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Terminal uridylyltransferase 4 (TUTase 4) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 11)

 TUT4_HUMAN              Reviewed;        1644 AA.
Q5TAX3; A2RRP0; B7Z8J5; D3DQ35; Q12764; Q5TAX2; Q5TAX4; Q86XZ3;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
05-DEC-2018, entry version 131.
RecName: Full=Terminal uridylyltransferase 4 {ECO:0000305};
Short=TUTase 4;
EC=2.7.7.52 {ECO:0000269|PubMed:19703396};
AltName: Full=Zinc finger CCHC domain-containing protein 11;
Name=TUT4 {ECO:0000312|HGNC:HGNC:28981};
Synonyms=KIAA0191, ZCCHC11 {ECO:0000312|HGNC:HGNC:28981};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1644.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[6]
FUNCTION, INTERACTION WITH T2BP, AND SUBCELLULAR LOCATION.
PubMed=16643855; DOI=10.1016/j.bbrc.2006.04.006;
Minoda Y., Saeki K., Aki D., Takaki H., Sanada T., Koga K.,
Kobayashi T., Takaesu G., Yoshimura A.;
"A novel Zinc finger protein, ZCCHC11, interacts with TIFA and
modulates TLR signaling.";
Biochem. Biophys. Res. Commun. 344:1023-1030(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[8]
ABSENCE OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
PubMed=18172165; DOI=10.1101/gad.1622708;
Mullen T.E., Marzluff W.F.;
"Degradation of histone mRNA requires oligouridylation followed by
decapping and simultaneous degradation of the mRNA both 5' to 3' and
3' to 5'.";
Genes Dev. 22:50-65(2008).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
LIN28A, AND MUTAGENESIS OF ASP-1011.
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
INTERACTION WITH LIN28A.
PubMed=22118463; DOI=10.1016/j.cell.2011.10.039;
Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J.,
Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.;
"Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct
mechanisms.";
Cell 147:1066-1079(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-156, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-1011.
PubMed=25480299; DOI=10.1016/j.cell.2014.10.055;
Lim J., Ha M., Chang H., Kwon S.C., Simanshu D.K., Patel D.J.,
Kim V.N.;
"Uridylation by TUT4 and TUT7 marks mRNA for degradation.";
Cell 159:1365-1376(2014).
[14]
FUNCTION.
PubMed=25979828; DOI=10.15252/embj.201590931;
Kim B., Ha M., Loeff L., Chang H., Simanshu D.K., Li S., Fareh M.,
Patel D.J., Joo C., Kim V.N.;
"TUT7 controls the fate of precursor microRNAs by using three
different uridylation mechanisms.";
EMBO J. 34:1801-1815(2015).
[15]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MOV10, AND
MUTAGENESIS OF ASP-1011.
PubMed=30122351; DOI=10.1016/j.cell.2018.07.022;
Warkocki Z., Krawczyk P.S., Adamska D., Bijata K., Garcia-Perez J.L.,
Dziembowski A.;
"Uridylation by TUT4/7 Restricts Retrotransposition of Human LINE-
1s.";
Cell 0:0-0(2018).
-!- FUNCTION: Uridylyltransferase that mediates the terminal
uridylation of mRNAs with short (less than 25 nucleotides) poly(A)
tails, hence facilitating global mRNA decay (PubMed:25480299).
Essential for both oocyte maturation and fertility. Through 3'
terminal uridylation of mRNA, sculpts, with TUT7, the maternal
transcriptome by eliminating transcripts during oocyte growth (By
similarity). Involved in microRNA (miRNA)-induced gene silencing
through uridylation of deadenylated miRNA targets. Also functions
as an integral regulator of microRNA biogenesis using 3 different
uridylation mechanisms (PubMed:25979828). Acts as a suppressor of
miRNA biogenesis by mediating the terminal uridylation of some
miRNA precursors, including that of let-7 (pre-let-7), miR107,
miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer
and undergo degradation. Degradation of pre-let-7 contributes to
the maintenance of embryonic stem (ES) cell pluripotency (By
similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA
that targets IL6 transcript. This abrogates the silencing of IL6
transcript, hence promoting cytokine expression (PubMed:19703396).
In the absence of LIN28A, TUT7 and TUT4 monouridylate group II
pre-miRNAs, which includes most of pre-let7 members, that shapes
an optimal 3' end overhang for efficient processing
(PubMed:25979828). Adds oligo-U tails to truncated pre-miRNAS with
a 5' overhang which may promote rapid degradation of non-
functional pre-miRNA species (PubMed:25979828). May also suppress
Toll-like receptor-induced NF-kappa-B activation via binding to
T2BP (PubMed:16643855). Does not play a role in replication-
dependent histone mRNA degradation (PubMed:18172165). Due to
functional redundancy between TUT4 and TUT7, the identification of
the specific role of each of these proteins is difficult
(PubMed:25979828, PubMed:25480299, PubMed:16643855,
PubMed:19703396, PubMed:18172165) (By similarity). TUT4 and TUT7
restrict retrotransposition of long interspersed element-1 (LINE-
1) in cooperation with MOV10 counteracting the RNA chaperonne
activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm
which inhibits initiation of reverse transcription once in the
nucleus, whereas uridylation by TUT4 destabilizes mRNAs in
cytoplasmic ribonucleoprotein granules (PubMed:30122351).
{ECO:0000250|UniProtKB:B2RX14, ECO:0000269|PubMed:16643855,
ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:25480299, ECO:0000269|PubMed:25979828,
ECO:0000269|PubMed:30122351}.
-!- CATALYTIC ACTIVITY:
Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine
ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:11128,
Rhea:RHEA-COMP:14648, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
ChEBI:CHEBI:83400, ChEBI:CHEBI:140627; EC=2.7.7.52;
Evidence={ECO:0000269|PubMed:19703396};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with LIN28A in the presence of pre-let-7 RNA
(PubMed:19703396, PubMed:22118463). Interacts with T2BP
(PubMed:16643855). Interacts with MOV10; the interaction IS RNA-
dependent (PubMed:30122351). {ECO:0000269|PubMed:16643855,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22118463,
ECO:0000269|PubMed:30122351}.
-!- INTERACTION:
Q96CG3:TIFA; NbExp=2; IntAct=EBI-1606425, EBI-740711;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16643855}.
Cytoplasm {ECO:0000269|PubMed:16643855,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:25480299}.
Cytoplasm, Cytoplasmic ribonucleoprotein granule
{ECO:0000269|PubMed:30122351}. Note=Mainly cytoplasmic
(PubMed:19703396, PubMed:25480299). Translocates into the
cytoplasm following treatment of the cell with LPS
(PubMed:16643855). Co-enriched in cytoplasmic foci with MOV10
(PubMed:30122351). {ECO:0000269|PubMed:30122351}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5TAX3-1; Sequence=Displayed;
Name=2;
IsoId=Q5TAX3-2; Sequence=VSP_038135, VSP_038136;
Note=No experimental confirmation available.;
-!- DOMAIN: Utilizes two multidomain functional modules during the
switch from monouridylation to oligouridylation. The catalytic
module (containing the 3 CCHC-type Zinc finger domains) is
essential for both activites while the Lin28-interacting module
(LIM) at the N-termail part is indispensable for oligouridylation.
{ECO:0000250|UniProtKB:B2RX14}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
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EMBL; AK303532; BAH13981.1; -; mRNA.
EMBL; AL138849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06778.1; -; Genomic_DNA.
EMBL; CH471059; EAX06780.1; -; Genomic_DNA.
EMBL; BC131734; AAI31735.1; -; mRNA.
EMBL; D83776; BAA12105.1; -; mRNA.
CCDS; CCDS30716.1; -. [Q5TAX3-1]
RefSeq; NP_001009881.1; NM_001009881.2.
RefSeq; NP_056084.1; NM_015269.2. [Q5TAX3-1]
UniGene; Hs.655407; -.
ProteinModelPortal; Q5TAX3; -.
SMR; Q5TAX3; -.
BioGrid; 116909; 23.
IntAct; Q5TAX3; 7.
STRING; 9606.ENSP00000257177; -.
iPTMnet; Q5TAX3; -.
PhosphoSitePlus; Q5TAX3; -.
BioMuta; ZCCHC11; -.
DMDM; 116242850; -.
EPD; Q5TAX3; -.
MaxQB; Q5TAX3; -.
PaxDb; Q5TAX3; -.
PeptideAtlas; Q5TAX3; -.
PRIDE; Q5TAX3; -.
ProteomicsDB; 64876; -.
ProteomicsDB; 64877; -. [Q5TAX3-2]
DNASU; 23318; -.
Ensembl; ENST00000371544; ENSP00000360599; ENSG00000134744. [Q5TAX3-1]
GeneID; 23318; -.
KEGG; hsa:23318; -.
UCSC; uc001ctx.3; human. [Q5TAX3-1]
CTD; 23318; -.
DisGeNET; 23318; -.
EuPathDB; HostDB:ENSG00000134744.13; -.
GeneCards; TUT4; -.
HGNC; HGNC:28981; TUT4.
HPA; HPA027412; -.
HPA; HPA027973; -.
MIM; 613692; gene.
neXtProt; NX_Q5TAX3; -.
OpenTargets; ENSG00000134744; -.
PharmGKB; PA134918178; -.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00940000156988; -.
InParanoid; Q5TAX3; -.
KO; K13291; -.
PhylomeDB; Q5TAX3; -.
TreeFam; TF315661; -.
BRENDA; 2.7.7.52; 2681.
Reactome; R-HSA-429947; Deadenylation of mRNA.
ChiTaRS; ZCCHC11; human.
GenomeRNAi; 23318; -.
PRO; PR:Q5TAX3; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134744; Expressed in 221 organ(s), highest expression level in kidney.
CleanEx; HS_ZCCHC11; -.
ExpressionAtlas; Q5TAX3; baseline and differential.
Genevisible; Q5TAX3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IDA:UniProtKB.
GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IDA:UniProtKB.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0001556; P:oocyte maturation; ISS:UniProtKB.
GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; ISS:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
GO; GO:0071076; P:RNA 3' uridylation; ISS:UniProtKB.
GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
InterPro; IPR002058; PAP_assoc.
InterPro; IPR002934; Polymerase_NTP_transf_dom.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01909; NTP_transf_2; 1.
Pfam; PF03828; PAP_assoc; 2.
Pfam; PF00098; zf-CCHC; 2.
SMART; SM00343; ZnF_C2HC; 3.
SUPFAM; SSF57756; SSF57756; 2.
PROSITE; PS50158; ZF_CCHC; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Magnesium;
Manganese; Metal-binding; Methylation; Nucleotidyltransferase;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
RNA-mediated gene silencing; Transferase; Zinc; Zinc-finger.
CHAIN 1 1644 Terminal uridylyltransferase 4.
/FTId=PRO_0000150970.
DOMAIN 628 678 PAP-associated 1.
DOMAIN 1184 1237 PAP-associated 2.
ZN_FING 304 334 Matrin-type. {ECO:0000255|PROSITE-
ProRule:PRU00130}.
ZN_FING 913 930 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1293 1310 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1357 1374 CCHC-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 901 1634 Sufficient for monouridylation activity.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 998 1001 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 1008 1011 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 1121 1125 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
COMPBIAS 1398 1483 Gln-rich.
COMPBIAS 1424 1598 Pro-rich.
METAL 1009 1009 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 1011 1011 Magnesium or manganese; catalytic.
{ECO:0000250}.
BINDING 1081 1081 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
BINDING 1103 1103 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
BINDING 1237 1237 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:B2RX14}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1624 1624 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:B2RX14}.
VAR_SEQ 685 719 RSLNSQLVYEYVVERFRAAYRYFACPQTKGGNKST -> LQ
PGRQEWKLCLKKKKKNSVKYTFIYEIQVSLFVI (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038135.
VAR_SEQ 720 1644 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038136.
VARIANT 796 796 D -> Y (in dbSNP:rs12127732).
/FTId=VAR_028402.
MUTAGEN 1011 1011 D->A: Loss of nucleotidyltransferase
activity and stabilization of pre-let-7
miRNAs. Abolishes inhibition of LIRE1
retrotransposition.
{ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:25480299,
ECO:0000269|PubMed:30122351}.
CONFLICT 1313 1313 S -> SS (in Ref. 4; AAI31735).
{ECO:0000305}.
SEQUENCE 1644 AA; 185166 MW; B7C88D7DCF0F3356 CRC64;
MEESKTLKSE NHEPKKNVIC EESKAVQVIG NQTLKARNDK SVKEIENSSP NRNSSKKNKQ
NDICIEKTEV KSCKVNAANL PGPKDLGLVL RDQSHCKAKK FPNSPVKAEK ATISQAKSEK
ATSLQAKAEK SPKSPNSVKA EKASSYQMKS EKVPSSPAEA EKGPSLLLKD MRQKTELQQI
GKKIPSSFTS VDKVNIEAVG GEKCALQNSP RSQKQQTCTD NTGDSDDSAS GIEDVSDDLS
KMKNDESNKE NSSEMDYLEN ATVIDESALT PEQRLGLKQA EERLERDHIF RLEKRSPEYT
NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE LRSLPPPSPA HLAALSVAVI
ELAKEHGITD DDLRVRQEIV EEMSKVITTF LPECSLRLYG SSLTRFALKS SDVNIDIKFP
PKMNHPDLLI KVLGILKKNV LYVDVESDFH AKVPVVVCRD RKSGLLCRVS AGNDMACLTT
DLLTALGKIE PVFIPLVLAF RYWAKLCYID SQTDGGIPSY CFALMVMFFL QQRKPPLLPC
LLGSWIEGFD PKRMDDFQLK GIVEEKFVKW ECNSSSATEK NSIAEENKAK ADQPKDDTKK
TETDNQSNAM KEKHGKSPLA LETPNRVSLG QLWLELLKFY TLDFALEEYV ICVRIQDILT
RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF RAAYRYFACP QTKGGNKSTV
DFKKREKGKI SNKKPVKSNN MATNGCILLG ETTEKINAER EQPVQCDEMD CTSQRCIIDN
NNLLVNELDF ADHGQDSSSL STSKSSEIEP KLDKKQDDLA PSETCLKKEL SQCNCIDLSK
SPDPDKSTGT DCRSNLETES SHQSVCTDTS ATSCNCKATE DASDLNDDDN LPTQELYYVF
DKFILTSGKP PTIVCSICKK DGHSKNDCPE DFRKIDLKPL PPMTNRFREI LDLVCKRCFD
ELSPPCSEQH NREQILIGLE KFIQKEYDEK ARLCLFGSSK NGFGFRDSDL DICMTLEGHE
NAEKLNCKEI IENLAKILKR HPGLRNILPI TTAKVPIVKF EHRRSGLEGD ISLYNTLAQH
NTRMLATYAA IDPRVQYLGY TMKVFAKRCD IGDASRGSLS SYAYILMVLY FLQQRKPPVI
PVLQEIFDGK QIPQRMVDGW NAFFFDKTEE LKKRLPSLGK NTESLGELWL GLLRFYTEEF
DFKEYVISIR QKKLLTTFEK QWTSKCIAIE DPFDLNHNLG AGVSRKMTNF IMKAFINGRK
LFGTPFYPLI GREAEYFFDS RVLTDGELAP NDRCCRVCGK IGHYMKDCPK RKSLLFRLKK
KDSEEEKEGN EEEKDSRDVL DPRDLHDTRD FRDPRDLRCF ICGDAGHVRR ECPEVKLARQ
RNSSVAAAQL VRNLVNAQQV AGSAQQQGDQ SIRTRQSSEC SESPSYSPQP QPFPQNSSQS
AAITQPSSQP GSQPKLGPPQ QGAQPPHQVQ MPLYNFPQSP PAQYSPMHNM GLLPMHPLQI
PAPSWPIHGP VIHSAPGSAP SNIGLNDPSI IFAQPAARPV AIPNTSHDGH WPRTVAPNSL
VNSGAVGNSE PGFRGLTPPI PWEHAPRPHF PLVPASWPYG LHQNFMHQGN ARFQPNKPFY
TQDRCATRRC RERCPHPPRG NVSE


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