STPAP_BOVIN
ID STPAP_BOVIN Reviewed; 871 AA.
AC Q1JPD6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT025417; ABF57373.1; -; mRNA.
DR RefSeq; NP_001073791.1; NM_001080322.1.
DR AlphaFoldDB; Q1JPD6; -.
DR SMR; Q1JPD6; -.
DR STRING; 9913.ENSBTAP00000015724; -.
DR PaxDb; Q1JPD6; -.
DR GeneID; 616339; -.
DR KEGG; bta:616339; -.
DR CTD; 64852; -.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; Q1JPD6; -.
DR OrthoDB; 1188122at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
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:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISS:UniProtKB.
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; 3.30.70.330; -; 1.
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 SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript 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..871
FT /note="Speckle targeted PIP5K1A-regulated poly(A)
FT polymerase"
FT /id="PRO_0000254185"
FT DOMAIN 56..128
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 489..547
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 252..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..871
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 636..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..684
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 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 392
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 414
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 432
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 547
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MHT4"
SQ SEQUENCE 871 AA; 93811 MW; E681018AFBA18459 CRC64;
MAAVDSDIEP LPRGGFRCCL CHITTANQPS LDAHLGGRKH RHLVELRATR KAQGLRSVFV
SGFPRDVDST QLSEYFQAFG PVASVVMDKD KGVFAIVEMG DLGAREAVLS QPQHSLGGRR
LRVRPREQIE FQSPASRSPK RVAPDSHQLI KALAEAPDVE AQMVKLVGLR ELSEAERQLR
SLVVALMQEV FAEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLDEPQ PAPKAPESPS
LDSALASPLD PQALACTPAS PPDSQPPASP QDSEALDFEA PSSSLAPRTP DSALASETLA
SPRSLPPASP LQEDQGDGDQ GKAVELAEAL KGEKAEGGAM LELVGSILRG CVPGVYRVQT
VPSARCPVVK FCHRPSGLHG DISLSNRLAL HNSRFLSLCS ELDGRVRPLV YTLRCWAQGR
GLSGSGPLLN NYALTLLVIY FLQTRDPPVL PTVSQLTQKA GEQVEVDGWD CSFPRDASRL
EPSTNKEPLS SLLAQFFSCV SCWDLRGSLL SLREGQALSV AGGLPSNLSE GLRLGPMNLQ
DPFDLSHNVA ANVTSRVAGR LQNCCRAAAN YCRSLQYQRR SSRGRDWGLL PLLQPSSPSS
ILSATPIPLP PASFTQLTAV LAQVLREALG CHIEQGTKRL RSEGGGPGEP PQGGTSKRAK
LDGQKKSCEE GPEEQQGCAG EHGEDGVEEM VIEVGESVQD WVMRSPGQLG ELPLMTGKHL
ATREEGQSGT AALAKQGPRG PEAACEGSQA EAEKRVSLTV SWRCALWHRV WQGRRRARRR
LQQQIKEGGG SGAGSGAEWL ATEAQVTREL RGLSSTEQRP EAEPLLTFVA STSQADQSLT
VTPLQDSQGL FPDLHHFLQV FLPQALRNLL K
