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cpsf-3 Cleavage and polyadenylation specificity factor subunit 3 [ Caenorhabditis elegans ]

Gene ID: 178285, updated on 25-Apr-2024

Summary

Gene symbol
cpsf-3
Gene description
Cleavage and polyadenylation specificity factor subunit 3
Primary source
WormBase:WBGene00013460
Locus tag
CELE_Y67H2A.1
See related
AllianceGenome:WB:WBGene00013460
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Predicted to enable 5'-3' exonuclease activity; RNA binding activity; and endoribonuclease activity. Predicted to be involved in mRNA 3'-end processing by stem-loop binding activity and cleavage and mRNA polyadenylation. Predicted to be located in nucleus. Predicted to be part of mRNA cleavage and polyadenylation specificity factor complex. Is expressed in excretory cell; intestine; spermathecal-uterine junction; and tail. Orthologous to human CPSF3 (cleavage and polyadenylation specific factor 3). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

Location:
chromosome: IV
Exon count:
10
Sequence:
Chromosome: IV; NC_003282.8 (13273846..13282878, complement)

Chromosome IV - NC_003282.8Genomic Context describing neighboring genes Neighboring gene Transmembrane protein Neighboring gene Transmembrane protein Neighboring gene Synaptojanin Neighboring gene C2H2-type domain-containing protein Neighboring gene Kelch domain-containing protein 10

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables 5'-3' RNA exonuclease activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables RNA binding IBA
Inferred from Biological aspect of Ancestor
more info
 
enables RNA endonuclease activity IBA
Inferred from Biological aspect of Ancestor
more info
 
Process Evidence Code Pubs
involved_in RNA metabolic process IEA
Inferred from Electronic Annotation
more info
 
involved_in mRNA 3'-end processing by stem-loop binding and cleavage IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in mRNA processing IEA
Inferred from Electronic Annotation
more info
 
involved_in macromolecule biosynthetic process IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
part_of mRNA cleavage and polyadenylation specificity factor complex IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
Cleavage and polyadenylation specificity factor subunit 3
NP_502553.2
  • Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003282.8 Reference assembly

    Range
    13273846..13282878 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_070152.6NP_502553.2  Cleavage and polyadenylation specificity factor subunit 3 [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_502553.2

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q95PY8
    Conserved Domains (5) summary
    smart01027
    Location:247368
    Beta-Casp; Beta-Casp domain
    smart01098
    Location:477694
    CPSF73-100_C; This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins
    COG1236
    Location:13456
    YSH1; RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis]
    pfam07521
    Location:381421
    RMMBL; RNA-metabolizing metallo-beta-lactamase
    cd16292
    Location:11206
    CPSF3-like_MBL-fold; cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain