STPAP_DANRE
ID STPAP_DANRE Reviewed; 797 AA.
AC Q4KMD7;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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; ORFNames=zgc:112254;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of
CC specific pre-mRNAs. In addition to polyadenylation, it is also required
CC for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted
CC pre-mRNAs and promotes the recruitment and assembly of the CPSF complex
CC on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity,
CC also has uridylyltransferase activity. However, the ATP ratio is higher
CC than UTP in cells, suggesting that it functions primarily as a poly(A)
CC polymerase. {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 -!- SUBUNIT: Associates with the cleavage and polyadenylation specificity
CC factor (CPSF) complex. {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 -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; BC098614; AAH98614.1; -; mRNA.
DR RefSeq; NP_001025359.1; NM_001030188.1.
DR AlphaFoldDB; Q4KMD7; -.
DR SMR; Q4KMD7; -.
DR STRING; 7955.ENSDARP00000074395; -.
DR PaxDb; Q4KMD7; -.
DR GeneID; 564388; -.
DR KEGG; dre:564388; -.
DR CTD; 64852; -.
DR ZFIN; ZDB-GENE-050706-68; tut1.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; Q4KMD7; -.
DR OrthoDB; 1188122at2759; -.
DR PhylomeDB; Q4KMD7; -.
DR PRO; PR:Q4KMD7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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: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: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 CDD; cd12279; RRM_TUT1; 1.
DR Gene3D; 3.30.460.10; -; 1.
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; IPR041252; RL.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034388; Star-PAP_RRM.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF17797; RL; 1.
DR Pfam; PF19088; TUTase; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW RNA-binding; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..797
FT /note="Speckle targeted PIP5K1A-regulated poly(A)
FT polymerase"
FT /id="PRO_0000404590"
FT DOMAIN 54..126
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 421..495
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT ZN_FING 14..44
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 544..787
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 611..659
FT /note="Disordered"
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 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 319
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 341
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 363
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 495
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
SQ SEQUENCE 797 AA; 89937 MW; C11F915CC7CCA221 CRC64;
MELDKDIQTT QKGFHCNLCH VNIPNRPSLE DHVKGKKHLH LLRLRAQRKT QEENSVFVSG
FKADTSQTEL KEYFQQFGLV TDVIMDKQKG VYAIVEFSES QDVQTTLAQP QHQLNGLKLR
VKPREKKEFK LASRGKQDCK NTLISLDKLN FELCKAMSVN EQIQKVVESL ELKDNEKKVR
DLLVQLLQEV FTEFFPDCQI VPFGSSVNTF GLHSCDLDLF LDLENTKVFQ ARAKSSEQTG
ENQSEDCRSE DSILSDIDLS TASPAEILEL VAVILRKCVP GVHKVQALST ARLPVVKFSH
KELNLQGDIT INNRLAVRNT KFLQLCSGID SRLRPLVYTI RLWAKQKQLA GNLSGPGPLL
NNYALTLLVI FFLQNRDPPV LPSVNQLKNM ACEEEECAIE EWDCTFPSQP FSVPPSKNTE
DLCTLLFGFF TFYSKFDFPA SVVSLRDGHV LPITDFLKSD MEALKTADAS SPKPKRSSAP
RLGPMNVLDP FELNHNVAGN LNERTQKNFK RECCEAEKYC RSLQYQRKSA KGKSWGLVRL
FAPQSEAAAS SQPRAEKVLE VSVPFKPASL PESLRAQLAS AGKDFRGLWF AEVCSAVQKV
FNEILQCSPT EETQSLDKTD KSGSEMEVNN NRSLEDTNIQ VKGEAGKKRP LSVEEGPSTF
TITQAKRQRL DVDLEHPEPL HWTWTQRSRV WAGRRKVRRD LLKTSDEASK PEGGCVDMES
RVTQSIVEKE EKLHDALEFK VDAEVVGGNE STKVVLRFHP SIDTAGVFQD FFHFLESFLP
KMAETIMGRA EDITDMS
