PNPT1_PONAB
ID PNPT1_PONAB Reviewed; 783 AA.
AC Q5RCW2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase 1, mitochondrial;
DE EC=2.7.7.8;
DE AltName: Full=Polynucleotide phosphorylase 1;
DE Short=PNPase 1;
DE Flags: Precursor;
GN Name=PNPT1; Synonyms=PNPASE;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein implicated in numerous RNA metabolic
CC processes. Catalyzes the phosphorolysis of single-stranded
CC polyribonucleotides processively in the 3'-to-5' direction.
CC Mitochondrial intermembrane factor with RNA-processing exoribonulease
CC activity. Component of the mitochondrial degradosome (mtEXO) complex,
CC that degrades 3' overhang double-stranded RNA with a 3'-to-5'
CC directionality in an ATP-dependent manner. Involved in the degradation
CC of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like
CC molecules (By similarity). Required for correct processing and
CC polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic
CC RNA import factor that mediates the translocation of small RNA
CC components like the 5S RNA, the RNA subunit of ribonuclease P and the
CC mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix.
CC Plays a role in mitochondrial morphogenesis and respiration; regulates
CC the expression of the electron transport chain (ETC) components at the
CC mRNA and protein levels. In the cytoplasm, shows a 3'-to-5'
CC exoribonuclease mediating mRNA degradation activity; degrades c-myc
CC mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest
CC in melanoma cells. Regulates the stability of specific mature miRNAs in
CC melanoma cells; specifically and selectively degrades miR-221,
CC preferentially. Also plays a role in RNA cell surveillance by cleaning
CC up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA
CC and miR-221 microRNA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8TCS8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC EC=2.7.7.8;
CC -!- SUBUNIT: Homotrimer; in free form. Homooligomer. Component of the
CC mitochondrial degradosome (mtEXO) complex which is a heteropentamer
CC containing 2 copies of SUPV3L1 and 3 copies of PNPT1. As part of the
CC mitochondrial degradosome complex, interacts with GRSF1 in an RNA-
CC dependent manner; the interaction enhances the activity of the complex.
CC Interacts with TCL1A; the interaction has no effect on PNPT1
CC exonuclease activity. {ECO:0000250|UniProtKB:Q8TCS8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TCS8}.
CC Mitochondrion matrix {ECO:0000250|UniProtKB:Q8TCS8}. Mitochondrion
CC intermembrane space {ECO:0000250|UniProtKB:Q8TCS8}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q8TCS8}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH90395.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858156; CAH90395.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001125193.1; NM_001131721.1.
DR RefSeq; XP_009235565.1; XM_009237290.1.
DR AlphaFoldDB; Q5RCW2; -.
DR SMR; Q5RCW2; -.
DR STRING; 9601.ENSPPYP00000013832; -.
DR PRIDE; Q5RCW2; -.
DR GeneID; 100172084; -.
DR KEGG; pon:100172084; -.
DR CTD; 87178; -.
DR eggNOG; KOG1067; Eukaryota.
DR InParanoid; Q5RCW2; -.
DR OrthoDB; 236073at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045025; C:mitochondrial degradosome; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0097222; P:mitochondrial mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0000964; P:mitochondrial RNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0043457; P:regulation of cellular respiration; ISS:UniProtKB.
DR GO; GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0035927; P:RNA import into mitochondrion; ISS:UniProtKB.
DR GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0035928; P:rRNA import into mitochondrion; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.30.230.70; -; 2.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR11252; PTHR11252; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 1.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF46915; SSF46915; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Exonuclease; Hydrolase; Membrane; Mitochondrion;
KW mRNA processing; Nuclease; Nucleotidyltransferase; Phosphoprotein;
KW Reference proteome; RNA-binding; Transferase; Transit peptide; Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..783
FT /note="Polyribonucleotide nucleotidyltransferase 1,
FT mitochondrial"
FT /id="PRO_0000024753"
FT DOMAIN 605..664
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 679..750
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1R3"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
FT MOD_RES 285
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
FT MOD_RES 289
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
FT MOD_RES 552
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1R3"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
SQ SEQUENCE 783 AA; 85851 MW; C9AE6896AC130CA8 CRC64;
MAACRYCCSC LRLRPLSDGP FCLPGRDRAL TQLLVRALWS STGSRAVAVD LGNRKLEISS
GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV DYRQKAAAAG RIPTNYLRRE
IGTSDKEILT SRIIDRSIRP LFPAGYFYDT QVLCNLLAVD GVNEPDVLAI NGASVALSLS
DIPWNGPVGA VRIGIIDGEC VVNPTRKEMS SSTLNLVVAG APKSQIVMLE ASAENILQQD
FCHAIKVGVK YTQQIIQGIQ QLVKETGVTK RTPQKLFTPS PEIVKHTHKL AMERLYAVFT
DYEHDKVSRD EAVNKIRLDT EEQLKEKFPQ ADPYEIIESF NVVAKEVFRN IILNEYKRCD
GRDLTSLRNV SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD SLESGIKSDQ VITAINGIKD
KNFMLHYEFP PYATNEIGKV TGLNRRELGH GALAEKALYP VIPRDFPFTI RVTSEVLESN
GSSSMASACG GSLALMDSGV PISSAVAGVA IGLVTKTDPE KGEIEDYRLL TDILGIEDYN
GDMDFKIAGT NKGITALQAD IKLPGIPIKI VMEAIQQASV AKKEILQIMN KTISKPRTSR
KENGPVVETV QVPLSKRAKF VGPGGYNLKK LQAETGVTIS QVDEETFSVF APTPSALHEA
RDFITEICKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP NMTAVLLHNT QLDQRKIRHP
TALGLEVGQE IQVKYFGRDP ADGRMRLSRK VLQSPATTVV RTLNDRSSIV MGEPISQSSS
NSQ
