UniProt ID: Q4KMD7 |
FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. {ECO:0000250|UniProtKB:Q9H6E5}. CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NVV4}; Note=Binds 1 divalent cation per subunit. {ECO:0000250|UniProtKB:Q9H6E5}; SUBUNIT: Associates with the cleavage and polyadenylation specificity factor (CPSF) complex. {ECO:0000250|UniProtKB:Q9H6E5}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H6E5}. DOMAIN: The zinc-finger domain is required for terminal uridylyltransferase activity. Together with the RRM domain, binds the 5'-area of U6 snRNA. {ECO:0000250|UniProtKB:Q9H6E5}. DOMAIN: The RRM domain is required for terminal uridylyltransferase activity. Together with the zinc-finger domain, binds the 5'-area of U6 snRNA. {ECO:0000250|UniProtKB:Q9H6E5}. SIMILARITY: Belongs to the DNA polymerase type-B-like family. {ECO:0000305}. |
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