STPAP_AILME
ID STPAP_AILME Reviewed; 869 AA.
AC D2HS90;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=PANDA_014931;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL193267; EFB28167.1; -; Genomic_DNA.
DR AlphaFoldDB; D2HS90; -.
DR SMR; D2HS90; -.
DR STRING; 9646.ENSAMEP00000007096; -.
DR eggNOG; KOG2277; Eukaryota.
DR HOGENOM; CLU_018757_1_0_1; -.
DR InParanoid; D2HS90; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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; 3.30.460.10; -; 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 3: Inferred from homology;
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..869
FT /note="Speckle targeted PIP5K1A-regulated poly(A)
FT polymerase"
FT /id="PRO_0000404589"
FT DOMAIN 56..128
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 490..548
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 111..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..869
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 637..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..686
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 391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 391
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 413
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 431
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 548
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3F9"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MHT4"
SQ SEQUENCE 869 AA; 94063 MW; 01BB7E4572A16511 CRC64;
MAAVDLDVQS LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRATR KAQGLRSVFV
SGFPRDVDSA QLTQYFQAFG PVASVVMDKD KGVFAIVEMG DVGTREAVLS QPQHTLGGHR
LRVRPREQKE FQSPASKSPK GAAPDSHQLT KALAEAPDVG AQMVKLVGLR ELSEAERQLR
NLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEESQ PAPKAPESPS
LDSALASPLD PQALACTPAS PPDSQPPSPQ DSEALDFETP SSSLAPQTPD SALASETLAS
PQSLPPASPL QEDRGEGDLG KALELAEALS GEKTEGVAML ELVGSILRGC VPGVYRVQTV
PSARRPVVKF CHRPSGLHGD VSLSNRLALH NSRFLSLCSE LDGRVRPLVY TLRCWAQGRG
LSGSGPLLSN YALTLLVIYF LQTRDPPVLP TVSQLTQKAG EGEQVEVDGW DCSFPRDASG
LEPSTNKEPL SSLLAQFFSC VSCWDLRGSL LSLREGQALP VAGDLPSNRW EGLRLGPMNL
QDPFDLSHNV AANVTSRVAG RLQNSCQAAA NYCRSLQYQR RSSRGRDWGL LPLLQPSSPS
SLLSATPIPL PPAPFTQLTA ALAQVLREAL GCHIEQGTKR LRSDRGGPEE SPQGGTSKRL
KLDGEEKSCE EGREEQQGYI RDHSEDGVEE MVVEVGEMVQ DWVQSPGRPG EPPQMLREQL
ATGEEGQSGH AALAEQGPKG PEAAREGSQG ETGRGVSLSS VSWRCALWHR VWQGRRRARR
RLQQQTKERG RGSAGTAEWL AVEAQVTREL RGLSSAAQRP EAEPLLTFVA SASQVNQTLT
VTPIQDSQGL FPDLHHFLQV FLPQALRNL
