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Cleavage and polyadenylation specificity factor subunit 5Known also as: Cleavage and polyadenylation specificity factor 25 kDa subunit, Nucleoside diphosphate-linked moiety X motif 21, Nudix motif 21, Pre-mRNA cleavage factor Im 25 kDa subunit Known abbreviations: CPSF5, CFIm25, CPSF25, NUDT21 Yeast homolog: not known Protein
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Sequence: 1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130 MSVVPPNRSQTGWPRGVTQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILG RQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN Gene location: 16q12.2 Summary NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export. Component of the cleavage factor Im (CFIm) complex, composed of, at least, NUDT21/CPSF5 and CPSF6 or CPSF7. Within the cleavage factor Im complex, the NUDT21/CPSF5 homodimer is at the core of a heterotetramer, and is clasped by two additional subunits (CPSF6 or CPSF7). Residues 81–160 of CFIm25 mediate interactions with the C-terminus of PAP (residues 472–739) and PABP. The primary function of CF Im may be to provide additional recognition of the pre-mRNA substrate and aid the definition of the proper polyadenylation site. SELEX analysis revealed that CF Im prefers to bind to the RNA sequences containing UGUAA, which is generally found just upstream of the PAS. Interacts with CPSF6, CPSF7, PABPN1 and SNRNP70. Interacts with PAPOLA (the interaction is diminished by acetylation). Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2. Althught it contains NUDIX hydrolase domain, it lacks the conserved metal-binding residues in the NUDIX motif and does not have hydrolase activity. See this protein in other databases: Literature:
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