STPAP_RAT
ID STPAP_RAT Reviewed; 866 AA.
AC Q3MHT4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase;
DE Short=Star-PAP;
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:Q9H6E5};
DE AltName: Full=RNA-binding motif protein 21;
DE Short=RNA-binding protein 21;
DE AltName: Full=U6 snRNA-specific terminal uridylyltransferase 1;
DE Short=U6-TUTase;
DE EC=2.7.7.52 {ECO:0000250|UniProtKB:Q9H6E5};
GN Name=Tut1; Synonyms=Rbm21;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of
CC specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A
CC and mediates polyadenylation of a select set of mRNAs, such as HMOX1.
CC In addition to polyadenylation, it is also required for the 3'-end
CC cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and
CC promotes the recruitment and assembly of the CPSF complex on the 3'UTR
CC of pre-mRNAs. In addition to adenylyltransferase activity, also has
CC uridylyltransferase activity. However, the ATP ratio is higher than UTP
CC in cells, suggesting that it functions primarily as a poly(A)
CC polymerase. Acts as a specific terminal uridylyltransferase for U6
CC snRNA in vitro: responsible for a controlled elongation reaction that
CC results in the restoration of the four 3'-terminal UMP-residues found
CC in newly transcribed U6 snRNA. Not involved in replication-dependent
CC histone mRNA degradation. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000250|UniProtKB:Q9H6E5};
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:Q9H6E5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H6E5};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC Note=Binds 1 divalent cation per subunit.
CC {ECO:0000250|UniProtKB:Q9H6E5};
CC -!- ACTIVITY REGULATION: Adenylyltransferase activity is specifically
CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
CC {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- SUBUNIT: Associates with the cleavage and polyadenylation specificity
CC factor (CPSF) complex. Interacts with CPSF1 and CPSF3; the interaction
CC is direct. Interacts with PIP5K1A. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- DOMAIN: The zinc-finger domain is required for terminal
CC uridylyltransferase activity. Together with the RRM domain, binds the
CC 5'-area of U6 snRNA. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- DOMAIN: The RRM domain is required for terminal uridylyltransferase
CC activity. Together with the zinc-finger domain, binds the 5'-area of U6
CC snRNA. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- DOMAIN: The proline-rich region is dispensable for terminal
CC uridylyltransferase activity. {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
CC {ECO:0000250|UniProtKB:Q9H6E5}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; BC104695; AAI04696.1; -; mRNA.
DR RefSeq; NP_001029073.1; NM_001033901.1.
DR AlphaFoldDB; Q3MHT4; -.
DR SMR; Q3MHT4; -.
DR BioGRID; 270623; 1.
DR IntAct; Q3MHT4; 1.
DR STRING; 10116.ENSRNOP00000027187; -.
DR iPTMnet; Q3MHT4; -.
DR PhosphoSitePlus; Q3MHT4; -.
DR PaxDb; Q3MHT4; -.
DR PRIDE; Q3MHT4; -.
DR Ensembl; ENSRNOT00000027187; ENSRNOP00000027187; ENSRNOG00000020047.
DR GeneID; 499314; -.
DR KEGG; rno:499314; -.
DR UCSC; RGD:1561043; rat.
DR CTD; 64852; -.
DR RGD; 1561043; Tut1.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000159914; -.
DR HOGENOM; CLU_018757_1_0_1; -.
DR InParanoid; Q3MHT4; -.
DR OMA; SLQYQHK; -.
DR OrthoDB; 1188122at2759; -.
DR PhylomeDB; Q3MHT4; -.
DR TreeFam; TF354308; -.
DR PRO; PR:Q3MHT4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020047; Expressed in testis and 20 other tissues.
DR Genevisible; Q3MHT4; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISS:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; ISS:UniProtKB.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; ISS:UniProtKB.
DR CDD; cd12279; RRM_TUT1; 1.
DR Gene3D; 3.30.460.10; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034388; Star-PAP_RRM.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF19088; TUTase; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..866
FT /note="Speckle targeted PIP5K1A-regulated poly(A)
FT polymerase"
FT /id="PRO_0000254188"
FT DOMAIN 56..128
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 492..550
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT ZN_FING 16..46
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 116..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..866
FT /note="KA1; binds the bulging loops of U6 snRNA but is
FT dispensable for terminal uridylyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT REGION 638..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 216
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 218
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 393
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 415
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 433
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 550
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3F9"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ 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
