Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3′-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085, PubMed:8626397, PubMed:9659921). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3′-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:14690600, PubMed:17024186, PubMed:8626397, PubMed:9659921). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3′-end formation (PubMed:17098938, PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5′-UGUA-3′ elements localized in the 3′-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:17098938, PubMed:20695905, PubMed:29276085). NUDT21/CPSF5 activates indirectly the mRNA 3′-processing machinery by recruiting CPSF6 and/or CPSF7 (PubMed:29276085). Binds to 5′-UGUA-3′ elements localized upstream of pA signals that act as enhancers of pre-mRNA 3′-end processing (PubMed:14690600, PubMed:15169763, PubMed:17024186, PubMed:20479262, PubMed:22813749, PubMed:8626397). The homodimer mediates simultaneous sequence-specific recognition of two 5′-UGUA-3′ elements within the pre-mRNA (PubMed:20479262, PubMed:21295486). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (By similarity). Binds to chromatin (By similarity). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (PubMed:18445629).
