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    Rngtt RNA guanylyltransferase and 5'-phosphatase [ Mus musculus (house mouse) ]

    Gene ID: 24018, updated on 9-Dec-2024

    Summary

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    Official Symbol
    Rngttprovided by MGI
    Official Full Name
    RNA guanylyltransferase and 5'-phosphataseprovided by MGI
    Primary source
    MGI:MGI:1329041
    See related
    Ensembl:ENSMUSG00000028274 AllianceGenome:MGI:1329041
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Mus musculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
    Also known as
    HCE; MCE1
    Summary
    Predicted to enable inorganic triphosphate phosphatase activity and mRNA guanylyltransferase activity. Predicted to be involved in 7-methylguanosine mRNA capping. Predicted to be located in nucleus. Is expressed in several structures, including heart; liver; lung; metanephros; and spleen. Orthologous to human RNGTT (RNA guanylyltransferase and 5'-phosphatase). [provided by Alliance of Genome Resources, Dec 2024]
    Expression
    Ubiquitous expression in CNS E11.5 (RPKM 2.4), CNS E14 (RPKM 2.1) and 28 other tissues See more
    Orthologs
    human all
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    Genomic context

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    See Rngtt in Genome Data Viewer
    Location:
    4 A5; 4 14.78 cM
    Exon count:
    22
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 4 NC_000070.7 (33310300..33502610)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 4 NC_000070.6 (33310300..33502614)

    Chromosome 4 - NC_000070.7Genomic Context describing neighboring genes Neighboring gene serine and arginine-rich splicing factor 12 Neighboring gene STARR-positive B cell enhancer ABC_E9235 Neighboring gene STARR-positive B cell enhancer ABC_E6159 Neighboring gene STARR-seq mESC enhancer starr_09889 Neighboring gene STARR-seq mESC enhancer starr_09890 Neighboring gene proline-rich nuclear receptor coactivator 1 Neighboring gene STARR-seq mESC enhancer starr_09892 Neighboring gene STARR-positive B cell enhancer ABC_E833 Neighboring gene STARR-seq mESC enhancer starr_09894 Neighboring gene STARR-seq mESC enhancer starr_09895 Neighboring gene STARR-seq mESC enhancer starr_09897 Neighboring gene microRNA 8118 Neighboring gene predicted gene, 52726 Neighboring gene STARR-seq mESC enhancer starr_09900 Neighboring gene predicted gene, 32893

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism. Wen Y, et al. Proc Natl Acad Sci U S A, 1998 Oct 13. PMID 9770468, Free PMC Article
    2. Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. Changela A, et al. EMBO J, 2001 May 15. PMID 11350947, Free PMC Article
    3. Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Yue Z, et al. Proc Natl Acad Sci U S A, 1997 Nov 25. PMID 9371772, Free PMC Article
    4. Functional characterization of the C-terminal domain of mouse capping enzyme. Liu L. Cell Biochem Funct, 2006 Mar-Apr. PMID 16342145
    5. The cytoplasmic capping complex assembles on adapter protein nck1 bound to the proline-rich C-terminus of Mammalian capping enzyme. Mukherjee C, et al. PLoS Biol, 2014 Aug. PMID 25137142, Free PMC Article

    See all (28) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Variation

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    Alleles

    Alleles of this type are documented at Mouse Genome Informatics  (MGI)
    • Endonuclease-mediated (1) 
    • Gene trapped (1) 

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by MGI

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables GTP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA guanylyltransferase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables inorganic triphosphate phosphatase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables inorganic triphosphate phosphatase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    enables mRNA 5'-triphosphate monophosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables mRNA guanylyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables mRNA guanylyltransferase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables mRNA guanylyltransferase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    enables phosphoprotein phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables polynucleotide 5'-phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in 7-methylguanosine mRNA capping IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in 7-methylguanosine mRNA capping ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in 7-methylguanosine mRNA capping ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in RNA processing ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    mRNA-capping enzyme
    NP_001292202.1
    NP_001413065.1
    NP_001413066.1
    NP_036014.1
    XP_006537952.1
    XP_006537953.1
    XP_011248317.1
    XP_017175678.2
    XP_030109377.1
    XP_036019988.1
    XP_036019989.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001305273.2 → NP_001292202.1  mRNA-capping enzyme isoform 2

      See identical proteins and their annotated locations for NP_001292202.1

      Status: VALIDATED

      Source sequence(s)
      AC093925, AL772272, BX842672
      Consensus CDS
      CCDS84712.1
      UniProtKB/TrEMBL
      Q3UCK1, Q9DCC1
      Related
      ENSMUSP00000029942.8, ENSMUST00000029942.8
      Conserved Domains (3) summary
      cd07895
      Location:248 → 461
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      pfam03919
      Location:465 → 545
      mRNA_cap_C; mRNA capping enzyme, C-terminal domain
      cl21483
      Location:47 → 143
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    2. NM_001426136.1 → NP_001413065.1  mRNA-capping enzyme isoform 3

      Status: VALIDATED

      Source sequence(s)
      AC093925, AL772272, BX842672
      UniProtKB/TrEMBL
      Q3UCK1

    3. NM_001426137.1 → NP_001413066.1  mRNA-capping enzyme isoform 4

      Status: VALIDATED

      Source sequence(s)
      AC093925, AL772272, BX842672
      UniProtKB/TrEMBL
      Q3UCK1

    4. NM_011884.4 → NP_036014.1  mRNA-capping enzyme isoform 1

      See identical proteins and their annotated locations for NP_036014.1

      Status: VALIDATED

      Source sequence(s)
      AC093925, AL772272, BX842672
      Consensus CDS
      CCDS38705.1
      UniProtKB/Swiss-Prot
      O55236
      UniProtKB/TrEMBL
      Q3UA94, Q3UCK1
      Related
      ENSMUSP00000103788.3, ENSMUST00000108153.9
      Conserved Domains (3) summary
      cd07895
      Location:248 → 461
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      pfam03919
      Location:465 → 558
      mRNA_cap_C; mRNA capping enzyme, C-terminal domain
      cl21483
      Location:47 → 143
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

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

    Reference GRCm39 C57BL/6J

    Genomic

    1. NC_000070.7 Reference GRCm39 C57BL/6J

      Range
      33310300..33502610
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_017320189.3 → XP_017175678.2  mRNA-capping enzyme isoform X3

      UniProtKB/TrEMBL
      Q3TUK6
      Conserved Domains (2) summary
      cd07895
      Location:238 → 451
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      cl28904
      Location:45 → 165
      PTP_DSP_cys; cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily

    2. XM_030253517.1 → XP_030109377.1  mRNA-capping enzyme isoform X7

      Conserved Domains (2) summary
      cd07895
      Location:238 → 414
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      cl28904
      Location:45 → 165
      PTP_DSP_cys; cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily

    3. XM_036164096.1 → XP_036019989.1  mRNA-capping enzyme isoform X2

      UniProtKB/TrEMBL
      Q3TUK6
      Conserved Domains (2) summary
      cd07895
      Location:248 → 461
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      cd17664
      Location:9 → 175
      Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

    4. XM_036164095.1 → XP_036019988.1  mRNA-capping enzyme isoform X1

      UniProtKB/TrEMBL
      Q3TUK6
      Conserved Domains (2) summary
      cd07895
      Location:248 → 461
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      cd17664
      Location:9 → 175
      Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

    5. XM_006537889.5 → XP_006537952.1  mRNA-capping enzyme isoform X4

      UniProtKB/TrEMBL
      Q3TUK6
      Conserved Domains (2) summary
      cd07895
      Location:248 → 447
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      cd17664
      Location:9 → 175
      Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

    6. XM_006537890.4 → XP_006537953.1  mRNA-capping enzyme isoform X5

      UniProtKB/TrEMBL
      Q3TUK6
      Conserved Domains (2) summary
      cd07895
      Location:248 → 456
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      cd17664
      Location:9 → 175
      Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme

    7. XM_011250015.3 → XP_011248317.1  mRNA-capping enzyme isoform X6

      UniProtKB/TrEMBL
      Q3TUK6
      Conserved Domains (2) summary
      cd07895
      Location:248 → 424
      Adenylation_mRNA_capping; Adenylation domain of GTP-dependent mRNA capping enzymes
      cd17664
      Location:9 → 175
      Mce1_N; N-terminal triphosphatase domain of mRNA capping enzyme
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    O55236.1 GenPept UniProtKB/Swiss-Prot:O55236

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