PAPD5_MOUSE Reviewed; 633 AA.
AC Q68ED3; A6H635; Q8C0K6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Terminal nucleotidyltransferase 4B {ECO:0000305};
DE AltName: Full=Non-canonical poly(A) RNA polymerase PAPD5;
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:Q8NDF8};
DE AltName: Full=PAP-associated domain-containing protein 5;
DE AltName: Full=Terminal guanylyltransferase {ECO:0000305};
DE EC=2.7.7.- {ECO:0000250|UniProtKB:Q8NDF8};
DE AltName: Full=Terminal uridylyltransferase 3;
DE Short=TUTase 3;
DE AltName: Full=Topoisomerase-related function protein 4-2;
DE Short=TRF4-2 {ECO:0000250|UniProtKB:Q8NDF8};
GN Name=Tent4b {ECO:0000250|UniProtKB:Q8NDF8};
GN Synonyms=Papd5 {ECO:0000312|MGI:MGI:1917820};
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Terminal nucleotidyltransferase that catalyzes preferentially
CC the transfer 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. Doesn't need a cofactor for
CC polyadenylation activity (in vitro). Plays a role in replication-
CC dependent histone mRNA degradation, probably through terminal
CC uridylation of mature histone mRNAs. May play a role in sister
CC chromatid cohesion (By similarity). {ECO:0000250|UniProtKB:Q8NDF8}.
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:Q8NDF8};
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 nucleolar 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. {ECO:0000250|UniProtKB:Q8NDF8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NDF8}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q8NDF8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8NDF8}. Note=Predominantly expressed in the
CC cytoplasm. {ECO:0000250|UniProtKB:Q8NDF8}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27158.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK030850; BAC27158.1; ALT_INIT; mRNA.
DR EMBL; AK077553; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC080314; AAH80314.1; -; mRNA.
DR EMBL; BC144796; AAI44797.1; -; mRNA.
DR EMBL; BC145737; AAI45738.1; -; mRNA.
DR RefSeq; NP_001157969.1; NM_001164497.1.
DR RefSeq; NP_001157970.1; NM_001164498.1.
DR RefSeq; NP_001157971.1; NM_001164499.1.
DR AlphaFoldDB; Q68ED3; -.
DR SMR; Q68ED3; -.
DR BioGRID; 229550; 2.
DR ELM; Q68ED3; -.
DR IntAct; Q68ED3; 1.
DR STRING; 10090.ENSMUSP00000112766; -.
DR iPTMnet; Q68ED3; -.
DR PhosphoSitePlus; Q68ED3; -.
DR EPD; Q68ED3; -.
DR jPOST; Q68ED3; -.
DR MaxQB; Q68ED3; -.
DR PaxDb; 10090-ENSMUSP00000112766; -.
DR ProteomicsDB; 288056; -.
DR Pumba; Q68ED3; -.
DR GeneID; 214627; -.
DR KEGG; mmu:214627; -.
DR AGR; MGI:1917820; -.
DR CTD; 64282; -.
DR MGI; MGI:1917820; Tent4b.
DR eggNOG; KOG1906; Eukaryota.
DR InParanoid; Q68ED3; -.
DR OrthoDB; 21395at2759; -.
DR PhylomeDB; Q68ED3; -.
DR BRENDA; 2.7.7.19; 3474.
DR BioGRID-ORCS; 214627; 18 hits in 79 CRISPR screens.
DR ChiTaRS; Tent4b; mouse.
DR PRO; PR:Q68ED3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q68ED3; Protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031499; C:TRAMP complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; 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:1990817; F:poly(A) RNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0033500; P:carbohydrate homeostasis; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; ISO:MGI.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0043634; P:polyadenylation-dependent ncRNA catabolic process; ISO:MGI.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
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:0006364; P:rRNA processing; 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 InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; POLY(A) RNA POLYMERASE; 1.
DR PANTHER; PTHR23092:SF51; TERMINAL NUCLEOTIDYLTRANSFERASE 4B; 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; DNA-binding;
KW DNA-directed DNA polymerase; Isopeptide bond; Magnesium; Manganese;
KW Metal-binding; Mitosis; mRNA processing; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; rRNA processing; Transferase;
KW Ubl conjugation.
FT CHAIN 1..633
FT /note="Terminal nucleotidyltransferase 4B"
FT /id="PRO_0000120311"
FT DOMAIN 322..382
FT /note="PAP-associated"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 618..624
FT /note="Basic, involved in binding of the RNA primer"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 531
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDF8"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDF8"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDF8"
FT CROSSLNK 587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDF8"
FT CONFLICT 466
FT /note="D -> Y (in Ref. 1; BAC27158)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="N -> S (in Ref. 1; BAC27158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 69704 MW; 49D474538E54FC93 CRC64;
MFRSGERPLG GLAVPAEQRD FLPLETTNNN NNHHQPAAWA RRASAGPSAS PVPSAPSSPR
PAAALPASES TDPASGSSNK RKRDNKASTY GLNYSLLQPS GGRAAGGGRA DGGGGVYSGT
PWKRRNYNQG VVGLHEEISD FYEYMSPRPE EEKMRMEVVS RIESVIKELW PSADVQIFGS
FKTGLYLPTS DIDLVVFGKW ENLPLWTLEE ALRKHKVADE DSVKVLDKAT VPIIKLTDSF
TEVKVDISFN VQNGVRAADL IKDFTKKYPV LPYLVLVLKQ FLLQRDLNEV FTGGIGSYSL
FLMAVSFLQL HPREDACIPN TNYGVLLIEF FELYGRHFNY LKTGIRIKDG GSYVAKDEVQ
KNMLDGYRPS MLYIEDPLQP GNDVGRSSYG AMQVKQAFDY AYVVLSHAVS PIAKYYPNNE
TESILGRIIR VTDEVATYRD WISKQWGLQN RPEPSCNGNG VTLIVDTQQL DKCNNNLSEE
KEALGKCRSN ASEPLSKHSS NSSSGPVSSS SATQSSSSDV DSDATPCKTP KQLLCRPPTV
TRVGSQDVSL EVSQAVGKMQ STQTTNTPNN ANKSQHGSAR LFRSSSKGFQ GTAQTSHGAL
MTSKQHQGKS NTQYYHGKKR RHKRDAPLSE LCR
//
