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

 TUT4_MOUSE              Reviewed;        1644 AA.
B2RX14; A2A8R8; Q3UYT6; Q5DU43;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 2.
23-MAY-2018, entry version 81.
RecName: Full=Terminal uridylyltransferase 4;
Short=TUTase 4;
EC=2.7.7.52;
AltName: Full=Zinc finger CCHC domain-containing protein 11;
Name=Zcchc11; Synonyms=Kiaa0191, Tut4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1644.
TISSUE=Brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 753-1644.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION IN PRE-LET-7 URIDYLATION AND MAINTENANCE OF EMBRYONIC STEM
CELL PLURIPOTENCY, AND SUBCELLULAR LOCATION.
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
ASP-1026 AND ASP-1028.
PubMed=19701194; DOI=10.1038/ncb1931;
Jones M.R., Quinton L.J., Blahna M.T., Neilson J.R., Fu S.,
Ivanov A.R., Wolf D.A., Mizgerd J.P.;
"Zcchc11-dependent uridylation of microRNA directs cytokine
expression.";
Nat. Cell Biol. 11:1157-1163(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION IN PRE-LET-7 URIDYLATION, AND MUTAGENESIS OF CYS-326 AND
CYS-329.
PubMed=22898984; DOI=10.1261/rna.034538.112;
Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.;
"Lin28-mediated control of let-7 microRNA expression by alternative
TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7).";
RNA 18:1875-1885(2012).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1624, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Uridylyltransferase that mediates the terminal
uridylation of mRNAs with short (less than 25 nucleotides) poly(A)
tails, hence facilitating global mRNA decay. Involved in microRNA
(miRNA)-induced gene silencing through uridylation of deadenylated
miRNA targets. Also 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 cell pluripotency (PubMed:19703396).
Does not bind RNA directly, but recruited to RNA targets by RNA-
binding protein LIN28A. 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:19701194). May also suppress Toll-like receptor-induced
NF-kappa-B activation via binding to T2BP. Does not play a role in
replication-dependent histone mRNA degradation. Due to functional
redundancy between ZCCHC6 and ZCCHC11, the identification of the
specific role of each of these proteins is difficult.
{ECO:0000250, ECO:0000250|UniProtKB:Q5TAX3,
ECO:0000269|PubMed:19701194, ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:22898984}.
-!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
{ECO:0000269|PubMed:19701194}.
-!- 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.
Interacts with T2BP. {ECO:0000250|UniProtKB:Q5TAX3}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TAX3}.
Cytoplasm {ECO:0000269|PubMed:19703396}. Note=Mainly cytoplasmic
(PubMed:19703396). Translocates into the cytoplasm following
treatment of the cell with LPS (By similarity).
{ECO:0000250|UniProtKB:Q5TAX3, ECO:0000269|PubMed:19703396}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:19701194}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAM23506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAM25329.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL626783; CAM23506.1; ALT_SEQ; Genomic_DNA.
EMBL; AL627238; CAM23506.1; JOINED; Genomic_DNA.
EMBL; AL627238; CAM25329.1; ALT_SEQ; Genomic_DNA.
EMBL; AL626783; CAM25329.1; JOINED; Genomic_DNA.
EMBL; BC150791; AAI50792.1; -; mRNA.
EMBL; AK220327; BAD90397.1; -; mRNA.
EMBL; AK134388; BAE22125.1; -; mRNA.
CCDS; CCDS18451.1; -.
RefSeq; NP_780681.2; NM_175472.3.
UniGene; Mm.25181; -.
UniGene; Mm.446602; -.
ProteinModelPortal; B2RX14; -.
SMR; B2RX14; -.
BioGrid; 230978; 1.
DIP; DIP-48571N; -.
IntAct; B2RX14; 1.
STRING; 10090.ENSMUSP00000044836; -.
iPTMnet; B2RX14; -.
PhosphoSitePlus; B2RX14; -.
EPD; B2RX14; -.
MaxQB; B2RX14; -.
PaxDb; B2RX14; -.
PRIDE; B2RX14; -.
Ensembl; ENSMUST00000043368; ENSMUSP00000044836; ENSMUSG00000034610.
GeneID; 230594; -.
KEGG; mmu:230594; -.
UCSC; uc008ubd.1; mouse.
CTD; 23318; -.
MGI; MGI:2445126; Zcchc11.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00550000074490; -.
HOGENOM; HOG000231134; -.
InParanoid; B2RX14; -.
KO; K13291; -.
ChiTaRS; Zcchc11; mouse.
PRO; PR:B2RX14; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000034610; -.
ExpressionAtlas; B2RX14; baseline and differential.
Genevisible; B2RX14; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001816; P:cytokine production; IDA:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISS: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.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Magnesium; Manganese; Metal-binding;
Methylation; Nucleotidyltransferase; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-mediated gene silencing; Transferase;
Zinc; Zinc-finger.
CHAIN 1 1644 Terminal uridylyltransferase 4.
/FTId=PRO_0000385330.
DOMAIN 649 698 PAP-associated 1.
DOMAIN 1201 1254 PAP-associated 2.
ZN_FING 930 947 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1310 1327 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1358 1375 CCHC-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
COMPBIAS 1425 1598 Pro-rich.
METAL 1026 1026 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 1028 1028 Magnesium or manganese; catalytic.
{ECO:0000250}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q5TAX3}.
MOD_RES 131 131 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1624 1624 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MUTAGEN 326 326 C->A: No effect on basal uridylation
activity, but loss of LIN28A-enhanced
uridylation; when associated with A-329.
{ECO:0000269|PubMed:22898984}.
MUTAGEN 329 329 C->A: No effect on basal uridylation
activity, but loss of LIN28A-enhanced
uridylation; when associated with A-326.
{ECO:0000269|PubMed:22898984}.
MUTAGEN 1026 1026 D->A: Loss of nucleotidyltransferase
activity; when associated with A-1028.
{ECO:0000269|PubMed:19701194}.
MUTAGEN 1028 1028 D->A: Loss of nucleotidyltransferase
activity; when associated with A-1026.
{ECO:0000269|PubMed:19701194}.
CONFLICT 815 815 D -> A (in Ref. 2; AAI50792 and 3;
BAD90397). {ECO:0000305}.
CONFLICT 1336 1336 S -> R (in Ref. 4; BAE22125).
{ECO:0000305}.
CONFLICT 1422 1422 S -> C (in Ref. 4; BAE22125).
{ECO:0000305}.
SEQUENCE 1644 AA; 184650 MW; 5EE701412E6157A0 CRC64;
MEEPKTSKNE NHEPKKNIIC EESKAVKIIS NQTLKPRNDK SEIGTSSLNR NSSKKTKQND
ICIEKTEAKS CKVNAASVPG PKDLGLVHRD QSHCKMKKLP NSPMKAQKGS SQTKLEKTPS
LQTKAEKVPK SPNLPVKAEK APCTTAEATT EKALNSQRKE ENTPTSQMKL QKTPRSPLEP
ENVPSLLLKE NVKQTESQQT GKKLTSSFVS MDKRKSEALQ GEKSALENSS LSQKQQTQTD
NIADSDDSAS GIEDTADDLS KMKSEESNKE NSSEMDYLEN ATVIDESALT PEQRLGLKQA
EERLERDHIF RLEKRSPEYT NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE
LRSLPSPSSA HLAALSVAVV ELAKEQGITD DDLRIRQDIV EEMSKVIMTF LPECSLRLYG
SSLTKFALKS SDVNIDIKFP PKMNHPDLLI QVLGILKKSA LYIDVESDFH AKVPVVVCKD
RKSALLCRVS AGNDMACLTT DLLAALGKVE PVFTPLVLAF RYWAKLCYID SQTDGGIPSY
CFALMVMFFL QQRKPPLLPC LLGSWIEGFD PKRMDDFQLK GIVEEKFVKW EYNSSSATEK
NLIADENKAK ADEPKDDTKK TETDNQSNAA KAKHGKSPLT LEAPNQVPLG QLWLELLKFY
TLDFALEEYV ICVRIQDILT RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF
RAAYRYFACP QKKGGNKSTM DPKKKEKGKL SSKKPVKSDC SATNCCILGE SAEKIHMERG
QPAKHDETEF TSQRCIVDND SLLVNELGLA NHGQDSSSLS TASGGSDLKQ KSAEKQGDLT
PSETSLKKEL SQCICIGTPD GAESAGTDCR SNLEMDSSHQ IVCNNVSATS CNCKATEVTS
DLVDEDNLPS QELYYVFDKF ILTSGKPPTI VCSICKKDGH SKNDCPEDFR KIDLKPLPPM
TNRFREILDL VCKRCFDELS PPCSEQHNRE QILIGLEKFI QKEYDEKARL CLFGSSKNGF
GFRDSDLDIC MTLEGHENAE KLNCKEIIEN LAKILKRHPG LRNILPITTA KVPIVKFEHR
RSGLEGDISL YNTLAQHNTR MLATYAAIDP RVQYLGYTMK VFAKRCDIGD ASRGSLSSYA
YILMVLYFLQ QRKPPVIPVL QEIFDGKQIP QRMVDGWNAF FFDKTEELKK RLPSLGKNTE
SLGELWLGLL RFYTEEFDFK EYVISIRQKK LLTTFEKQWT SKCIAIEDPF DLNHNLGAGV
SRKMTNFIMK AFINGRKLFG TPFYPLIGRE AEYFFDSRVL TDGELAPNDR CCRVCGKIGH
YMKDCPKRKR LKKKDSEEEK EGNEEEKDSR DLLDSRDLRC FICGDAGHVR RECPEVKMAR
QRNSSVAAAQ LVRNLVNAQQ VAGSAQQQSD QSIRTRQSSE CSDSPSYSPQ PQPFPQNSPQ
PSALPPPPSQ PGSQPKLGPP QQGGQPPHQV QMPLYNFPQS PPAHYSPMHS MGLLPMHPLQ
IPAPSWPIHG PMLHSAPGST PSNIGLNDPS IIFAQPAARP MAIPSPSHDG HWPRTVAPNS
LVNNGAVGNS EPRFRGLNPP IPWEHAPRHF PLVPASWPYG LHQNFMHQGN PRFQPKPFYA
QADRCATRRC RERCPHPPRG NVSE


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6017 Snell Ave, Ste 357
San Jose, CA 95123




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