UniProtKB - Q6DJE4 (CPSF5_XENLA)
Protein
Cleavage and polyadenylation specificity factor subunit 5
Gene
nudt21
Organism
Xenopus laevis (African clawed frog)
Status
Functioni
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. 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). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. 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. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function. Binds to chromatin. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides.By similarity
Caution
Lacks the conserved metal-binding residues in the NUDIX motif and is not expected to have hydrolase activity.Curated
GO - Molecular functioni
- hydrolase activity Source: InterPro
- identical protein binding Source: UniProtKB
- mRNA 3'-UTR AU-rich region binding Source: UniProtKB
- mRNA binding Source: UniProtKB
GO - Biological processi
- cell differentiation Source: UniProtKB-KW
- messenger ribonucleoprotein complex assembly Source: UniProtKB
- mRNA alternative polyadenylation Source: UniProtKB
- mRNA polyadenylation Source: InterPro
- mRNA processing Source: UniProtKB
- positive regulation of mRNA cleavage Source: UniProtKB
- positive regulation of mRNA polyadenylation Source: UniProtKB
- positive regulation of pro-B cell differentiation Source: UniProtKB
- positive regulation of stem cell differentiation Source: UniProtKB
- posttranscriptional regulation of gene expression Source: UniProtKB
- protein heterotetramerization Source: UniProtKB
Keywordsi
Molecular function | RNA-binding |
Biological process | Differentiation, mRNA processing |
Names & Taxonomyi
Protein namesi | Recommended name: Cleavage and polyadenylation specificity factor subunit 5By similarityAlternative name(s): Nudix hydrolase 21By similarity |
Gene namesi | Name:nudt21By similarity Synonyms:cpsf5By similarity |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Organism-specific databases
Xenbasei | XB-GENE-921424, nudt21.L |
Subcellular locationi
Nucleus
- mRNA cleavage factor complex Source: UniProtKB
- nucleus Source: UniProtKB
- paraspeckles Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000057155 | 1 – 227 | Cleavage and polyadenylation specificity factor subunit 5Add BLAST | 227 |
Proteomic databases
MaxQBi | Q6DJE4 |
Interactioni
Subunit structurei
Homodimer (via N- and C-terminus); binds RNA as homodimer.
Component of the cleavage factor Im (CFIm) complex.
By similaritySites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 55 | Interaction with RNABy similarity | 1 | |
Sitei | 63 | Interaction with RNABy similarity | 1 |
GO - Molecular functioni
- identical protein binding Source: UniProtKB
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 76 – 201 | Nudix hydrolasePROSITE-ProRule annotationAdd BLAST | 126 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 102 – 104 | Interaction with RNABy similarity | 3 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 109 – 130 | Nudix boxAdd BLAST | 22 |
Sequence similaritiesi
Phylogenomic databases
OMAi | EWEIGDC |
OrthoDBi | 1194206at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR016706, Cleav_polyA_spec_factor_su5 IPR015797, NUDIX_hydrolase-like_dom_sf IPR000086, NUDIX_hydrolase_dom |
PANTHERi | PTHR13047, PTHR13047, 1 hit |
Pfami | View protein in Pfam PF13869, NUDIX_2, 1 hit |
PIRSFi | PIRSF017888, CPSF-25, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit |
i Sequence
Sequence statusi: Complete.
Q6DJE4-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSVLPPNRSQ TGWPRGVNQF GNKYLQQTKP LTLERTINLY PLTNYTFGTK
60 70 80 90 100
EPLYEKDSSV AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG
110 120 130 140 150
TTFFKLPGGE LNPGEDEVEG LKRLMTEILG RQDGVQQDWV IDDCIGNWWR
160 170 180 190 200
PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ EKALFAVPKN YKLVAAPLFE
210 220
LYDNAPGYGP IISSLPQLLS RFNFIYN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC075235 mRNA Translation: AAH75235.1 |
RefSeqi | NP_001086401.1, NM_001092932.1 |
Genome annotation databases
GeneIDi | 444830 |
KEGGi | xla:444830 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC075235 mRNA Translation: AAH75235.1 |
RefSeqi | NP_001086401.1, NM_001092932.1 |
3D structure databases
SMRi | Q6DJE4 |
ModBasei | Search... |
Proteomic databases
MaxQBi | Q6DJE4 |
Genome annotation databases
GeneIDi | 444830 |
KEGGi | xla:444830 |
Organism-specific databases
CTDi | 444830 |
Xenbasei | XB-GENE-921424, nudt21.L |
Phylogenomic databases
OMAi | EWEIGDC |
OrthoDBi | 1194206at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR016706, Cleav_polyA_spec_factor_su5 IPR015797, NUDIX_hydrolase-like_dom_sf IPR000086, NUDIX_hydrolase_dom |
PANTHERi | PTHR13047, PTHR13047, 1 hit |
Pfami | View protein in Pfam PF13869, NUDIX_2, 1 hit |
PIRSFi | PIRSF017888, CPSF-25, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CPSF5_XENLA | |
Accessioni | Q6DJE4Primary (citable) accession number: Q6DJE4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 7, 2006 |
Last sequence update: | August 16, 2004 | |
Last modified: | December 2, 2020 | |
This is version 80 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |