UniProt Accession

 PNPT1_MOUSE; Q8K1R3; Q3UEP9; Q810U7; Q812B3; Q8R2U3; Q9DC52 

Genbank Protein ID

 AJ507387; AF465249; AK004563; AK149419; BX000351; BC027228; BC049283; BC055826 

Genbank Nucleotide ID

 CAD45436.1; AAO33354.1; BAB23374.1; BAE28862.1; CAI25081.1; AAH27228.2; AAH49283.1; AAH55826.1 

Protein Name

 Polyribonucleotide nucleotidyltransferase 1, mitochondrial 

Protein Synonyms/Alias

 3'-5' RNA exonuclease OLD35; PNPase old-35; Polynucleotide phosphorylase 1; PNPase 1; Polynucleotide phosphorylase-like protein 

Gene Name

 Pnpt1 

Gene Synonyms/Alias

 Pnpase 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
250	HAIKVGVKYTQQIIQ	acetylation	[1]
275	VAKRTPQKIFTPSAE	acetylation	[2]
285	TPSAEIVKYTKIIAM	acetylation	[1, 2, 3, 4, 5]
288	AEIVKYTKIIAMEKL	acetylation	[2, 6]
306	FTDYEHDKVSRDEAV	acetylation	[2, 6]
357	SIILNEYKRCDGRDL	ubiquitination	[7]
421	AINGVKDKNFMLHYE	acetylation	[2]
439	YATNETGKVTGVNRR	acetylation	[8]
439	YATNETGKVTGVNRR	succinylation	[8]
456	GHGALAEKALCPVIP	acetylation	[2, 6]
464	ALCPVIPKDFPFTIR	acetylation	[2, 6]
521	VTKTNPEKGEIEDYR	acetylation	[2, 6]
552	FKIAGTNKGITALQA	acetylation	[8]
552	FKIAGTNKGITALQA	succinylation	[8]
569	KLPGVPIKIIMEAIQ	acetylation	[4]
583	QQASVAKKEILQIMN	acetylation	[8]
583	QQASVAKKEILQIMN	succinylation	[8]
591	EILQIMNKTISKPRA	acetylation	[2]
595	IMNKTISKPRASRKE	acetylation	[2]

Reference

 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [7] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [8] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

Functional Description

 RNA-binding protein implicated in numerous RNA metabolic processes. Hydrolyzes 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. 

Sequence Annotation

 DOMAIN 605 664 KH.
 DOMAIN 679 750 S1 motif.
 MOD_RES 264 264 N6-acetyllysine (By similarity).
 MOD_RES 285 285 N6-acetyllysine (By similarity).  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Membrane; Mitochondrion; mRNA processing; Nuclease; Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase; Transit peptide; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 783 AA 

Protein Sequence

Gene Ontology

 GO:0045025; C:mitochondrial degradosome; ISS:UniProtKB.
 GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
 GO:0035198; F:miRNA binding; ISS:UniProtKB.
 GO:0034046; F:poly(G) RNA binding; ISS:UniProtKB.
 GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
 GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; ISS:UniProtKB.
 GO:0035458; P:cellular response to interferon-beta; IEA:Compara.
 GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
 GO:0000958; P:mitochondrial mRNA catabolic process; IMP:UniProtKB.
 GO:0097222; P:mitochondrial mRNA polyadenylation; ISS:UniProtKB.
 GO:0000965; P:mitochondrial RNA 3'-end processing; ISS:UniProtKB.
 GO:0000964; P:mitochondrial RNA 5'-end processing; ISS:UniProtKB.
 GO:0070584; P:mitochondrion morphogenesis; IMP:UniProtKB.
 GO:0071850; P:mitotic cell cycle arrest; ISS:UniProtKB.
 GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
 GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; ISS:UniProtKB.
 GO:2000627; P:positive regulation of miRNA catabolic process; ISS:UniProtKB.
 GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; ISS:UniProtKB.
 GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
 GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
 GO:0043457; P:regulation of cellular respiration; IMP:UniProtKB.
 GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
 GO:0035928; P:rRNA import into mitochondrion; ISS:UniProtKB. 

Interpro

 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. 

Pfam

 PF00013; KH_1
 PF03726; PNPase
 PF01138; RNase_PH
 PF03725; RNase_PH_C
 PF00575; S1 

SMART

 SM00322; KH
 SM00316; S1 

PROSITE

 PS50084; KH_TYPE_1
 PS50126; S1 

PRINTS