ID A0A3Q7RRL1_VULVU Unreviewed; 784 AA.
AC A0A3Q7RRL1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase 1, mitochondrial {ECO:0000256|ARBA:ARBA00072100};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
DE AltName: Full=Polynucleotide phosphorylase 1 {ECO:0000256|ARBA:ARBA00031451};
GN Name=PNPT1 {ECO:0000313|RefSeq:XP_025848462.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP001652641, ECO:0000313|RefSeq:XP_025848462.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025848462.1}
RP IDENTIFICATION.
RC TISSUE=Cell line {ECO:0000313|RefSeq:XP_025848462.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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:0000256|ARBA:ARBA00064869}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00060410};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00060410}.
CC Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR RefSeq; XP_025848462.1; XM_025992677.2.
DR AlphaFoldDB; A0A3Q7RRL1; -.
DR STRING; 9627.ENSVVUP00000013674; -.
DR GeneID; 112915264; -.
DR KEGG; vvp:112915264; -.
DR CTD; 87178; -.
DR OMA; RFMFHYN; -.
DR Proteomes; UP001652641; Chromosome 16.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0045025; C:mitochondrial degradosome; IEA:Ensembl.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR GO; GO:0034046; F:poly(G) binding; IEA:Ensembl.
DR GO; GO:0008266; F:poly(U) RNA binding; IEA:Ensembl.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0097222; P:mitochondrial mRNA polyadenylation; IEA:Ensembl.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IEA:Ensembl.
DR GO; GO:0000964; P:mitochondrial RNA 5'-end processing; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IEA:Ensembl.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; IEA:Ensembl.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; IEA:Ensembl.
DR GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
DR GO; GO:0043457; P:regulation of cellular respiration; IEA:Ensembl.
DR GO; GO:2000772; P:regulation of cellular senescence; IEA:Ensembl.
DR GO; GO:0035928; P:rRNA import into mitochondrion; IEA:Ensembl.
DR CDD; cd09033; KH-I_PNPT1; 1.
DR CDD; cd11363; RNase_PH_PNPase_1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR FunFam; 3.30.230.70:FF:000032; Polyribonucleotide nucleotidyltransferase 1; 1.
DR FunFam; 1.10.10.400:FF:000001; Polyribonucleotide nucleotidyltransferase 1, mitochondrial; 1.
DR FunFam; 2.40.50.140:FF:000113; polyribonucleotide nucleotidyltransferase 1, mitochondrial; 1.
DR FunFam; 3.30.1370.10:FF:000044; Polyribonucleotide nucleotidyltransferase 1, mitochondrial; 1.
DR FunFam; 3.30.230.70:FF:000008; polyribonucleotide nucleotidyltransferase 1, mitochondrial; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.10.400; Polyribonucleotide nucleotidyltransferase, RNA-binding domain; 1.
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_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR NCBIfam; NF008805; PRK11824.1; 1.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001652641};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 679..750
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 784 AA; 86022 MW; 4C5A2BCB3BB6E0B3 CRC64;
MAACRRCCSC LRLRPLREGP VRLPGRGRAL TQLQVRALWS GTGFRAVAVD LGSRKLEISS
GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV DYRQKAAAAG RIPTNYLRRE
VGSSDKEVLT SRVIDRSIRP LFPAGYFYDT QVLCNLLAVD GVNEPDVLAI NGASVALSLS
DIPWNGPIGA VRIGMIDGEC VVNPTRKEMS SSTLNLVVAG APKSQIVMME ASAENILQQD
FCHAIKVGVK YTQQIIQGIQ QLVKEIGVTK RTPQKLFTPS PEIVEHIHKL TMERLYAVFT
DYEHDKISRD EAINKIRLDT EEQLKEKFPE ADTYEIIESF NVVAKEVFRS IILNEYKRCD
GRDLTSLRNI NCEVDLFKTL HGSALFQRGQ TQVFCTVTFD SLESSIKSDR IVTAINGIKD
KNFMLHYEFP PYATNEIGKV TGVNRRELGH GALAEKALYP VIPKDFPFTI RVTSEVLESN
GSSSMASACG GSLALMDAGV PISSAVAGVA IGLVTKSNPD KGEIEDYRLL TDILGIEDYN
GDMDFKIAGT SKGITALQAD IKLPGIPIKI VMEAIQQASV AKREILQIMN KTISKPRASR
KENGPVVETI QVPLSKRAKF VGPGGYHLKK LQAETGVTVS QVDEETFSVF APTPSAMHEA
RDFITELCKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP NMTAVLLHNT QLDQRKIKHP
TALGLEVGQE IQVKYFGRDP ADGRMRLSRK VLQSPATTVV KTLNDRSSIV MGESISQSSS
NSTQ
//
