STPAP_MOUSE
ID STPAP_MOUSE Reviewed; 869 AA.
AC Q8R3F9; Q3UUH3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3F9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3F9-2; Sequence=VSP_021201, VSP_021202;
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; AK138418; BAE23652.1; -; mRNA.
DR EMBL; BC023900; AAH23900.1; -; mRNA.
DR EMBL; BC025499; AAH25499.1; -; mRNA.
DR CCDS; CCDS29562.1; -. [Q8R3F9-1]
DR RefSeq; NP_932110.1; NM_197993.3. [Q8R3F9-1]
DR AlphaFoldDB; Q8R3F9; -.
DR SMR; Q8R3F9; -.
DR BioGRID; 213834; 4.
DR STRING; 10090.ENSMUSP00000093958; -.
DR iPTMnet; Q8R3F9; -.
DR PhosphoSitePlus; Q8R3F9; -.
DR EPD; Q8R3F9; -.
DR jPOST; Q8R3F9; -.
DR MaxQB; Q8R3F9; -.
DR PaxDb; Q8R3F9; -.
DR PeptideAtlas; Q8R3F9; -.
DR PRIDE; Q8R3F9; -.
DR ProteomicsDB; 257462; -. [Q8R3F9-1]
DR ProteomicsDB; 257463; -. [Q8R3F9-2]
DR Ensembl; ENSMUST00000096239; ENSMUSP00000093958; ENSMUSG00000071645. [Q8R3F9-1]
DR GeneID; 70044; -.
DR KEGG; mmu:70044; -.
DR UCSC; uc008gog.1; mouse. [Q8R3F9-2]
DR UCSC; uc008goh.1; mouse. [Q8R3F9-1]
DR CTD; 64852; -.
DR MGI; MGI:1917294; Tut1.
DR VEuPathDB; HostDB:ENSMUSG00000071645; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000159914; -.
DR HOGENOM; CLU_018757_1_0_1; -.
DR InParanoid; Q8R3F9; -.
DR OMA; SLQYQHK; -.
DR OrthoDB; 1188122at2759; -.
DR PhylomeDB; Q8R3F9; -.
DR TreeFam; TF354308; -.
DR BioGRID-ORCS; 70044; 24 hits in 71 CRISPR screens.
DR ChiTaRS; Tut1; mouse.
DR PRO; PR:Q8R3F9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8R3F9; protein.
DR Bgee; ENSMUSG00000071645; Expressed in ear vesicle and 166 other tissues.
DR Genevisible; Q8R3F9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
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 Alternative splicing; ATP-binding; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..869
FT /note="Speckle targeted PIP5K1A-regulated poly(A)
FT polymerase"
FT /id="PRO_0000254187"
FT DOMAIN 56..128
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 494..552
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 114..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..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 640..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..689
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 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 395
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 417
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 435
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT BINDING 552
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MHT4"
FT VAR_SEQ 391..405
FT /note="LALYNSRFLNLCSEM -> YFCVGLKAGSKVWGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021201"
FT VAR_SEQ 406..869
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021202"
SQ SEQUENCE 869 AA; 94603 MW; 0D0D2C73AAC78A25 CRC64;
MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR KAQGLRSVFV
SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG DISAREAVLS QPKHSLGGHG
LRVRPREQKE FQSPASKSPK GVDSSSHQLV QALAEAADVG AQMVKLVELR ELSEAERQLR
NLVVALMQEV FTEFFPGCVV HPFGSTVNSF DVHGCDLDLF LDMGDMEETE PDPKAPKVPE
TSSLDSALAS SLDPQALACT PASPLDSLSP TSVQESESLD FDTPSSLAPQ TPDSALGSDT
VTSPQSLPPV SPLQEDRKEG KQGKELELAE EASKDEKEEA AAVLELVGSI LRGCVPGVYR
VQTVPSARRP VVKFCHRPSG LHGDVSLSNR LALYNSRFLN LCSEMDGRVR PLVYTLRCWA
QHNGLSGGGP LLNNYALTLL VIYFLQTRDP PVLPTVAQLT QRAGEGEQVE VDGWDCSFPK
DASRLEPSTN VEPLSSLLAQ FFSCVSCLDL SGSLLSLREG RPLMVAEGLP SDLWEGLRLG
PMNLQDPFDL SHNVAANVTG RVAKRLQSCC GAAASYCRSL QYQQRSSRGR DWGLLPLLQP
SSPSSLLSAK LIPLPSAPFP QVIMALVDVL REALGCHIEQ GTKRRRSEGA RIKDSPLGGV
NKRQRLGGQE KSFEEGKEEP QGCAGDHSEN EVEEMVIEVR ETPQDWALLH SGPPEEELPL
MTANCLDKAA EHNPMKPEVA GEGSQGETGK EASHPSSVSW RCALWHQVWQ GRRRARRRLQ
QQTKEEGRGG PTTGAEWLAM EARVTQELKG PNSEQERPPG EPLLSFVASA SQAEQTLTVA
PLQDSQGLFP GLHHFLQGFI PQALKNLLK
