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    Pars2 prolyl-tRNA synthetase 2, mitochondrial [ Rattus norvegicus (Norway rat) ]

    Gene ID: 313429, updated on 9-Dec-2024

    Summary

    Official Symbol
    Pars2provided by RGD
    Official Full Name
    prolyl-tRNA synthetase 2, mitochondrialprovided by RGD
    Primary source
    RGD:1305345
    See related
    EnsemblRapid:ENSRNOG00000007327 AllianceGenome:RGD:1305345
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Rattus norvegicus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
    Also known as
    RGD1305345
    Summary
    Predicted to enable proline-tRNA ligase activity. Predicted to be involved in prolyl-tRNA aminoacylation. Predicted to be located in mitochondrial matrix. Predicted to be active in mitochondrion. Human ortholog(s) of this gene implicated in developmental and epileptic encephalopathy 75. Orthologous to human PARS2 (prolyl-tRNA synthetase 2, mitochondrial). [provided by Alliance of Genome Resources, Dec 2024]
    Expression
    Biased expression in Adrenal (RPKM 35.4), Thymus (RPKM 28.9) and 9 other tissues See more
    Orthologs
    NEW
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    Try the new Transcript table

    Genomic context

    See Pars2 in Genome Data Viewer
    Location:
    5q34
    Exon count:
    2
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCr8 (GCF_036323735.1) 5 NC_086023.1 (126662882..126667981)
    RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 5 NC_051340.1 (121433993..121439158)
    106 previous assembly Rnor_6.0 (GCF_000001895.5) 5 NC_005104.4 (126254090..126259204)

    Chromosome 5 - NC_086023.1Genomic Context describing neighboring genes Neighboring gene ciliary microtubule associated protein 2 Neighboring gene uncharacterized LOC120102944 Neighboring gene tetratricopeptide repeat domain 22 Neighboring gene tetratricopeptide repeat domain 4 Neighboring gene maestro heat-like repeat family member 7

    Genomic regions, transcripts, and products

    General gene information

    Markers

    Gene Ontology Provided by RGD

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables proline-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables proline-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    involved_in prolyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in prolyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
     
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in mitochondrion ISO
    Inferred from Sequence Orthology
    more info
    PubMed 

    General protein information

    Preferred Names
    probable proline--tRNA ligase, mitochondrial
    Names
    proRS
    probable prolyl-tRNA synthetase, mitochondrial
    proline--tRNA ligase
    prolyl-tRNA synthetase (mitochondrial)(putative)
    prolyl-tRNA synthetase 2, mitochondrial (putative)
    NP_001014086.2
    XP_006238574.1
    XP_006238575.1
    XP_017448872.1

    NCBI Reference Sequences (RefSeq)

    NEW Try the new Transcript table

    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_001014064.2NP_001014086.2  probable proline--tRNA ligase, mitochondrial precursor

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000005
      UniProtKB/TrEMBL
      A0A8I6A4Z4
      Related
      ENSRNOP00000109209.1, ENSRNOT00000146972.1
      Conserved Domains (2) summary
      cd00779
      Location:70359
      ProRS_core_prok; Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      cd00861
      Location:374475
      ProRS_anticodon_short; ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, ...

    RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

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

    Reference GRCr8

    Genomic

    1. NC_086023.1 Reference GRCr8

      Range
      126662882..126667981
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_006238513.5XP_006238575.1  probable proline--tRNA ligase, mitochondrial isoform X1

      See identical proteins and their annotated locations for XP_006238575.1

      UniProtKB/Swiss-Prot
      Q5M7W7
      UniProtKB/TrEMBL
      A6JYN5
      Conserved Domains (3) summary
      PRK09194
      Location:42470
      PRK09194; prolyl-tRNA synthetase; Provisional
      cd00779
      Location:65354
      ProRS_core_prok; Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      cd00861
      Location:369470
      ProRS_anticodon_short; ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, ...
    2. XM_006238512.4XP_006238574.1  probable proline--tRNA ligase, mitochondrial isoform X2

      UniProtKB/TrEMBL
      A0A8I6A4Z4
      Related
      ENSRNOP00000087000.1, ENSRNOT00000110417.2
      Conserved Domains (2) summary
      cd00779
      Location:70359
      ProRS_core_prok; Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      cd00861
      Location:374475
      ProRS_anticodon_short; ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, ...
    3. XM_017593383.3XP_017448872.1  probable proline--tRNA ligase, mitochondrial isoform X1

      UniProtKB/Swiss-Prot
      Q5M7W7
      UniProtKB/TrEMBL
      A6JYN5
      Conserved Domains (3) summary
      PRK09194
      Location:42470
      PRK09194; prolyl-tRNA synthetase; Provisional
      cd00779
      Location:65354
      ProRS_core_prok; Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      cd00861
      Location:369470
      ProRS_anticodon_short; ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, ...