CPSF5_DANRE
ID CPSF5_DANRE Reviewed; 228 AA.
AC Q7T3C6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000250|UniProtKB:O43809};
DE AltName: Full=Nudix hydrolase 21 {ECO:0000250|UniProtKB:O43809};
GN Name=nudt21 {ECO:0000250|UniProtKB:O43809};
GN Synonyms=cpsf5 {ECO:0000250|UniProtKB:O43809};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) 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. Binds to 5'-UGUA-3' elements localized upstream of
CC pA signals that act as enhancers of pre-mRNA 3'-end processing. The
CC homodimer mediates simultaneous sequence-specific recognition of two
CC 5'-UGUA-3' elements within the pre-mRNA. Plays a role in somatic cell
CC fate transitions and pluripotency by regulating widespread changes in
CC gene expression through an APA-dependent function. Binds to chromatin.
CC Binds to, but 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.
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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC053172; AAH53172.1; -; mRNA.
DR RefSeq; NP_957411.1; NM_201117.1.
DR AlphaFoldDB; Q7T3C6; -.
DR SMR; Q7T3C6; -.
DR STRING; 7955.ENSDARP00000017229; -.
DR PaxDb; Q7T3C6; -.
DR Ensembl; ENSDART00000023721; ENSDARP00000017229; ENSDARG00000003153.
DR GeneID; 394092; -.
DR KEGG; dre:394092; -.
DR CTD; 11051; -.
DR ZFIN; ZDB-GENE-040426-1316; nudt21.
DR eggNOG; KOG1689; Eukaryota.
DR GeneTree; ENSGT00390000015814; -.
DR HOGENOM; CLU_068704_2_1_1; -.
DR InParanoid; Q7T3C6; -.
DR OMA; EHYEQYG; -.
DR OrthoDB; 1194206at2759; -.
DR PhylomeDB; Q7T3C6; -.
DR TreeFam; TF106356; -.
DR Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DRE-72187; mRNA 3'-end processing.
DR Reactome; R-DRE-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DRE-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q7T3C6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000003153; Expressed in testis and 28 other tissues.
DR ExpressionAtlas; Q7T3C6; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS:UniProtKB.
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 Cytoplasm; Differentiation; mRNA processing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..228
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 5"
FT /id="PRO_0000057154"
FT DOMAIN 77..202
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 103..105
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOTIF 110..131
FT /note="Nudix box"
FT SITE 56
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT SITE 64
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
SQ SEQUENCE 228 AA; 26272 MW; 3ADFD7E8CB397C4D CRC64;
MSVVPPNRSS TGWPRGVNQF GNKYITQATK PLTLERTINL YPLTNYTFGT KEPLYEKDSS
VAARFQRMRE EFEKIGMRRT VEGVLIVHEH RLPHVLLLQL GTTFFKLPGG ELNPGEDEVE
GLKRLMTEIL GRQDGVKQDW VIDDCIGNWW RPNFEPPQYP YIPAHITKPK EHKKLFLVQL
QEKALFAVPK NYKLVAAPLF ELYDNAPGYG PIISSLPQLL SRFNFIYN
