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Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52)

 STPAP_MOUSE             Reviewed;         869 AA.
Q8R3F9; Q3UUH3;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase;
Short=Star-PAP;
EC=2.7.7.19;
AltName: Full=RNA-binding motif protein 21;
Short=RNA-binding protein 21;
AltName: Full=U6 snRNA-specific terminal uridylyltransferase 1;
Short=U6-TUTase;
EC=2.7.7.52;
Name=Tut1; Synonyms=Rbm21;
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 MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, 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).
-!- FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of
specific pre-mRNAs. Localizes to nuclear speckles together with
PIP5K1A and mediates polyadenylation of a select set of mRNAs,
such as HMOX1. In addition to polyadenylation, it is also required
for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of
targeted pre-mRNAs and promotes the recruitment and assembly of
the CPSF complex on the 3'UTR of pre-mRNAs. In addition to
adenylyltransferase activity, also has uridylyltransferase
activity. However, the ATP ratio is higher than UTP in cells,
suggesting that it functions primarily as a poly(A) polymerase.
Acts as a specific terminal uridylyltransferase for U6 snRNA in
vitro: responsible for a controlled elongation reaction that
results in the restoration of the four 3'-terminal UMP-residues
found in newly transcribed U6 snRNA. Not involved in replication-
dependent histone mRNA degradation (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
-!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Adenylyltransferase activity is specifically
phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
{ECO:0000250}.
-!- SUBUNIT: Associates with the cleavage and polyadenylation
specificity factor (CPSF) complex. Interacts with CPSF1 and CPSF3;
the interaction is direct. Interacts with PIP5K1A; interaction (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle
{ECO:0000250|UniProtKB:Q9H6E5}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8R3F9-1; Sequence=Displayed;
Name=2;
IsoId=Q8R3F9-2; Sequence=VSP_021201, VSP_021202;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK138418; BAE23652.1; -; mRNA.
EMBL; BC023900; AAH23900.1; -; mRNA.
EMBL; BC025499; AAH25499.1; -; mRNA.
CCDS; CCDS29562.1; -. [Q8R3F9-1]
RefSeq; NP_932110.1; NM_197993.3. [Q8R3F9-1]
UniGene; Mm.165979; -.
ProteinModelPortal; Q8R3F9; -.
SMR; Q8R3F9; -.
STRING; 10090.ENSMUSP00000093958; -.
iPTMnet; Q8R3F9; -.
PhosphoSitePlus; Q8R3F9; -.
EPD; Q8R3F9; -.
PaxDb; Q8R3F9; -.
PeptideAtlas; Q8R3F9; -.
PRIDE; Q8R3F9; -.
Ensembl; ENSMUST00000096239; ENSMUSP00000093958; ENSMUSG00000071645. [Q8R3F9-1]
GeneID; 70044; -.
KEGG; mmu:70044; -.
UCSC; uc008gog.1; mouse. [Q8R3F9-2]
UCSC; uc008goh.1; mouse. [Q8R3F9-1]
CTD; 64852; -.
MGI; MGI:1917294; Tut1.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00550000074490; -.
HOVERGEN; HBG079670; -.
InParanoid; Q8R3F9; -.
KO; K18709; -.
OMA; FCHRPSG; -.
OrthoDB; EOG091G091J; -.
PhylomeDB; Q8R3F9; -.
TreeFam; TF354308; -.
PRO; PR:Q8R3F9; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000071645; -.
Genevisible; Q8R3F9; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISS:UniProtKB.
GO; GO:0016180; P:snRNA processing; ISS:UniProtKB.
CDD; cd12279; RRM_TUT1; 1.
InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
InterPro; IPR002058; PAP_assoc.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034389; Star-PAP.
InterPro; IPR034388; Star-PAP_RRM.
InterPro; IPR036236; Znf_C2H2_sf.
PANTHER; PTHR12271:SF11; PTHR12271:SF11; 1.
Pfam; PF03828; PAP_assoc; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SMART; SM00451; ZnF_U1; 1.
SUPFAM; SSF54928; SSF54928; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Magnesium;
Manganese; Metal-binding; mRNA processing; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; Transferase; Zinc; Zinc-finger.
CHAIN 1 869 Speckle targeted PIP5K1A-regulated
poly(A) polymerase.
/FTId=PRO_0000254187.
DOMAIN 56 128 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 494 552 PAP-associated.
ZN_FING 16 40 C2H2-type.
COMPBIAS 229 312 Pro-rich.
METAL 216 216 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 218 218 Magnesium or manganese; catalytic.
{ECO:0000250}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000250|UniProtKB:Q3MHT4}.
VAR_SEQ 391 405 LALYNSRFLNLCSEM -> YFCVGLKAGSKVWGI (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021201.
VAR_SEQ 406 869 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021202.
SEQUENCE 869 AA; 94603 MW; 0D0D2C73AAC78A25 CRC64;
MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR KAQGLRSVFV
SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG DISAREAVLS QPKHSLGGHG
LRVRPREQKE FQSPASKSPK GVDSSSHQLV QALAEAADVG AQMVKLVELR ELSEAERQLR
NLVVALMQEV FTEFFPGCVV HPFGSTVNSF DVHGCDLDLF LDMGDMEETE PDPKAPKVPE
TSSLDSALAS SLDPQALACT PASPLDSLSP TSVQESESLD FDTPSSLAPQ TPDSALGSDT
VTSPQSLPPV SPLQEDRKEG KQGKELELAE EASKDEKEEA AAVLELVGSI LRGCVPGVYR
VQTVPSARRP VVKFCHRPSG LHGDVSLSNR LALYNSRFLN LCSEMDGRVR PLVYTLRCWA
QHNGLSGGGP LLNNYALTLL VIYFLQTRDP PVLPTVAQLT QRAGEGEQVE VDGWDCSFPK
DASRLEPSTN VEPLSSLLAQ FFSCVSCLDL SGSLLSLREG RPLMVAEGLP SDLWEGLRLG
PMNLQDPFDL SHNVAANVTG RVAKRLQSCC GAAASYCRSL QYQQRSSRGR DWGLLPLLQP
SSPSSLLSAK LIPLPSAPFP QVIMALVDVL REALGCHIEQ GTKRRRSEGA RIKDSPLGGV
NKRQRLGGQE KSFEEGKEEP QGCAGDHSEN EVEEMVIEVR ETPQDWALLH SGPPEEELPL
MTANCLDKAA EHNPMKPEVA GEGSQGETGK EASHPSSVSW RCALWHQVWQ GRRRARRRLQ
QQTKEEGRGG PTTGAEWLAM EARVTQELKG PNSEQERPPG EPLLSFVASA SQAEQTLTVA
PLQDSQGLFP GLHHFLQGFI PQALKNLLK


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