Q5SGE0 · LPPRC_RAT

  • Protein
    Leucine-rich PPR motif-containing protein, mitochondrial
  • Gene
    Lrpprc
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. Positively modulates nuclear export of mRNAs containing the EIF4E sensitivity element (4ESE) by binding simultaneously to both EIF4E and the 4ESE and acting as a platform for assembly for the RNA export complex (By similarity).
Also binds to exportin XPO1/CRM1 to engage the nuclear pore and traffic the bound mRNAs to the cytoplasm (By similarity).
May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity).
Required for maintaining mitochondrial potential (By similarity).
Suppresses the initiation of basal levels of autophagy and mitophagy by sustaining BCL2 levels (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcondensed nuclear chromosome
Cellular Componentcytoplasm
Cellular Componentcytoskeleton
Cellular Componentmicrotubule
Cellular Componentmitochondrial nucleoid
Cellular Componentmitochondrion
Cellular Componentnuclear inner membrane
Cellular Componentnuclear outer membrane
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentribonucleoprotein complex
Molecular Functionbeta-tubulin binding
Molecular FunctionmRNA 3'-UTR binding
Molecular FunctionRNA binding
Molecular Functionsingle-stranded DNA binding
Molecular Functionubiquitin protein ligase binding
Biological Processautophagy
Biological Processmitochondrial RNA catabolic process
Biological ProcessmRNA transport
Biological Processnegative regulation of mitochondrial RNA catabolic process
Biological Processregulation of mitochondrial translation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Leucine-rich PPR motif-containing protein, mitochondrial
  • Alternative names
    • 130 kDa leucine-rich protein (LRP 130)
    • Leucine rich protein 157 (rLRP157)

Gene names

    • Name
      Lrpprc
    • Synonyms
      Lrp157

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q5SGE0

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-77Mitochondrion
ChainPRO_000029554778-1392Leucine-rich PPR motif-containing protein, mitochondrial
Modified residue151N6-acetyllysine
Modified residue186N6-acetyllysine
Modified residue291N6-acetyllysine
Modified residue462N6-acetyllysine
Modified residue749N6-acetyllysine
Modified residue1025Phosphoserine
Modified residue1026Phosphoserine
Modified residue1028Phosphoserine
Modified residue1137Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed. Expressed in liver, brain and a subset of small diameter sensory neurons in the dorsal root ganglion (at protein level).

Induction

Induced by NGF in nociceptors.

Interaction

Subunit

Component of mRNP complexes associated with HNRPA1 (By similarity).
Component of the complex, at least composed of LRPPRC, BECN1 and BCL2; the interactions prevent BECN1 from forming an autophagy-inducing complex with PIK3C3 (By similarity).
Interacts with CECR2, HEBP2, MAP1S, UXT, PPARGC1A and FOXO1. Interacts (via N-terminus) with EIF4E; the interaction promotes association of EIF4E with 4ESE-containing mRNAs (By similarity).
Interacts with exportin XPO1/CRM1; interacts both alone and in complex with EIF4E and 4ESE-containing mRNAs to form an EIF4E-dependent mRNA export complex (By similarity).
Interacts with importin IPO8; the interaction occurs when LRPPRC is in its RNA-free form and returns LRPPRC to the nucleus for further export rounds (By similarity).
Interacts with BECN1 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat125-159PPR 1
Repeat160-194PPR 2
Repeat195-229PPR 3
Repeat230-264PPR 4
Repeat265-299PPR 5
Repeat300-334PPR 6
Repeat402-436PPR 7
Repeat437-471PPR 8
Repeat677-708PPR 9
Repeat709-745PPR 10
Repeat746-783PPR 11
Repeat784-820PPR 12
Repeat821-856PPR 13
Repeat953-987PPR 14
Repeat1030-1064PPR 15
Repeat1065-1101PPR 16
Repeat1102-1136PPR 17
Repeat1137-1173PPR 18
Repeat1174-1208PPR 19
Repeat1315-1349PPR 20

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,392
  • Mass (Da)
    156,653
  • Last updated
    2004-12-21 v1
  • Checksum
    80D6040F4671D097
MSALLRPARWLLGAAAVPRLPLSLRLPAGGPGRLPSVVRVAAAGGRPAAGELLSQARLYAIVAEKKDLPEEPAPVRRSGSQFDWALMRLDNSVRRTGRITKGLLQKVFESTCRSGSPGSNQALLLLRSCGSLLPELSLAERTEFAHKIWDKLQQLGTVYDVSHYNALLKVYLQNEYRFSPTDFLAKMEGANIQPNRVTYQRLIAAYCSVGDIEGASKILGFMKTRDLPITEAVFSALVTGHARAGDMESAENILTVMKQAGIEPGPDTYLALLNAHAEKGDIDHVKQILEKVEKSDHYFMDRDFLQIIVSFSKAGYPQYVSEILEKITYERRSIPDAMNLILLLVTEKLEDTAFQVLLALPLARDETSSSFGSFFLRHCVTMDTPAEKLIDYCKRLRDAKVHSSSLQFTLHCALQANKTALAKAVMEALRDEGFPIRTHYFWPLLVGHQKTKNVQGIIDILKIMKEMGVDPDQETYINYVFPCFGSVQSARAALQENKCLPKSTTFAQAEVRNEAINGNLQNILSFLESNALPFSFNSLRGSLILGFRRSMNIDLWSKITELLYKDDRYCQKPPGPTEAVGYFLYNLIDSMSDSEVQAKEERLRQYFHQLREMNVKVSENIYKGICNLLDNYHVPELIKDVKVLVDREKIDSRKTSQFTSSDLESTLEKLKAEGHPVGDPLKQLILLLCSEENMQKALEVKAKYESDMVIGGYAALINLCCRHDNAEDALNLKQEFDRLDPSAVLDTAKYVALVKVLGKHGRVQDAINILKEMKEKDVVIKDAAVLSFFHILNGAALRGEIETVKQLHEAIVTLGLAKPSSNISFPLVTVHLEKDDLPAALEASIACHEKYKVLPRIHDVLCKLIEKGETDLIQKAMDFVSQEQGEMSMLYDLFFAFLQTGNYKEAKKIIETPGIRARPTRLQWFCDRCIANNQVETLEKLVELTEKLFECDRDQMYYNLLKLYKISGDWQRADAVWNKMQEENLIPRERTLRLLAGILKTSNQEVPFDVPELWFGDDRSSLSSSSPSAGDTVTEKMLLSDCRLKKSKDAYNIFLKAEKQDVVFSSEAYSTLVGLLLSKDDFTRAMHVKDFAETHIKGFTLNGAASSLLIIAQVRRDYLKVALETLKAALDLEQVPSELAVTRLIQALALQGDVKSIETIQKMVKGLDAIELSRMVFINNIALAQMKNNEIDAAIENIEHMLASENQTVEHQYFGLSYLFRKVIEEQMEPALEKLSIMSERLANQFALYKPVTDLFLQLVDSGKVDEARALLERCGAIAEQTSILSVFCLRTSQKPKKAPVLKTLLELIPELRENDRVYSCSMKSYVADKDVASAKALYEHLTAKNMKLDDLFLKRYASLLKDVGEPVPFTEPPESFGFYIKQLKEARENPS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F1LM33F1LM33_RATLrpprc1398

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY293808
EMBL· GenBank· DDBJ
AAQ74626.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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