Mouse Gene A1cf (ENSMUST00000224564.1) from GENCODE VM23 Comprehensive Transcript Set (only Basic displayed by default)
  Description: Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also seems to protect the edited APOB mRNA from nonsense-mediated decay (By similarity). (from UniProt Q5YD48)
Gencode Transcript: ENSMUST00000224564.1
Gencode Gene: ENSMUSG00000052595.8
Transcript (Including UTRs)
   Position: mm10 chr19:31,868,764-31,932,848 Size: 64,085 Total Exon Count: 8 Strand: +
Coding Region
   Position: mm10 chr19:31,893,100-31,932,712 Size: 39,613 Coding Exon Count: 7 

Page IndexSequence and LinksUniProtKB CommentsPrimersCTDRNA Structure
Protein StructureOther SpeciesGO AnnotationsmRNA DescriptionsPathwaysOther Names
Model InformationMethods
Data last updated at UCSC: 2019-09-19

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr19:31,868,764-31,932,848)mRNA (may differ from genome)Protein (384 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneTable SchemaAlphaFold
BioGPSEnsemblExonPrimerGeneCardsMGIPubMed
ReactomeSOURCEUniProtKBWikipedia

-  Comments and Description Text from UniProtKB
  ID: A1CF_MOUSE
DESCRIPTION: RecName: Full=APOBEC1 complementation factor; AltName: Full=APOBEC1-stimulating protein;
FUNCTION: Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also seems to protect the edited APOB mRNA from nonsense-mediated decay (By similarity).
SUBUNIT: Part of the apolipoprotein B mRNA editing complex with APOBEC1. Interacts with TNPO2; TNPO2 may be responsible for transport of A1CF into the nucleus. Interacts with SYNCRIP. Interacts with CELF2/CUGBP2 (By similarity).
SUBCELLULAR LOCATION: Nucleus (By similarity). Endoplasmic reticulum (By similarity). Cytoplasm (By similarity). Note=Predominantly nuclear where it localizes to heterochromatin. Also cytoplasmic where it is found at the outer surface of the endoplasmic reticulum. Shuttles between the nucleus and cytoplasm. May be transported into the nucleus by the nuclear import protein TNPO2/TRN2 or by APOBEC1 (By similarity).
TISSUE SPECIFICITY: Expressed primarily in liver, small intestine and kidney.
DOMAIN: The RRM domains are necessary but not sufficient for binding to APOB mRNA. Additional residues in the pre-RRM and C- terminal regions are required for RNA-binding and for complementing APOBEC1 activity (By similarity).
DISRUPTION PHENOTYPE: Mice display embryonic lethality at E3.5 due to failure of embryos to implant.
SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.

-  Primer design for this transcript
 

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Click here to load the transcript sequence and exon structure into Primer3Plus

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To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -25.90141-0.184 Picture PostScript Text
3' UTR -21.20136-0.156 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR014720 - dsRNA-bd-like
IPR006535 - HnRNP_R/Q_splicing_fac
IPR012677 - Nucleotide-bd_a/b_plait
IPR000504 - RRM_dom

Pfam Domains:
PF00076 - RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)
PF13893 - RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)

SCOP Domains:
50249 - Nucleic acid-binding proteins
55658 - L9 N-domain-like
160387 - NosL/MerB-like
54928 - RNA-binding domain, RBD
55608 - Homing endonucleases

ModBase Predicted Comparative 3D Structure on Q5YD48
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The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
HumanRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologGenome BrowserNo orthologNo orthologNo orthologNo ortholog
Gene Details     
Gene Sorter     
 RGD    
 Protein Sequence    
 Alignment    

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003676 nucleic acid binding
GO:0003723 RNA binding
GO:0003727 single-stranded RNA binding
GO:0003729 mRNA binding
GO:0005515 protein binding
GO:0003725 double-stranded RNA binding

Biological Process:
GO:0006397 mRNA processing
GO:0007566 embryo implantation
GO:0010609 mRNA localization resulting in posttranscriptional regulation of gene expression
GO:0016554 cytidine to uridine editing
GO:0016556 mRNA modification
GO:0050821 protein stabilization

Cellular Component:
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005720 nuclear heterochromatin
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0030895 apolipoprotein B mRNA editing enzyme complex
GO:0045293 mRNA editing complex


-  Descriptions from all associated GenBank mRNAs
  AY566864 - Mus musculus truncated APOBEC-1 stimulating protein (Asp) mRNA, complete cds, alternatively spliced.
AY566862 - Mus musculus APOBEC-1 stimulating protein (Asp) mRNA, complete cds, alternatively spliced.
AY566863 - Mus musculus APOBEC-1 stimulating protein (Asp) mRNA, complete cds, alternatively spliced.
AK007970 - Mus musculus 10 day old male pancreas cDNA, RIKEN full-length enriched library, clone:1810073H04 product:weakly similar to APOBEC-1 COMPLEMENTATION FACTOR SHORT ISOFORM [Rattus norvegicus], full insert sequence.
BC089622 - Mus musculus APOBEC1 complementation factor, mRNA (cDNA clone MGC:107689 IMAGE:6760455), complete cds.
BC038942 - Mus musculus RIKEN cDNA 1810073H04 gene, mRNA (cDNA clone IMAGE:4241227), partial cds.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q5YD48 (Reactome details) participates in the following event(s):

R-MMU-77608 Binding of A1CF to stem-looped RNA
R-MMU-77609 Binding of APOBEC-1 to form editosome
R-MMU-83677 C4 deamination of cytidine
R-MMU-75094 Formation of the Editosome
R-MMU-72200 mRNA Editing: C to U Conversion
R-MMU-75072 mRNA Editing
R-MMU-8953854 Metabolism of RNA

-  Other Names for This Gene
  Alternate Gene Symbols: A1CF_MOUSE, Acf, Asp, BC089622, E9QJS8, Q5FW55, Q5YD47, Q5YD48, uc008het.1, uc008het.2
UCSC ID: uc008het.2
RefSeq Accession: NM_001365078
Protein: Q5YD48 (aka A1CF_MOUSE)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.