CPSF5_BOVIN
ID CPSF5_BOVIN Reviewed; 227 AA.
AC Q3ZCA2;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 5;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 21;
DE Short=Nudix motif 21;
GN Name=NUDT21; Synonyms=CPSF5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that
CC functions as an activator of the pre-mRNA 3'-end cleavage and
CC polyadenylation processing required for the maturation of pre-mRNA into
CC functional mRNAs. CFIm contributes to the recruitment of multiprotein
CC complexes on specific sequences on the pre-mRNA 3'-end, so called
CC cleavage and polyadenylation signals (pA signals). Most pre-mRNAs
CC contain multiple pA signals, resulting in alternative cleavage and
CC polyadenylation (APA) producing mRNAs with variable 3'-end formation.
CC The CFIm complex acts as a key regulator of cleavage and
CC polyadenylation site choice during APA through its binding to 5'-UGUA-
CC 3' elements localized in the 3'-untranslated region (UTR) for a huge
CC number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-
CC processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-
CC UGUA-3' elements localized upstream of pA signals that act as enhancers
CC of pre-mRNA 3'-end processing. The homodimer mediates simultaneous
CC sequence-specific recognition of two 5'-UGUA-3' elements within the
CC pre-mRNA. Plays a role in somatic cell fate transitions and
CC pluripotency by regulating widespread changes in gene expression
CC through an APA-dependent function. Binds to chromatin. Binds to, but
CC does not hydrolyze mono- and di-adenosine nucleotides.
CC {ECO:0000250|UniProtKB:O43809, ECO:0000250|UniProtKB:Q9CQF3}.
CC -!- SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer.
CC Component of the cleavage factor Im (CFIm) complex which is a
CC heterotetramer composed of two subunits of NUDT21/CPSF5 and two
CC subunits of CPSF6 or CPSF7 or a heterodimer of CPSF6 and CPSF7. The
CC cleavage factor Im (CFIm) complex associates with the CPSF and CSTF
CC complexes to promote the assembly of the core mRNA 3'-processing
CC machinery. Interacts with CPSF6 (via the RRM domain); this interaction
CC is direct and enhances binding to RNA. Interacts with CPSF7. Interacts
CC with FIP1L1; this interaction occurs in a RNA sequence-specific manner.
CC Interacts with PABPN1. Interacts (via N-terminus) with PAPOLA (via C-
CC terminus); this interaction is direct and diminished by acetylation.
CC Interacts with SNRNP70. Interacts with VIRMA.
CC {ECO:0000250|UniProtKB:O43809}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43809}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43809}. Note=Shuttles between the nucleus and
CC the cytoplasm in a transcription- and XPO1/CRM1-independent manner,
CC most probably in complex with the cleavage factor Im complex (CFIm). In
CC punctate subnuclear structures localized adjacent to nuclear speckles,
CC called paraspeckles. {ECO:0000250|UniProtKB:O43809}.
CC -!- PTM: Acetylated mainly by p300/CBP, recruited to the complex by CPSF6.
CC Acetylation decreases interaction with PAPAO. Deacetylated by the class
CC I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1
CC AND SIRT2. {ECO:0000250|UniProtKB:O43809}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved metal-binding residues in the NUDIX motif
CC and is not expected to have hydrolase activity. {ECO:0000305}.
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DR EMBL; BC102697; AAI02698.1; -; mRNA.
DR RefSeq; NP_001030408.1; NM_001035331.2.
DR AlphaFoldDB; Q3ZCA2; -.
DR SMR; Q3ZCA2; -.
DR STRING; 9913.ENSBTAP00000013467; -.
DR PaxDb; Q3ZCA2; -.
DR PeptideAtlas; Q3ZCA2; -.
DR PRIDE; Q3ZCA2; -.
DR Ensembl; ENSBTAT00000013467; ENSBTAP00000013467; ENSBTAG00000010207.
DR GeneID; 518859; -.
DR KEGG; bta:518859; -.
DR CTD; 11051; -.
DR VEuPathDB; HostDB:ENSBTAG00000010207; -.
DR VGNC; VGNC:32336; NUDT21.
DR eggNOG; KOG1689; Eukaryota.
DR GeneTree; ENSGT00390000015814; -.
DR HOGENOM; CLU_068704_2_1_1; -.
DR InParanoid; Q3ZCA2; -.
DR OMA; EHYEQYG; -.
DR OrthoDB; 1194206at2759; -.
DR TreeFam; TF106356; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000010207; Expressed in oocyte and 110 other tissues.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:Ensembl.
DR GO; GO:0005849; C:mRNA cleavage factor complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042382; C:paraspeckles; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; ISS:UniProtKB.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; ISS:UniProtKB.
DR GO; GO:0031439; P:positive regulation of mRNA cleavage; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:2000975; P:positive regulation of pro-B cell differentiation; IEA:Ensembl.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:Ensembl.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR13047; PTHR13047; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR PIRSF; PIRSF017888; CPSF-25; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Methylation; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT CHAIN 2..227
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 5"
FT /id="PRO_0000057149"
FT DOMAIN 76..201
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 2..147
FT /note="Necessary for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT REGION 81..160
FT /note="Necessary for interactions with PAPOLA and PABPN1"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT REGION 102..104
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOTIF 109..130
FT /note="Nudix box"
FT SITE 55
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT SITE 63
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT SITE 208
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOD_RES 15
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOD_RES 40
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43809"
SQ SEQUENCE 227 AA; 26227 MW; D204243E57F1CCC5 CRC64;
MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK EPLYEKDSSV
AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG TTFFKLPGGE LNPGEDEVEG
LKRLMTEILG RQDGVLQDWV IDDCIGNWWR PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ
EKALFAVPKN YKLVAAPLFE LYDNAPGYGP IISSLPQLLS RFNFIYN
