ID   A0A0A8K9B1_HUMAN        Unreviewed;       874 AA.
AC   A0A0A8K9B1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   18-JUN-2025, entry version 59.
DE   RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase {ECO:0000256|ARBA:ARBA00021679};
DE            EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
DE            EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
DE   AltName: Full=RNA-binding motif protein 21 {ECO:0000256|ARBA:ARBA00030790};
DE   AltName: Full=U6 snRNA-specific terminal uridylyltransferase 1 {ECO:0000256|ARBA:ARBA00033036};
GN   Name=URLC6 {ECO:0000313|EMBL:BAQ19752.1};
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 {ECO:0000313|EMBL:BAQ19752.1};
RN   [1] {ECO:0000313|EMBL:BAQ19752.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Daigo Y., Nakamura Y.;
RT   "Isolation and characterization of novel human genes, which are up-
RT   regulated in lung cancer.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00045789}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + ATP = RNA(n)-3'-adenine ribonucleotide + diphosphate;
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:0000256|ARBA:ARBA00048830};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + UTP = RNA(n)-3'-uridine ribonucleotide + diphosphate;
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:0000256|ARBA:ARBA00049105};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:0000256|ARBA:ARBA00046411}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC       Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000256|ARBA:ARBA00008593}.
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DR   EMBL; AB101208; BAQ19752.1; -; mRNA.
DR   RefSeq; NP_073741.2; NM_022830.2.
DR   AlphaFoldDB; A0A0A8K9B1; -.
DR   SMR; A0A0A8K9B1; -.
DR   Antibodypedia; 28452; 87 antibodies from 17 providers.
DR   DNASU; 64852; -.
DR   GeneID; 64852; -.
DR   KEGG; hsa:64852; -.
DR   CTD; 64852; -.
DR   DisGeNET; 64852; -.
DR   VEuPathDB; HostDB:ENSG00000149016; -.
DR   HOGENOM; CLU_018757_1_0_1; -.
DR   OrthoDB; 2274644at2759; -.
DR   PhylomeDB; A0A0A8K9B1; -.
DR   ChiTaRS; TUT1; human.
DR   ExpressionAtlas; A0A0A8K9B1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProtKB-ARBA.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   CDD; cd12279; RRM_TUT1; 1.
DR   FunFam; 1.10.1410.10:FF:000008; speckle targeted PIP5K1A-regulated poly(A) polymerase; 1.
DR   FunFam; 3.30.70.330:FF:000305; speckle targeted PIP5K1A-regulated poly(A) polymerase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR054708; MTPAP-like_central.
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; PF22600; MTPAP-like_central; 2.
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.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          56..128
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
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          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        259..269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//