UniProt functional annotation for P25500



	UniProt functional annotation for P25500

UniProt code: P25500.

Organism: Bos taurus (Bovine).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C- terminus. {ECO:0000250|UniProtKB:P51003, ECO:0000269|PubMed:9463383}.

Catalytic activity: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:11128, Rhea:RHEA-COMP:14647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83400, ChEBI:CHEBI:140626; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:15328606};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15328606}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15328606}; Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000269|PubMed:15328606};

Biophysicochemical properties: Kinetic parameters: KM=0.229 mM for ATP {ECO:0000269|PubMed:15328606};

Subunit: Monomer (PubMed:10944102, PubMed:15328606). Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and FIP1L1; the interaction with AHCYL1 seems to increase interaction with FIP1L1 (By similarity). Interacts with NUDT21; the interaction is diminished by acetylation (PubMed:17172643). Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP (PubMed:17172643). {ECO:0000250|UniProtKB:P51003, ECO:0000250|UniProtKB:Q61183, ECO:0000269|PubMed:10944102, ECO:0000269|PubMed:15328606, ECO:0000269|PubMed:17172643}.

Subcellular location: Nucleus {ECO:0000269|PubMed:17172643}.

Ptm: Polysumoylated. Varying sumolyation depending on tissue- and cell- type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity). {ECO:0000250}.

Ptm: Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity). {ECO:0000250}.

Ptm: Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex. {ECO:0000269|PubMed:17172643}.

Similarity: Belongs to the poly(A) polymerase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bos taurus (Bovine).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.



Function:		Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C- terminus. {ECO:0000250\|UniProtKB:P51003, ECO:0000269\|PubMed:9463383}.


Catalytic activity:		Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:11128, Rhea:RHEA-COMP:14647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83400, ChEBI:CHEBI:140626; EC=2.7.7.19; Evidence={ECO:0000269\|PubMed:15328606};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:15328606}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269\|PubMed:15328606}; Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000269\|PubMed:15328606};
Biophysicochemical properties:		Kinetic parameters: KM=0.229 mM for ATP {ECO:0000269\|PubMed:15328606};
Subunit:		Monomer (PubMed:10944102, PubMed:15328606). Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and FIP1L1; the interaction with AHCYL1 seems to increase interaction with FIP1L1 (By similarity). Interacts with NUDT21; the interaction is diminished by acetylation (PubMed:17172643). Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP (PubMed:17172643). {ECO:0000250\|UniProtKB:P51003, ECO:0000250\|UniProtKB:Q61183, ECO:0000269\|PubMed:10944102, ECO:0000269\|PubMed:15328606, ECO:0000269\|PubMed:17172643}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:17172643}.
Ptm:		Polysumoylated. Varying sumolyation depending on tissue- and cell- type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity). {ECO:0000250}.
Ptm:		Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity). {ECO:0000250}.
Ptm:		Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex. {ECO:0000269\|PubMed:17172643}.
Similarity:		Belongs to the poly(A) polymerase family. {ECO:0000305}.