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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_RAT               Reviewed;         866 AA.
Q3MHT4;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 1.
22-NOV-2017, entry version 88.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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}.
-!- PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
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EMBL; BC104695; AAI04696.1; -; mRNA.
RefSeq; NP_001029073.1; NM_001033901.1.
UniGene; Rn.129389; -.
ProteinModelPortal; Q3MHT4; -.
SMR; Q3MHT4; -.
BioGrid; 270623; 1.
IntAct; Q3MHT4; 1.
STRING; 10116.ENSRNOP00000027187; -.
iPTMnet; Q3MHT4; -.
PhosphoSitePlus; Q3MHT4; -.
PaxDb; Q3MHT4; -.
PRIDE; Q3MHT4; -.
Ensembl; ENSRNOT00000027187; ENSRNOP00000027187; ENSRNOG00000020047.
GeneID; 499314; -.
KEGG; rno:499314; -.
UCSC; RGD:1561043; rat.
CTD; 64852; -.
RGD; 1561043; Tut1.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00550000074490; -.
HOVERGEN; HBG079670; -.
InParanoid; Q3MHT4; -.
KO; K18709; -.
OMA; FCHRPSG; -.
OrthoDB; EOG091G091J; -.
PhylomeDB; Q3MHT4; -.
TreeFam; TF354308; -.
PRO; PR:Q3MHT4; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000020047; -.
Genevisible; Q3MHT4; RN.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
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;
ATP-binding; Complete proteome; Magnesium; Manganese; Metal-binding;
mRNA processing; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding; Transferase; Zinc;
Zinc-finger.
CHAIN 1 866 Speckle targeted PIP5K1A-regulated
poly(A) polymerase.
/FTId=PRO_0000254188.
DOMAIN 56 128 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 492 550 PAP-associated.
ZN_FING 16 40 C2H2-type.
COMPBIAS 229 311 Pro-rich.
METAL 216 216 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 218 218 Magnesium or manganese; catalytic.
{ECO:0000250}.
MOD_RES 686 686 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R3F9}.
MOD_RES 741 741 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
SEQUENCE 866 AA; 94378 MW; E85DE9E051D30412 CRC64;
MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR KAQGLRSVFV
SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG DISAREAVLS QPKHSLGGHT
LRVRPREQKE FQSPASKSPK GVDSNSHQLA QALAEAADVG AQMVKLVELR ELSEAERQLR
TLVVALMQEV FTEFFPGCVV HPFGSSVNSF DVHGCDLDLF LDLGDMEEPQ PDPQTPKLPE
ASSLDSTLAS SLDPQVLACT PASLDSLSPT SLQDSEALDF ETPSSLAPQT PDSALGSDTV
TSPQSLPPVS PLEEDRGEGK HRKELELAEA SKDEKEEATA VLELVGSILR GCVPGVYRVQ
TVPSARRPVV KFCHRPSGLH GDISLSNRLA LYNSRFLNLC SEMDSRVRPL VYTLRCWAQH
NGLSGGGPLL NNYALTLLVI YFLQTRDPPV LPTVAQLTQR SGEGEQVEVD GWDCSFPKDA
SRLEPSTNVE PLSSLLAQFF SCVSCWDLSG SLLSLREGQA LMVAGGLPSD LWEGLRLGPM
NLQDPFDLSH NVAANVTSRV AKRLQSSCGA AASYCRSLQY QQRSSRGRDW GLLPLLQPSS
PSSLLSAKLI PLPSAPFPQI ITALVSVLRE ALGCHIEQGT KRRRSEGARS KDSPLGGANK
RPRLSGQEKS CEEGKEEPQG CAGDHSENEV EEMVIELRET PQDWALLHCG PPGELPLMTA
KCLDKTAEQN PMEPEGAGEG SPGETEKEAS HPSSVSWRCA LWHQIWQGRR RARRRFQQQT
KEEGRGGPST GAEWLAVEAR VTQELKGPKS EQQRLQGEPL LTFVASASQA EQTLTVAPLQ
DPQGLFPGLH HFLQVFIPQA LKNLLK


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