CPSF5_XENLA
ID CPSF5_XENLA Reviewed; 227 AA.
AC Q6DJE4;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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}.
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DR EMBL; BC075235; AAH75235.1; -; mRNA.
DR RefSeq; NP_001086401.1; NM_001092932.1.
DR AlphaFoldDB; Q6DJE4; -.
DR SMR; Q6DJE4; -.
DR BioGRID; 102993; 1.
DR MaxQB; Q6DJE4; -.
DR PRIDE; Q6DJE4; -.
DR DNASU; 444830; -.
DR GeneID; 444830; -.
DR KEGG; xla:444830; -.
DR CTD; 444830; -.
DR Xenbase; XB-GENE-921424; nudt21.L.
DR OMA; EHYEQYG; -.
DR OrthoDB; 1194206at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 444830; Expressed in egg cell and 19 other tissues.
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..227
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 5"
FT /id="PRO_0000057155"
FT DOMAIN 76..201
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
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"
SQ SEQUENCE 227 AA; 26269 MW; 643A56172FA9A50B CRC64;
MSVLPPNRSQ TGWPRGVNQF GNKYLQQTKP LTLERTINLY PLTNYTFGTK EPLYEKDSSV
AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG TTFFKLPGGE LNPGEDEVEG
LKRLMTEILG RQDGVQQDWV IDDCIGNWWR PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ
EKALFAVPKN YKLVAAPLFE LYDNAPGYGP IISSLPQLLS RFNFIYN
