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Q5RCW2

- PNPT1_PONAB

UniProt

Q5RCW2 - PNPT1_PONAB

Protein

Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Gene

PNPT1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      Previous versions | rss
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    Functioni

    RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA By similarity.By similarity

    Catalytic activityi

    RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. miRNA binding Source: UniProtKB
    3. poly(G) binding Source: UniProtKB
    4. poly(U) RNA binding Source: UniProtKB
    5. polyribonucleotide nucleotidyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to oxidative stress Source: UniProtKB
    2. mitochondrial mRNA catabolic process Source: UniProtKB
    3. mitochondrial mRNA polyadenylation Source: UniProtKB
    4. mitochondrial RNA 3'-end processing Source: UniProtKB
    5. mitochondrial RNA 5'-end processing Source: UniProtKB
    6. mitochondrial RNA catabolic process Source: UniProtKB
    7. mitochondrion morphogenesis Source: UniProtKB
    8. mitotic cell cycle arrest Source: UniProtKB
    9. mRNA catabolic process Source: UniProtKB
    10. negative regulation of growth Source: UniProtKB
    11. nuclear polyadenylation-dependent mRNA catabolic process Source: UniProtKB
    12. positive regulation of miRNA catabolic process Source: UniProtKB
    13. positive regulation of mitochondrial RNA catabolic process Source: UniProtKB
    14. positive regulation of mRNA catabolic process Source: UniProtKB
    15. protein homooligomerization Source: UniProtKB
    16. protein homotrimerization Source: UniProtKB
    17. regulation of cellular respiration Source: UniProtKB
    18. regulation of cellular senescence Source: UniProtKB
    19. RNA catabolic process Source: UniProtKB
    20. RNA import into mitochondrion Source: UniProtKB
    21. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    22. RNA polyadenylation Source: UniProtKB
    23. rRNA import into mitochondrion Source: UniProtKB

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    mRNA processing, Transport

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC:2.7.7.8)
    Alternative name(s):
    Polynucleotide phosphorylase 1
    Short name:
    PNPase 1
    Gene namesi
    Name:PNPT1
    Synonyms:PNPASE
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion intermembrane space By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. membrane Source: UniProtKB-KW
    2. mitochondrial degradosome Source: UniProtKB
    3. mitochondrial intermembrane space Source: UniProtKB-SubCell
    4. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4646MitochondrionSequence AnalysisAdd
    BLAST
    Chaini47 – 783737Polyribonucleotide nucleotidyltransferase 1, mitochondrialPRO_0000024753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei250 – 2501N6-acetyllysineBy similarity
    Modified residuei264 – 2641N6-acetyllysineBy similarity
    Modified residuei285 – 2851N6-acetyllysineBy similarity
    Modified residuei289 – 2891N6-acetyllysineBy similarity
    Modified residuei552 – 5521N6-succinyllysineBy similarity
    Modified residuei782 – 7821PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ5RCW2.

    Interactioni

    Subunit structurei

    Homotrimer; in free form. Homooligomer. Component of the mitochondrial degradosome (mtEXO) complex which is a heteropentamer containing 2 copies of SUPV3L1 and 3 copies of PNPT1. Interacts with TCL1A; the interaction has no effect on PNPT1 exonuclease activity By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RCW2.
    SMRiQ5RCW2. Positions 273-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini605 – 66460KHPROSITE-ProRule annotationAdd
    BLAST
    Domaini679 – 75072S1 motifPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 KH domain.PROSITE-ProRule annotation
    Contains 1 S1 motif domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG053625.
    KOiK00962.

    Family and domain databases

    Gene3Di1.10.10.400. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1370.10. 1 hit.
    3.30.230.70. 2 hits.
    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    IPR012162. PNPase.
    IPR027408. PNPase/RNase_PH_dom.
    IPR015848. PNPase_PH_RNA-bd_bac/org-type.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view]
    PANTHERiPTHR11252. PTHR11252. 1 hit.
    PfamiPF00013. KH_1. 1 hit.
    PF03726. PNPase. 1 hit.
    PF01138. RNase_PH. 2 hits.
    PF03725. RNase_PH_C. 2 hits.
    PF00575. S1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005499. PNPase. 1 hit.
    SMARTiSM00322. KH. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF46915. SSF46915. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54211. SSF54211. 2 hits.
    SSF54791. SSF54791. 1 hit.
    SSF55666. SSF55666. 2 hits.
    TIGRFAMsiTIGR03591. polynuc_phos. 1 hit.
    PROSITEiPS50084. KH_TYPE_1. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5RCW2-1 [UniParc]FASTAAdd to Basket

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    MAACRYCCSC LRLRPLSDGP FCLPGRDRAL TQLLVRALWS STGSRAVAVD    50
    LGNRKLEISS GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV 100
    DYRQKAAAAG RIPTNYLRRE IGTSDKEILT SRIIDRSIRP LFPAGYFYDT 150
    QVLCNLLAVD GVNEPDVLAI NGASVALSLS DIPWNGPVGA VRIGIIDGEC 200
    VVNPTRKEMS SSTLNLVVAG APKSQIVMLE ASAENILQQD FCHAIKVGVK 250
    YTQQIIQGIQ QLVKETGVTK RTPQKLFTPS PEIVKHTHKL AMERLYAVFT 300
    DYEHDKVSRD EAVNKIRLDT EEQLKEKFPQ ADPYEIIESF NVVAKEVFRN 350
    IILNEYKRCD GRDLTSLRNV SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD 400
    SLESGIKSDQ VITAINGIKD KNFMLHYEFP PYATNEIGKV TGLNRRELGH 450
    GALAEKALYP VIPRDFPFTI RVTSEVLESN GSSSMASACG GSLALMDSGV 500
    PISSAVAGVA IGLVTKTDPE KGEIEDYRLL TDILGIEDYN GDMDFKIAGT 550
    NKGITALQAD IKLPGIPIKI VMEAIQQASV AKKEILQIMN KTISKPRTSR 600
    KENGPVVETV QVPLSKRAKF VGPGGYNLKK LQAETGVTIS QVDEETFSVF 650
    APTPSALHEA RDFITEICKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP 700
    NMTAVLLHNT QLDQRKIRHP TALGLEVGQE IQVKYFGRDP ADGRMRLSRK 750
    VLQSPATTVV RTLNDRSSIV MGEPISQSSS NSQ 783
    Length:783
    Mass (Da):85,851
    Last modified:May 10, 2005 - v2
    Checksum:iC9AE6896AC130CA8
    GO

    Sequence cautioni

    The sequence CAH90395.1 differs from that shown. Reason: Frameshift at position 75.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858156 mRNA. Translation: CAH90395.1. Frameshift.
    RefSeqiNP_001125193.1. NM_001131721.1.
    UniGeneiPab.14131.

    Genome annotation databases

    GeneIDi100172084.
    KEGGipon:100172084.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858156 mRNA. Translation: CAH90395.1 . Frameshift.
    RefSeqi NP_001125193.1. NM_001131721.1.
    UniGenei Pab.14131.

    3D structure databases

    ProteinModelPortali Q5RCW2.
    SMRi Q5RCW2. Positions 273-363.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5RCW2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100172084.
    KEGGi pon:100172084.

    Organism-specific databases

    CTDi 87178.

    Phylogenomic databases

    HOVERGENi HBG053625.
    KOi K00962.

    Family and domain databases

    Gene3Di 1.10.10.400. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1370.10. 1 hit.
    3.30.230.70. 2 hits.
    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012340. NA-bd_OB-fold.
    IPR012162. PNPase.
    IPR027408. PNPase/RNase_PH_dom.
    IPR015848. PNPase_PH_RNA-bd_bac/org-type.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR022967. RNA-binding_domain_S1.
    [Graphical view ]
    PANTHERi PTHR11252. PTHR11252. 1 hit.
    Pfami PF00013. KH_1. 1 hit.
    PF03726. PNPase. 1 hit.
    PF01138. RNase_PH. 2 hits.
    PF03725. RNase_PH_C. 2 hits.
    PF00575. S1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005499. PNPase. 1 hit.
    SMARTi SM00322. KH. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46915. SSF46915. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54211. SSF54211. 2 hits.
    SSF54791. SSF54791. 1 hit.
    SSF55666. SSF55666. 2 hits.
    TIGRFAMsi TIGR03591. polynuc_phos. 1 hit.
    PROSITEi PS50084. KH_TYPE_1. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiPNPT1_PONAB
    AccessioniPrimary (citable) accession number: Q5RCW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 65 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3