ID   STPAP_HUMAN             Reviewed;         874 AA.
AC   Q9H6E5; A1A527; A8K995; Q2NL65; Q7L583; Q9H6H7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase;
DE            Short=Star-PAP;
DE            EC=2.7.7.19 {ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410, ECO:0000269|PubMed:28589955};
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:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:28589955};
GN   Name=TUT1; Synonyms=RBM21;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Eye;
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   [5]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, CATALYTIC
RP   ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16790842; DOI=10.1261/rna.87706;
RA   Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R.,
RA   Benecke B.-J.;
RT   "Identification, cloning, and functional analysis of the human U6 snRNA-
RT   specific terminal uridylyl transferase.";
RL   RNA 12:1494-1504(2006).
RN   [6]
RP   LACK OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
RX   PubMed=18172165; DOI=10.1101/gad.1622708;
RA   Mullen T.E., Marzluff W.F.;
RT   "Degradation of histone mRNA requires oligouridylation followed by
RT   decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT   5'.";
RL   Genes Dev. 22:50-65(2008).
RN   [7]
RP   FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF ASP-216 AND ASP-218.
RX   PubMed=18288197; DOI=10.1038/nature06666;
RA   Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C.,
RA   Anderson R.A.;
RT   "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of
RT   select mRNAs.";
RL   Nature 451:1013-1017(2008).
RN   [8]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY CK1.
RX   PubMed=18305108; DOI=10.1074/jbc.m800656200;
RA   Gonzales M.L., Mellman D.L., Anderson R.A.;
RT   "CKIalpha is associated with and phosphorylates star-PAP and is also
RT   required for expression of select star-PAP target messenger RNAs.";
RL   J. Biol. Chem. 283:12665-12673(2008).
RN   [9]
RP   FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, RNA-BINDING, AND
RP   INTERACTION WITH CPSF1 AND CPSF3.
RX   PubMed=21102410; DOI=10.1038/emboj.2010.287;
RA   Laishram R.S., Anderson R.A.;
RT   "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF
RT   interaction and specificity toward the pre-mRNA.";
RL   EMBO J. 29:4132-4145(2010).
RN   [10]
RP   STRUCTURE BY NMR OF 54-141.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RNA binding domain in RNA binding motif protein
RT   21.";
RL   Submitted (JUN-2007) to the PDB data bank.
RN   [11] {ECO:0007744|PDB:5WU1, ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3, ECO:0007744|PDB:5WU4, ECO:0007744|PDB:5WU5, ECO:0007744|PDB:5WU6}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH
RP   MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, DOMAIN, AND MUTAGENESIS OF ARG-779 AND ARG-783.
RX   PubMed=28589955; DOI=10.1038/ncomms15788;
RA   Yamashita S., Takagi Y., Nagaike T., Tomita K.;
RT   "Crystal structures of U6 snRNA-specific terminal uridylyltransferase.";
RL   Nat. Commun. 8:15788-15788(2017).
CC   -!- FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of
CC       specific pre-mRNAs (PubMed:18288197, PubMed:21102410). Localizes to
CC       nuclear speckles together with PIP5K1A and mediates polyadenylation of
CC       a select set of mRNAs, such as HMOX1 (PubMed:18288197). In addition to
CC       polyadenylation, it is also required for the 3'-end cleavage of pre-
CC       mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the
CC       recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs
CC       (PubMed:21102410). In addition to adenylyltransferase activity, also
CC       has uridylyltransferase activity (PubMed:16790842, PubMed:18288197,
CC       PubMed:28589955). However, the ATP ratio is higher than UTP in cells,
CC       suggesting that it functions primarily as a poly(A) polymerase
CC       (PubMed:18288197). Acts as a specific terminal uridylyltransferase for
CC       U6 snRNA in vitro: responsible for a controlled elongation reaction
CC       that results in the restoration of the four 3'-terminal UMP-residues
CC       found in newly transcribed U6 snRNA (PubMed:16790842, PubMed:18288197,
CC       PubMed:28589955). Not involved in replication-dependent histone mRNA
CC       degradation. {ECO:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197,
CC       ECO:0000269|PubMed:21102410, ECO:0000269|PubMed:28589955}.
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:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197,
CC         ECO:0000269|PubMed:28589955};
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:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410,
CC         ECO:0000269|PubMed:28589955};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:28589955};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC       Note=Binds 1 divalent cation per subunit.
CC       {ECO:0000269|PubMed:28589955};
CC   -!- ACTIVITY REGULATION: Adenylyltransferase activity is specifically
CC       phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
CC       {ECO:0000269|PubMed:18288197}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=59 uM for UTP {ECO:0000269|PubMed:28589955};
CC         KM=1380 uM for ATP {ECO:0000269|PubMed:28589955};
CC         KM=55 uM for U6 snRNA-u4 {ECO:0000269|PubMed:28589955};
CC         Note=kcat is 0.059 sec(-1) with UTP as substrate. kcat is 0.002
CC         sec(-1) with ATP as substrate. kcat is 0.061 sec(-1) with U6 snRNA-u4
CC         as substrate. {ECO:0000269|PubMed:28589955};
CC   -!- SUBUNIT: Associates with the cleavage and polyadenylation specificity
CC       factor (CPSF) complex (PubMed:21102410). Interacts with CPSF1 and
CC       CPSF3; the interaction is direct (PubMed:21102410). Interacts with
CC       PIP5K1A (PubMed:18288197). {ECO:0000269|PubMed:18288197,
CC       ECO:0000269|PubMed:21102410}.
CC   -!- INTERACTION:
CC       Q9H6E5; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-2511680, EBI-715394;
CC       Q9H6E5; Q99755: PIP5K1A; NbExp=3; IntAct=EBI-2511680, EBI-726414;
CC       Q9H6E5; Q99755-1: PIP5K1A; NbExp=2; IntAct=EBI-2511680, EBI-15687389;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16790842}.
CC       Nucleus speckle {ECO:0000269|PubMed:18288197,
CC       ECO:0000269|PubMed:18305108}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18288197}.
CC   -!- DOMAIN: The zinc-finger domain is required for terminal
CC       uridylyltransferase activity (PubMed:28589955). Together with the RRM
CC       domain, binds the 5'-area of U6 snRNA (PubMed:28589955).
CC       {ECO:0000269|PubMed:28589955}.
CC   -!- DOMAIN: The RRM domain is required for terminal uridylyltransferase
CC       activity (PubMed:28589955). Together with the zinc-finger domain, binds
CC       the 5'-area of U6 snRNA (PubMed:28589955).
CC       {ECO:0000269|PubMed:28589955}.
CC   -!- DOMAIN: The proline-rich region is dispensable for terminal
CC       uridylyltransferase activity. {ECO:0000269|PubMed:28589955}.
CC   -!- PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
CC       {ECO:0000269|PubMed:18305108}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK025920; BAB15282.1; ALT_INIT; mRNA.
DR   EMBL; AK026000; BAB15314.1; -; mRNA.
DR   EMBL; AK292610; BAF85299.1; -; mRNA.
DR   EMBL; AP002990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74029.1; -; Genomic_DNA.
DR   EMBL; BC005013; AAH05013.2; -; mRNA.
DR   EMBL; BC110910; AAI10911.1; -; mRNA.
DR   EMBL; BC128263; AAI28264.1; -; mRNA.
DR   CCDS; CCDS8021.3; -.
DR   RefSeq; NP_073741.2; NM_022830.2.
DR   PDB; 2E5G; NMR; -; A=55-141.
DR   PDB; 5WU1; X-ray; 2.80 A; A/B=141-874.
DR   PDB; 5WU2; X-ray; 2.95 A; A/B=141-874.
DR   PDB; 5WU3; X-ray; 2.70 A; A/B=141-874.
DR   PDB; 5WU4; X-ray; 2.80 A; A/B=141-874.
DR   PDB; 5WU5; X-ray; 3.40 A; A/B/C/D=141-874.
DR   PDB; 5WU6; X-ray; 3.21 A; A/B/C/D=53-599.
DR   PDB; 8IDF; X-ray; 3.70 A; A=1-599.
DR   PDBsum; 2E5G; -.
DR   PDBsum; 5WU1; -.
DR   PDBsum; 5WU2; -.
DR   PDBsum; 5WU3; -.
DR   PDBsum; 5WU4; -.
DR   PDBsum; 5WU5; -.
DR   PDBsum; 5WU6; -.
DR   PDBsum; 8IDF; -.
DR   AlphaFoldDB; Q9H6E5; -.
DR   SMR; Q9H6E5; -.
DR   BioGRID; 122325; 67.
DR   DIP; DIP-53651N; -.
DR   IntAct; Q9H6E5; 32.
DR   MINT; Q9H6E5; -.
DR   STRING; 9606.ENSP00000308000; -.
DR   iPTMnet; Q9H6E5; -.
DR   MetOSite; Q9H6E5; -.
DR   PhosphoSitePlus; Q9H6E5; -.
DR   BioMuta; TUT1; -.
DR   DMDM; 126302611; -.
DR   EPD; Q9H6E5; -.
DR   jPOST; Q9H6E5; -.
DR   MassIVE; Q9H6E5; -.
DR   MaxQB; Q9H6E5; -.
DR   PaxDb; 9606-ENSP00000308000; -.
DR   PeptideAtlas; Q9H6E5; -.
DR   ProteomicsDB; 80983; -.
DR   Pumba; Q9H6E5; -.
DR   Antibodypedia; 28452; 96 antibodies from 17 providers.
DR   DNASU; 64852; -.
DR   Ensembl; ENST00000476907.6; ENSP00000419607.1; ENSG00000149016.16.
DR   GeneID; 64852; -.
DR   KEGG; hsa:64852; -.
DR   MANE-Select; ENST00000476907.6; ENSP00000419607.1; NM_022830.3; NP_073741.3.
DR   UCSC; uc058cig.1; human.
DR   AGR; HGNC:26184; -.
DR   CTD; 64852; -.
DR   DisGeNET; 64852; -.
DR   GeneCards; TUT1; -.
DR   HGNC; HGNC:26184; TUT1.
DR   HPA; ENSG00000149016; Low tissue specificity.
DR   MIM; 610641; gene.
DR   neXtProt; NX_Q9H6E5; -.
DR   OpenTargets; ENSG00000149016; -.
DR   PharmGKB; PA162407405; -.
DR   VEuPathDB; HostDB:ENSG00000149016; -.
DR   eggNOG; KOG2277; Eukaryota.
DR   GeneTree; ENSGT00940000159914; -.
DR   HOGENOM; CLU_018757_1_0_1; -.
DR   InParanoid; Q9H6E5; -.
DR   OrthoDB; 170176at2759; -.
DR   PhylomeDB; Q9H6E5; -.
DR   BRENDA; 2.7.7.19; 2681.
DR   PathwayCommons; Q9H6E5; -.
DR   SignaLink; Q9H6E5; -.
DR   SIGNOR; Q9H6E5; -.
DR   BioGRID-ORCS; 64852; 815 hits in 1139 CRISPR screens.
DR   ChiTaRS; TUT1; human.
DR   EvolutionaryTrace; Q9H6E5; -.
DR   GenomeRNAi; 64852; -.
DR   Pharos; Q9H6E5; Tbio.
DR   PRO; PR:Q9H6E5; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9H6E5; Protein.
DR   Bgee; ENSG00000149016; Expressed in cerebellar vermis and 179 other cell types or tissues.
DR   ExpressionAtlas; Q9H6E5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0140767; F:enzyme-substrate adaptor activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; IDA:UniProtKB.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IMP:UniProtKB.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0016180; P:snRNA processing; IMP:UniProtKB.
DR   GO; GO:0034477; P:U6 snRNA 3'-end processing; IDA:UniProtKB.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   CDD; cd12279; RRM_TUT1; 1.
DR   Gene3D; 1.10.1410.10; -; 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; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF127; SPECKLE TARGETED PIP5K1A-REGULATED POLY(A) POLYMERASE; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q9H6E5; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Direct protein sequencing; Magnesium; Manganese;
KW   Metal-binding; mRNA processing; Nucleotide-binding; Nucleotidyltransferase;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..874
FT                   /note="Speckle targeted PIP5K1A-regulated poly(A)
FT                   polymerase"
FT                   /id="PRO_0000254186"
FT   DOMAIN          56..128
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          491..549
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          113..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..874
FT                   /note="KA1; binds the bulging loops of U6 snRNA but is
FT                   dispensable for terminal uridylyltransferase activity"
FT                   /evidence="ECO:0000269|PubMed:28589955"
FT   REGION          638..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU4"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:28589955"
FT   BINDING         216
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:28589955"
FT   BINDING         218
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT   BINDING         392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU4"
FT   BINDING         392
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT   BINDING         414
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT   BINDING         432
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT   BINDING         549
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000269|PubMed:28589955,
FT                   ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3"
FT   MOD_RES         750
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3MHT4"
FT   VARIANT         442
FT                   /note="L -> F (in dbSNP:rs3197865)"
FT                   /id="VAR_028833"
FT   MUTAGEN         216
FT                   /note="D->A: Abolishes adenylyltransferase activity; when
FT                   associated with A-218."
FT                   /evidence="ECO:0000269|PubMed:18288197"
FT   MUTAGEN         218
FT                   /note="D->A: Abolishes adenylyltransferase activity; when
FT                   associated with A-216."
FT                   /evidence="ECO:0000269|PubMed:18288197"
FT   MUTAGEN         779
FT                   /note="R->A: Reduced terminal uridylyltransferase activity;
FT                   when associated with A-783."
FT                   /evidence="ECO:0000269|PubMed:28589955"
FT   MUTAGEN         783
FT                   /note="R->A: Reduced terminal uridylyltransferase activity;
FT                   when associated with A-779."
FT                   /evidence="ECO:0000269|PubMed:28589955"
FT   CONFLICT        66
FT                   /note="D -> G (in Ref. 1; BAB15314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        809
FT                   /note="Q -> R (in Ref. 1; BAF85299)"
FT                   /evidence="ECO:0000305"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   HELIX           69..76
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:5WU6"
FT   HELIX           148..155
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           159..170
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           174..194
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          217..222
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           330..350
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          355..361
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          368..373
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   TURN            374..377
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          378..385
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           388..402
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           406..419
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          423..429
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           431..443
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          444..447
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           453..459
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           479..481
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           491..504
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          510..513
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   TURN            514..517
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          518..521
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          523..525
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           526..529
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          537..542
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   TURN            551..554
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           557..574
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           577..580
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          584..586
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           591..595
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           600..606
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           616..628
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          629..631
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          634..636
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          764..770
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           778..791
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           805..812
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   TURN            816..819
FT                   /evidence="ECO:0007829|PDB:5WU5"
FT   STRAND          829..836
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          838..840
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          842..849
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   STRAND          851..853
FT                   /evidence="ECO:0007829|PDB:5WU3"
FT   HELIX           855..874
FT                   /evidence="ECO:0007829|PDB:5WU3"
SQ   SEQUENCE   874 AA;  93847 MW;  85A4117A040FC90D CRC64;
     MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR KAQGLRSVFV
     SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG DVGAREAVLS QSQHSLGGHR
     LRVRPREQKE FQSPASKSPK GAAPDSHQLA KALAEAADVG AQMIKLVGLR ELSEAERQLR
     SLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS
     LDSALASPLD PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA
     SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG CVPGVYRVQT
     VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS ELDGRVRPLV YTLRCWAQGR
     GLSGSGPLLS NYALTLLVIY FLQTRDPPVL PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS
     RLEPSINVEP LSSLLAQFFS CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN
     LQDPFDLSHN VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP
     SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG ESSQGGTSKR
     LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV QDWAMQSPGQ PGDLPLTTGK
     HGAPGEEGQP SHAALAERGP KGHEAAQEWS QGEAGKGASL PSSASWRCAL WHRVWQGRRR
     ARRRLQQQTK EGAGGGAGTR AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD
     RMLTVTPLQD PQGLFPDLHH FLQVFLPQAI RHLK
//