ID A0A8C7AET7_NEOVI Unreviewed; 745 AA.
AC A0A8C7AET7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
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|Ensembl:ENSNVIP00000004513.1};
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Neogale.
OX NCBI_TaxID=452646 {ECO:0000313|Ensembl:ENSNVIP00000004513.1, ECO:0000313|Proteomes:UP000694425};
RN [1] {ECO:0000313|Ensembl:ENSNVIP00000004513.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSNVIP00000004513.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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 AlphaFoldDB; A0A8C7AET7; -.
DR Ensembl; ENSNVIT00000005316.1; ENSNVIP00000004513.1; ENSNVIG00000003555.1.
DR GeneTree; ENSGT00390000014001; -.
DR Proteomes; UP000694425; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:TreeGrafter.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IEA:TreeGrafter.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IEA:TreeGrafter.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd09033; KH-I_PNPT1; 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 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; 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; 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; 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:UP000694425};
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 641..712
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 745 AA; 82195 MW; 32F5B05AC8FF911F CRC64;
MAACRHCCSC LRLRPLCDGP PRLPGRDRTL TQLQVRTLWG GARFRAVAVD LGSRKLEISS
GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV DYRQKAAAAG RIPTNYLRRE
IGSSDKEILT SRVIDRSIRP LFPAGYFYDT QVLCNLLAVD GVNEPDILAI NGASVALSLS
DIPWNGPIVM MEASAENILQ QDFCHAIKVG VKYTQQIIQG IQQLVKEIGV TKRTPQKLFT
PSPEIVEYIH KLSMERLYAV FTDYEHDKIS RDEAVNKIRL DTEEQLKEKF PEADTFEIIE
SFNVVAKEVF RSIILNEYKR CDGRDLTSLR NISCEVDMFK TLHGSALFQR GQTQVLCTVT
FDSLESSMKS DRIITAINGI KDKNFMLHYE FPPYATNEIG KVTGVNRREL GHGALAEKAL
YPVIPKDFPF TIRVTSEVLE SNGSSSMASA CCGSLALMDA GVPISSAVAG VAIGLVTKNN
REKGEIEDYR LLTDILGIED YNGDMDFKIA GTNKGITALQ ADIKLPGIPI KIVMEAIQQA
SVAKKEILQI MNKTISKPRA SRKENGPVVE TIQVPLSKRA KFVGPGGYHL KKLQAETGVT
VSQVDEETFS VFAPTPSAMH EARDFITEIC KDDQEQQLEF GAVYTATITE IRDTGVMVKL
YPNMTAVLLH NTQLDQRKIK HPTALGLEVG QEIQVKYFGR DPADGRMRLS RKVLQSPATS
VVKTLNDRSS IVMGESISQS SSNST
//
